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class="vector-toc-numb">3.1</span> <span>Factors affecting oxygen affinity</span> </div> </a> <ul id="toc-Factors_affecting_oxygen_affinity-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Even_higher_oxygen_affinity_–_hemoglobin_Barts_(four_γ_subunits)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Even_higher_oxygen_affinity_–_hemoglobin_Barts_(four_γ_subunits)"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.2</span> <span>Even higher oxygen affinity – hemoglobin Barts (four γ subunits)</span> </div> </a> <ul id="toc-Even_higher_oxygen_affinity_–_hemoglobin_Barts_(four_γ_subunits)-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Quantification_of_oxygen_binding" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Quantification_of_oxygen_binding"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.3</span> <span>Quantification of oxygen binding</span> </div> </a> <ul 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<div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>Conditions with high hemoglobin F</span> </div> </a> <button aria-controls="toc-Conditions_with_high_hemoglobin_F-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Conditions with high hemoglobin F subsection</span> </button> <ul id="toc-Conditions_with_high_hemoglobin_F-sublist" class="vector-toc-list"> <li id="toc-During_pregnancy" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#During_pregnancy"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.1</span> <span>During pregnancy</span> </div> </a> <ul id="toc-During_pregnancy-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Hereditary_persistence_of_fetal_hemoglobin_(HPFH)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Hereditary_persistence_of_fetal_hemoglobin_(HPFH)"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.2</span> <span>Hereditary persistence of fetal hemoglobin (HPFH)</span> </div> </a> <ul id="toc-Hereditary_persistence_of_fetal_hemoglobin_(HPFH)-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Delta_beta-thalassemia" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Delta_beta-thalassemia"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.3</span> <span>Delta beta-thalassemia</span> </div> </a> <ul id="toc-Delta_beta-thalassemia-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Clinical_significance" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Clinical_significance"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>Clinical significance</span> </div> </a> <button 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cancers</span> </div> </a> <ul id="toc-Hemoglobin_F_as_a_marker_for_cancers-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>External links</span> </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" 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class="firstHeading mw-first-heading"><span class="mw-page-title-main">Fetal hemoglobin</span></h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 15 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-15" aria-hidden="true" ><span class="vector-icon mw-ui-icon-language-progressive mw-ui-icon-wikimedia-language-progressive"></span> <span class="vector-dropdown-label-text">15 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D9%87%D9%8A%D9%85%D9%88%D8%BA%D9%84%D9%88%D8%A8%D9%8A%D9%86_%D8%AC%D9%86%D9%8A%D9%86%D9%8A" title="هيموغلوبين جنيني – Arabic" lang="ar" hreflang="ar" data-title="هيموغلوبين جنيني" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Fetusni_hemoglobin" title="Fetusni hemoglobin – Bosnian" lang="bs" hreflang="bs" data-title="Fetusni hemoglobin" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target"><span>Bosanski</span></a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Hemoglobina_fetal" title="Hemoglobina fetal – Catalan" lang="ca" hreflang="ca" data-title="Hemoglobina fetal" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Hemoglobina_fetal" title="Hemoglobina fetal – Spanish" lang="es" hreflang="es" data-title="Hemoglobina fetal" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/H%C3%A9moglobine_f%C5%93tale" title="Hémoglobine fœtale – French" lang="fr" hreflang="fr" data-title="Hémoglobine fœtale" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/Hemoglobina_fetal" title="Hemoglobina fetal – Galician" lang="gl" hreflang="gl" data-title="Hemoglobina fetal" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target"><span>Galego</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Emoglobina_fetale" title="Emoglobina fetale – Italian" lang="it" hreflang="it" data-title="Emoglobina fetale" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-ms mw-list-item"><a href="https://ms.wikipedia.org/wiki/Hemoglobin_janin" title="Hemoglobin janin – Malay" lang="ms" hreflang="ms" data-title="Hemoglobin janin" data-language-autonym="Bahasa Melayu" data-language-local-name="Malay" class="interlanguage-link-target"><span>Bahasa Melayu</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Foetaal_hemoglobine" title="Foetaal hemoglobine – Dutch" lang="nl" hreflang="nl" data-title="Foetaal hemoglobine" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target"><span>Nederlands</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Hemoglobina_p%C5%82odowa" title="Hemoglobina płodowa – Polish" lang="pl" hreflang="pl" data-title="Hemoglobina płodowa" data-language-autonym="Polski" data-language-local-name="Polish" class="interlanguage-link-target"><span>Polski</span></a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%93%D0%B5%D0%BC%D0%BE%D0%B3%D0%BB%D0%BE%D0%B1%D0%B8%D0%BD_F" title="Гемоглобин F – Russian" lang="ru" hreflang="ru" data-title="Гемоглобин F" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Fetalni_hemoglobin" title="Fetalni hemoglobin – Serbian" lang="sr" hreflang="sr" data-title="Fetalni hemoglobin" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target"><span>Српски / srpski</span></a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Fetalni_hemoglobin" title="Fetalni hemoglobin – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Fetalni hemoglobin" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li><li class="interlanguage-link interwiki-th mw-list-item"><a href="https://th.wikipedia.org/wiki/%E0%B8%AE%E0%B8%B5%E0%B9%82%E0%B8%A1%E0%B9%82%E0%B8%81%E0%B8%A5%E0%B8%9A%E0%B8%B4%E0%B8%99_%E0%B9%80%E0%B8%AD%E0%B8%9F" title="ฮีโมโกลบิน เอฟ – Thai" lang="th" hreflang="th" data-title="ฮีโมโกลบิน เอฟ" data-language-autonym="ไทย" data-language-local-name="Thai" class="interlanguage-link-target"><span>ไทย</span></a></li><li class="interlanguage-link interwiki-uk mw-list-item"><a href="https://uk.wikipedia.org/wiki/%D0%93%D0%B5%D0%BC%D0%BE%D0%B3%D0%BB%D0%BE%D0%B1%D1%96%D0%BD_F" title="Гемоглобін F – Ukrainian" lang="uk" hreflang="uk" data-title="Гемоглобін F" data-language-autonym="Українська" data-language-local-name="Ukrainian" 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id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Oxygen carrier protein in the human fetus</div> <style data-mw-deduplicate="TemplateStyles:r1257001546">.mw-parser-output .infobox-subbox{padding:0;border:none;margin:-3px;width:auto;min-width:100%;font-size:100%;clear:none;float:none;background-color:transparent}.mw-parser-output .infobox-3cols-child{margin:auto}.mw-parser-output .infobox .navbar{font-size:100%}@media screen{html.skin-theme-clientpref-night .mw-parser-output .infobox-full-data:not(.notheme)>div:not(.notheme)[style]{background:#1f1f23!important;color:#f8f9fa}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .infobox-full-data:not(.notheme) div:not(.notheme){background:#1f1f23!important;color:#f8f9fa}}@media(min-width:640px){body.skin--responsive .mw-parser-output .infobox-table{display:table!important}body.skin--responsive .mw-parser-output .infobox-table>caption{display:table-caption!important}body.skin--responsive .mw-parser-output .infobox-table>tbody{display:table-row-group}body.skin--responsive .mw-parser-output .infobox-table tr{display:table-row!important}body.skin--responsive .mw-parser-output .infobox-table th,body.skin--responsive .mw-parser-output .infobox-table td{padding-left:inherit;padding-right:inherit}}</style><table class="infobox"><tbody><tr><th colspan="2" class="infobox-above">Fetal hemoglobin</th></tr><tr><td colspan="2" class="infobox-subheader">(4 subunits, α<sub>2</sub>γ<sub>2</sub>)</td></tr><tr><td colspan="2" class="infobox-image"><span class="mw-default-size" typeof="mw:File/Frameless"><a href="/wiki/File:Structure_of_Fetal_Hemoglobin_(HbF).png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/7/77/Structure_of_Fetal_Hemoglobin_%28HbF%29.png/220px-Structure_of_Fetal_Hemoglobin_%28HbF%29.png" decoding="async" width="220" height="179" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/7/77/Structure_of_Fetal_Hemoglobin_%28HbF%29.png/330px-Structure_of_Fetal_Hemoglobin_%28HbF%29.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/7/77/Structure_of_Fetal_Hemoglobin_%28HbF%29.png/440px-Structure_of_Fetal_Hemoglobin_%28HbF%29.png 2x" data-file-width="664" data-file-height="541" /></a></span><div class="infobox-caption">Structure of fetal hemoglobin (HbF). The <b>2α</b> and <b>2γ</b> subunits are in red and yellow, respectively, and the iron-containing <a href="/wiki/Heme" title="Heme">heme</a> groups in green. From <span class="plainlinks"><a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a>: <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/4MQJ">4MQJ</a></span>, by authors Soman, J. and Olson J.S.</div></td></tr><tr><th scope="row" class="infobox-label">Protein type</th><td class="infobox-data"><a href="/wiki/Metalloprotein" title="Metalloprotein">metalloprotein</a>, <a href="/wiki/Globulin" title="Globulin">globulin</a></td></tr><tr><th scope="row" class="infobox-label">Function</th><td class="infobox-data"><a href="/wiki/Oxygen" title="Oxygen">oxygen</a>-transport</td></tr><tr><th scope="row" class="infobox-label">Cofactor(s)</th><td class="infobox-data"><a href="/wiki/Heme" title="Heme">heme</a> (4)</td></tr><tr><td colspan="2" class="infobox-below"> <table width="100%"> <tbody><tr style="background-color: #ccf; font-weight: bold;"> <th>Subunit name</th> <th>Gene</th> <th>Chromosomal locus </th></tr> <tr> <td>Hb-α1</td> <td><a href="/wiki/HBA1" class="mw-redirect" title="HBA1">HBA1</a></td> <td><a href="/wiki/Chromosome_16" title="Chromosome 16">Chr. 16</a> <a rel="nofollow" class="external text" href="https://ghr.nlm.nih.gov/gene/HBA1#location?chromosome=16p13.3">p13.3</a> </td></tr> <tr> <td>Hb-α2</td> <td><a href="/wiki/HBA2" class="mw-redirect" title="HBA2">HBA2</a></td> <td><a href="/wiki/Chromosome_16" title="Chromosome 16">Chr. 16</a> <a rel="nofollow" class="external text" href="https://ghr.nlm.nih.gov/gene/HBA2#location?chromosome=16p13.3">p13.3</a> </td></tr> <tr> <td>Hb-γ1</td> <td><a href="/wiki/HBG1" title="HBG1">HBG1</a></td> <td><a href="/wiki/Chromosome_11" title="Chromosome 11">Chr. 11</a> <a rel="nofollow" class="external text" href="https://ghr.nlm.nih.gov/gene/HBG1#location?chromosome=11p15.4">p15.4</a> </td></tr> <tr> <td>Hb-γ2</td> <td><a href="/wiki/HBG2" title="HBG2">HBG2</a></td> <td><a href="/wiki/Chromosome_11" title="Chromosome 11">Chr. 11</a> <a rel="nofollow" class="external text" href="https://ghr.nlm.nih.gov/gene/HBG2#location?chromosome=11p15.4">p15.4</a> </td></tr></tbody></table></td></tr></tbody></table> <p><b>Fetal hemoglobin</b>, or <b>foetal haemoglobin</b> (also <b>hemoglobin F</b>, <b>HbF</b>, or <b>α<sub>2</sub>γ<sub>2</sub></b>) is the main <a href="/wiki/Oxygen" title="Oxygen">oxygen</a> <a href="/wiki/Transport_protein" title="Transport protein">carrier protein</a> in the human <a href="/wiki/Fetus" title="Fetus">fetus</a>. Hemoglobin<span class="nowrap"> </span>F is found in fetal <a href="/wiki/Red_blood_cell" title="Red blood cell">red blood cells</a>, and is involved in transporting oxygen from the mother's <a href="/wiki/Bloodstream" class="mw-redirect" title="Bloodstream">bloodstream</a> to organs and tissues in the fetus. It is produced at around 6<span class="nowrap"> </span>weeks of pregnancy <sup id="cite_ref-David_1998_1-0" class="reference"><a href="#cite_note-David_1998-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> and the levels remain high after birth until the baby is roughly 2–4<span class="nowrap"> </span>months old.<sup id="cite_ref-Schechter2008_2-0" class="reference"><a href="#cite_note-Schechter2008-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Hemoglobin<span class="nowrap"> </span>F has a different composition than adult forms of <a href="/wiki/Hemoglobin" title="Hemoglobin">hemoglobin</a>, allowing it to bind (or attach to) oxygen more strongly; this in turn enables the developing fetus to retrieve oxygen from the mother's bloodstream, which occurs through the <a href="/wiki/Placenta" title="Placenta">placenta</a> found in the mother's <a href="/wiki/Uterus" title="Uterus">uterus</a>.<sup id="cite_ref-Wang_Y_&_Zhao_S_3-0" class="reference"><a href="#cite_note-Wang_Y_&_Zhao_S-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> </p><p>In the newborn, levels of hemoglobin F gradually decrease and reach adult levels (less than 1% of total hemoglobin) usually within the first year, as adult forms of hemoglobin begin to be produced.<sup id="cite_ref-Barbara2017_4-0" class="reference"><a href="#cite_note-Barbara2017-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Diseases such as <a href="/wiki/Beta_thalassemia" title="Beta thalassemia">beta thalassemias</a>, which affect components of the <a href="/wiki/Hemoglobin_A" title="Hemoglobin A">adult hemoglobin</a>, can delay this process, and cause hemoglobin F levels to be higher than normal.<sup id="cite_ref-Orapan2016_5-0" class="reference"><a href="#cite_note-Orapan2016-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> In <a href="/wiki/Sickle_cell_anemia" class="mw-redirect" title="Sickle cell anemia">sickle cell anemia</a>, increasing the production of hemoglobin F has been used as a treatment to relieve some of the symptoms.<sup id="cite_ref-pmid18458272_6-0" class="reference"><a href="#cite_note-pmid18458272-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Structure_and_genetics">Structure and genetics</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=1" title="Edit section: Structure and genetics"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Hemoglobin F, like adult hemoglobin (<a href="/wiki/Hemoglobin_A" title="Hemoglobin A">hemoglobin A</a> and <a href="/wiki/Hemoglobin_A2" title="Hemoglobin A2">hemoglobin A2</a>), has four <a href="/wiki/Protein_subunit" title="Protein subunit">subunits</a> or chains. Each subunit contains a <a href="/wiki/Heme" title="Heme">heme</a> group with an iron element which is key in allowing the binding and unbinding of oxygen. As such, hemoglobin F can adopt two states: <a href="/wiki/Hemoglobin#Oxyhemoglobin" title="Hemoglobin">oxyhemoglobin</a> (bound to oxygen) and <a href="/wiki/Hemoglobin#Deoxygenated_hemoglobin" title="Hemoglobin">deoxyhemoglobin</a> (without oxygen). As hemoglobin F has 4 heme groups, it can bind to up to four oxygen molecules.<sup id="cite_ref-brsphys_7-0" class="reference"><a href="#cite_note-brsphys-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> It is composed of <b>two α (alpha)</b> subunits and <b>two γ (gamma)</b> subunits, whereas hemoglobin A (97% of total hemoglobin in adults) is composed of two α and two β (beta) subunits. </p><p>In humans, the α subunit is encoded on <a href="/wiki/Chromosome_16_(human)" class="mw-redirect" title="Chromosome 16 (human)">chromosome 16</a> and the γ subunit is encoded on <a href="/wiki/Chromosome_11_(human)" class="mw-redirect" title="Chromosome 11 (human)">chromosome 11</a>. There are two very similar <a href="/wiki/Gene" title="Gene">genes</a> that code for the α subunit, <i><a href="/wiki/HBA1" class="mw-redirect" title="HBA1">HBA1</a></i> and <i><a href="/wiki/HBA2" class="mw-redirect" title="HBA2">HBA2</a></i>. The protein that they produce is identical, but they differ in gene regulatory regions that determine when or how much of the protein is produced. This leads to HBA1 and HBA2 contributing 40% and 60%, respectively, of the total α subunits produced. As a consequence, mutations on the <i>HBA2</i> gene are expected to have a stronger effect than mutations on the <i>HBA1</i> gene.<sup id="cite_ref-Samaneh2018_8-0" class="reference"><a href="#cite_note-Samaneh2018-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> There are also two similar copies of the gene coding for the γ subunit, <i>HBG1</i> and <i>HBG2</i>, but the protein produced is slightly different, just in one <a href="/wiki/Amino_acid" title="Amino acid">protein unit</a>: <i>HBG1</i> codes for the protein form with an <a href="/wiki/Alanine" title="Alanine">alanine</a> at position 136, whereas <i>HBG2</i> codes for a <a href="/wiki/Glycine" title="Glycine">glycine</a><sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> BCL11A and ZBTB7A are major repressor proteins of hemoglobin F production, by binding to the gene coding for the γ subunit at their promoter region.<sup id="cite_ref-Martyn2018_10-0" class="reference"><a href="#cite_note-Martyn2018-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> This happens naturally as the newborn baby starts to switch from producing hemoglobin F to producing hemoglobin A. Some genetic diseases can take place due to mutations to genes coding for components of hemoglobin F. Mutations to <i>HBA1</i> and <i>HBA2</i> genes can cause <a href="/wiki/Alpha-thalassemia" title="Alpha-thalassemia">alpha-thalassemia</a><sup id="cite_ref-Zeynep2015_11-0" class="reference"><a href="#cite_note-Zeynep2015-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> and mutations to the promoter regions of <i>HBG1</i> and <i>HBG2</i> can cause hemoglobin F to still be produced after the switch to hemoglobin A should have occurred, which is called <a href="/wiki/Hereditary_persistence_of_fetal_hemoglobin" title="Hereditary persistence of fetal hemoglobin">hereditary persistence of fetal hemoglobin</a>.<sup id="cite_ref-Martyn2018_10-1" class="reference"><a href="#cite_note-Martyn2018-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Production">Production</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=2" title="Edit section: Production"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Postnatal_genetics_en.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/8/87/Postnatal_genetics_en.svg/330px-Postnatal_genetics_en.svg.png" decoding="async" width="330" height="252" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/8/87/Postnatal_genetics_en.svg/495px-Postnatal_genetics_en.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/8/87/Postnatal_genetics_en.svg/660px-Postnatal_genetics_en.svg.png 2x" data-file-width="800" data-file-height="610" /></a><figcaption><a href="/wiki/Gene_expression" title="Gene expression">Gene expression</a> of hemoglobin before and after birth, also showing the cells types and organs where different subunits are being produced over time (data on <i>Wood W.G.</i>, (1976). <b>Br. Med. Bull. 32, 282.</b>) Figure last adapted by user Leonid 2.</figcaption></figure> <p>During the first 3 months of pregnancy, the main form of hemoglobin in the embryo/fetus is <a href="/wiki/Embryonic_hemoglobin" title="Embryonic hemoglobin">embryonic hemoglobin</a>, which has 3 variants depending on the types of subunits it contains. The production of hemoglobin F starts from week 6, but it's only from 3 months onwards that it becomes the main type found in fetal red blood cells.<sup id="cite_ref-Barbara2017_4-1" class="reference"><a href="#cite_note-Barbara2017-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> The switch to produce adult forms of hemoglobin (essentially hemoglobin A) starts at around 40 weeks of gestation, which is close to the expected time of birth.<sup id="cite_ref-David_1998_1-1" class="reference"><a href="#cite_note-David_1998-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> At birth, hemoglobin F accounts for 50-95% of the infant's hemoglobin and at around 6 months after birth, hemoglobin A becomes the predominant type. By the time the baby is one year old, the proportions of different types of hemoglobin are expected to approximate the adult levels, with hemoglobin F reduced to very low levels.<sup id="cite_ref-Barbara2017_4-2" class="reference"><a href="#cite_note-Barbara2017-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> The small proportion of red blood cells containing hemoglobin F are called F-cells, which also contain other types of hemoglobin. </p><p>In healthy adults, the composition of hemoglobin is hemoglobin A (~97%), hemoglobin A2 (2.2 - 3.5%) and hemoglobin F (<1%).<sup id="cite_ref-Caroline_2012_12-0" class="reference"><a href="#cite_note-Caroline_2012-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p><p>Certain genetic abnormalities can cause the switch to adult hemoglobin synthesis to fail, resulting in a condition known as <a href="/wiki/Hereditary_persistence_of_fetal_hemoglobin" title="Hereditary persistence of fetal hemoglobin">hereditary persistence of fetal hemoglobin</a>. </p> <div class="mw-heading mw-heading2"><h2 id="Binding_to_oxygen">Binding to oxygen</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=3" title="Edit section: Binding to oxygen"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:HbA_vs_HbF_saturation_curve.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/f/fb/HbA_vs_HbF_saturation_curve.png/220px-HbA_vs_HbF_saturation_curve.png" decoding="async" width="220" height="186" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/f/fb/HbA_vs_HbF_saturation_curve.png/330px-HbA_vs_HbF_saturation_curve.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/f/fb/HbA_vs_HbF_saturation_curve.png/440px-HbA_vs_HbF_saturation_curve.png 2x" data-file-width="639" data-file-height="541" /></a><figcaption>Oxygen-hemoglobin dissociation curves in fetus and adult</figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Factors_affecting_oxygen_affinity">Factors affecting oxygen affinity</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=4" title="Edit section: Factors affecting oxygen affinity"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The four hemes, which are the oxygen-binding parts of hemoglobin, are similar between hemoglobin F and other types of hemoglobin, including hemoglobin A. Thus, the key feature that allows hemoglobin F to bind more strongly to oxygen is by having γ subunits (instead of β, for example). In fact, some naturally existing molecules in our body can bind to hemoglobin and change its binding affinity for oxygen. One of the molecules is <a href="/wiki/2,3-bisphosphoglycerate" class="mw-redirect" title="2,3-bisphosphoglycerate">2,3-bisphosphoglycerate (2,3-BPG)</a> and it enhances hemoglobin's ability to release oxygen.<sup id="cite_ref-Gerald_2018_13-0" class="reference"><a href="#cite_note-Gerald_2018-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> 2,3-BPG interacts much more with hemoglobin A than hemoglobin F. This is because the adult β subunit has more positive charges than the fetal γ subunit, which attract the negative charges from 2,3-BPG. Due to the preference of 2,3-BPG for hemoglobin A, hemoglobin F binds to oxygen with more affinity, in average.<sup id="cite_ref-Duane_2016_14-0" class="reference"><a href="#cite_note-Duane_2016-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Even_higher_oxygen_affinity_–_hemoglobin_Barts_(four_γ_subunits)"><span id="Even_higher_oxygen_affinity_.E2.80.93_hemoglobin_Barts_.28four_.CE.B3_subunits.29"></span>Even higher oxygen affinity – hemoglobin Barts (four γ subunits)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=5" title="Edit section: Even higher oxygen affinity – hemoglobin Barts (four γ subunits)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Hemoglobin_Barts" title="Hemoglobin Barts">Hemoglobin Barts</a> is an abnormal form of hemoglobin produced in hemoglobin Barts syndrome or alpha-thalassemia major, the most severe form of <a href="/wiki/Alpha-thalassemia" title="Alpha-thalassemia">alpha-thalassemia</a>. Alpha-thalassemia is a genetic blood disorder and one of the most common hemoglobin-related diseases, affecting the production of α subunits from hemoglobin.<sup id="cite_ref-Renzo2011_15-0" class="reference"><a href="#cite_note-Renzo2011-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> Depending on how many genes coding for the α subunit are impacted (between one and four), patients with this disease can have reduced to no production of the α subunit of the hemoglobin. As a consequence, less hemoglobin is available and this affects oxygen supply to the tissues. Hemoglobin Barts syndrome manifests when all four genes coding for α subunit are deleted. This is often fatal for the fetus carrying the disorder, as in the absence of α subunits, a form of hemoglobin with four γ subunits, hemoglobin Barts, is produced. This form of hemoglobin isn't fit for oxygen exchange precisely due to its very high affinity for oxygen. While hemoglobin Barts is very efficient at binding oxygen, it doesn't release oxygen to the organs and tissues.<sup id="cite_ref-Bernard2013_16-0" class="reference"><a href="#cite_note-Bernard2013-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> The disease is fatal for the fetus or newborn unless early diagnosis and intervention is carried out during pregnancy, and the child will be dependent on lifelong blood transfusions. </p> <div class="mw-heading mw-heading3"><h3 id="Quantification_of_oxygen_binding">Quantification of oxygen binding</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=6" title="Edit section: Quantification of oxygen binding"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>To quantify how strongly a certain type of hemoglobin binds to oxygen (or its affinity for oxygen), a parameter called P50 is often used. In a given situation, P50 can be understood as the partial pressure of oxygen at which Hb is 50% saturated.<sup id="cite_ref-Vibhu2006_17-0" class="reference"><a href="#cite_note-Vibhu2006-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup> For example, Hemoglobin F has a lower P50 than hemoglobin A. This means that if we have the same amount of hemoglobin F and hemoglobin A in the blood and add oxygen to it, half of hemoglobin F will bind to oxygen before half of hemoglobin A manages to do so. Therefore, a lower P50 means stronger binding or higher affinity for oxygen. </p><p>For reference, the P50 of fetal hemoglobin is roughly 19 mmHg (a measure of pressure), whereas adult hemoglobin is approximately 26.8 mmHg (see <a href="/wiki/Blood_gas_tension" title="Blood gas tension">Blood gas tension</a>).<sup id="cite_ref-Yacov2017_18-0" class="reference"><a href="#cite_note-Yacov2017-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Oxygen_exchange_in_the_womb">Oxygen exchange in the womb</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=7" title="Edit section: Oxygen exchange in the womb"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>During pregnancy, the mother's circulatory system delivers oxygen and nutrients to the fetus and carries away nutrient-depleted blood enriched with carbon dioxide. The maternal and fetal blood circulations are separate and the exchange of molecules occurs through the placenta, in a region called <a href="/wiki/Intervillous_space" title="Intervillous space">intervillous space</a> which is located in between maternal and fetal blood vessels.<sup id="cite_ref-Wang_Y_&_Zhao_S_3-1" class="reference"><a href="#cite_note-Wang_Y_&_Zhao_S-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> </p><p>Focusing on oxygen exchange, there are three important aspects that allow oxygen to pass from the maternal circulation into the fetal circulation. Firstly, the presence of hemoglobin F in the fetus allows a stronger binding to oxygen than maternal hemoglobin (see <a href="#Factors_affecting_oxygen_affinity"><i>Factors affecting oxygen affinity</i></a>). Secondly, the mother's bloodstream is richer in oxygen than that of the fetus, so oxygen naturally flows towards the fetal circulation by diffusion.<sup id="cite_ref-Metcalfe1967_19-0" class="reference"><a href="#cite_note-Metcalfe1967-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> The final factor is related to the effects of pH on maternal and fetal hemoglobin. As the maternal blood acquires more carbon dioxide, it becomes more acidic and this favors the release of oxygen by the maternal hemoglobin. At the same time, the decrease in carbon dioxide in fetal blood makes it more alkaline and favors the uptake of oxygen. This is called the Bohr effect or <a href="/wiki/Haldane_effect" title="Haldane effect">Haldane effect</a>, which also happens in the air exchange in the lungs.<sup id="cite_ref-Sarah2015_20-0" class="reference"><a href="#cite_note-Sarah2015-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> All of these three factors are present simultaneously and cooperate to improve the fetus’ access to oxygen from the mother. </p> <div class="mw-heading mw-heading2"><h2 id="F-cells">F-cells</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=8" title="Edit section: F-cells"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>F-cells are the subpopulation of red blood cells that contain hemoglobin F, in amongst other types of hemoglobin. While common in fetuses, in normal adults, only around 3-7% of red blood cells contain hemoglobin F.<sup id="cite_ref-Italia2007_21-0" class="reference"><a href="#cite_note-Italia2007-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> The low percentage of F-cells in adults owes to two factors: very low levels of hemoglobin F being present and its tendency to be produced only in a subset of cells rather than evenly distributed amongst all red blood cells. In fact, there is a positive correlation between the levels of hemoglobin F and number of F-cells, with patients with higher percentages of hemoglobin F also having a higher proportion of F-cells.<sup id="cite_ref-Wood1975_22-0" class="reference"><a href="#cite_note-Wood1975-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> Despite the correlations between hemoglobin F levels and F-cell numbers, usually they are determined by direct measurements. While the amount of hemoglobin F is calculated using cell lysates, which are fluids with contents of cells that were broken open, F-cell numbers are done by counting intact red blood cells.<sup id="cite_ref-Italia2007_21-1" class="reference"><a href="#cite_note-Italia2007-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> </p><p>Due to the correlation between the amount of hemoglobin F and F-cells, F-cell numbers are higher in some inherited hemoglobin disorders, including <a href="/wiki/Beta-thalassemia" class="mw-redirect" title="Beta-thalassemia">beta-thalassemia</a>, <a href="/wiki/Sickle_cell_anemia" class="mw-redirect" title="Sickle cell anemia">sickle cell anemia</a> and <a href="/wiki/Hereditary_persistence_of_fetal_hemoglobin" title="Hereditary persistence of fetal hemoglobin">hereditary persistence of fetal hemoglobin</a>. Additionally, some acquired conditions can also have higher F-cell numbers, such as acute erythropoietic stress (response to poor oxygenation which includes very rapid synthesis of new red blood cells)<sup id="cite_ref-Kim2015_23-0" class="reference"><a href="#cite_note-Kim2015-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> and pregnancy.<sup id="cite_ref-Italia2007_21-2" class="reference"><a href="#cite_note-Italia2007-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> F-cells have similar mass of haemoglobin per cell compared to red blood cells without haemoglobin F, which is measured <a href="/wiki/Mean_cell_haemoglobin" class="mw-redirect" title="Mean cell haemoglobin">mean cell haemoglobin</a> values (MCH).<sup id="cite_ref-Dover1987_24-0" class="reference"><a href="#cite_note-Dover1987-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Conditions_with_high_hemoglobin_F">Conditions with high hemoglobin F</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=9" title="Edit section: Conditions with high hemoglobin F"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="During_pregnancy">During pregnancy</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=10" title="Edit section: During pregnancy"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>There is a significant increase in hemoglobin F levels during early pregnancy. However, it's not clear whether these levels are stable or decrease as the pregnancy goes on, as different sources reported different results.<sup id="cite_ref-Ibrahim2009_25-0" class="reference"><a href="#cite_note-Ibrahim2009-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Takashi2013_26-0" class="reference"><a href="#cite_note-Takashi2013-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> The increase in hemoglobin F then induces a 3 to 7 fold increase in the number of F-cells in pregnant women, which was observed between the 23rd to 31st week of gestation.<sup id="cite_ref-Boyer1975_27-0" class="reference"><a href="#cite_note-Boyer1975-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> However, as to the reason of the increase in hemoglobin F levels in pregnant women, there doesn't seem to be conclusive evidence. While an early study suggested that maternal red blood cells switch on hemoglobin F production during pregnancy,<sup id="cite_ref-Boyer1975_27-1" class="reference"><a href="#cite_note-Boyer1975-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> more recent literature suggested that the increase in haemoglobin F could be, at least in part, due to fetal red blood cells being transferred to the maternal circulation.<sup id="cite_ref-Dana2018_28-0" class="reference"><a href="#cite_note-Dana2018-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Italia2007_21-3" class="reference"><a href="#cite_note-Italia2007-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> </p><p>Presence of high levels of hemoglobin F in pregnant women can impact the growth of the fetus, as fetal red blood cells struggle to compete for the oxygen from the mother's circulation. This is because instead of competing with hemoglobin A, which has a weaker association to oxygen than hemoglobin F, it becomes a competition between fetal and maternal hemoglobin F which have similar affinities for oxygen. As a result, women with hemoglobin F as >70% of total hemoglobin are much more likely to have fetuses that are small for their gestational age compared women with <70% hemoglobin F (at a rate of 100% compared to 8%, respectively).<sup id="cite_ref-Ally2011_29-0" class="reference"><a href="#cite_note-Ally2011-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Hereditary_persistence_of_fetal_hemoglobin_(HPFH)"><span id="Hereditary_persistence_of_fetal_hemoglobin_.28HPFH.29"></span>Hereditary persistence of fetal hemoglobin (HPFH)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=11" title="Edit section: Hereditary persistence of fetal hemoglobin (HPFH)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Hereditary_persistence_of_fetal_hemoglobin" title="Hereditary persistence of fetal hemoglobin">Hereditary persistence of fetal hemoglobin</a></div> <p>This is a rare benign genetic disease where production of hemoglobin F persists after twelve months of life and into the adulthood. As a result, hemoglobin F is present in a higher number of adult red blood cells than normal.<sup id="cite_ref-Ada2014_30-0" class="reference"><a href="#cite_note-Ada2014-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup> It doesn't present symptoms and is usually discovered when screening for other blood-related diseases. In this condition, the genes coding for the γ subunit (HBG1 and HBG2) are not suppressed shortly before birth. This can happen when a mutation occurs in the promoter region of HBG1 and HBG2, preventing the binding of BCL11A and ZBTB7A proteins. These proteins would normally bind and suppress the production of γ subunits and as they can't bind due to the mutation, γ subunits continue to be produced.<sup id="cite_ref-Martyn2018_10-2" class="reference"><a href="#cite_note-Martyn2018-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> There are two types of patients with HPFH: either with one normal copy of the gene and one disease form or with two disease copies. Whereas normal adults have less than 1% of hemoglobin F, patients with only one disease gene have 5-30%. Patients with two disease copies can have hemoglobin F in up to 100% of red blood cells.<sup id="cite_ref-Thein1998_31-0" class="reference"><a href="#cite_note-Thein1998-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> As other diseases such as sickle cell disease could also cause a higher level of hemoglobin F to be present, it can sometimes be misdiagnosed.<sup id="cite_ref-Irfan2018_32-0" class="reference"><a href="#cite_note-Irfan2018-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Delta_beta-thalassemia">Delta beta-thalassemia</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=12" title="Edit section: Delta beta-thalassemia"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Delta beta-thalassemia is a rare genetic blood disorder in which the production of both δ and β subunits are reduced or absent. In these cases, the production of the γ subunit increases to compensate for the loss of δ and β subunits, resulting in a higher amount of hemoglobin F present in the blood. Normally, people have two sets of genes for producing δ and β subunits. People with only one set of working genes don't get any symptoms and in the rarely reported cases where both sets of genes are affected, the patients only experienced mild symptoms.<sup id="cite_ref-Amer2015_33-0" class="reference"><a href="#cite_note-Amer2015-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Clinical_significance">Clinical significance</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=13" title="Edit section: Clinical significance"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Treatment_of_sickle-cell_disease">Treatment of sickle-cell disease</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=14" title="Edit section: Treatment of sickle-cell disease"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Sicklecells.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/9/92/Sicklecells.jpg" decoding="async" width="144" height="168" class="mw-file-element" data-file-width="144" data-file-height="168" /></a><figcaption>Increasing the body's production of fetal hemoglobin is used as a strategy to treat <a href="/wiki/Sickle-cell_disease" class="mw-redirect" title="Sickle-cell disease">sickle-cell disease</a>.</figcaption></figure> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Sickle-cell_disease#Hydroxyurea" class="mw-redirect" title="Sickle-cell disease">Sickle-cell disease § Hydroxyurea</a></div> <p>The discovery that hemoglobin F alleviated the symptoms of sickle cell disease occurred in 1948. Janet Watson observed that red blood cells from infants with the disease took longer to sickle and did not deform as much compared to their mother's cells, which carried the disease trait. Later, it was noted that patients with sickle cell trait as well as hereditary persistence of hemoglobin F (HPFH) didn't have symptoms.<sup id="cite_ref-Idowu2011_34-0" class="reference"><a href="#cite_note-Idowu2011-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> Additionally, in sickle cell patients, F-cells were found to be more long living than non-F cells as they contain hemoglobin F. </p><p>When fetal hemoglobin production is switched off after birth, normal children begin producing adult hemoglobin (HbA). Children with <a href="/wiki/Sickle-cell_disease" class="mw-redirect" title="Sickle-cell disease">sickle-cell disease</a> begin producing a defective form of hemoglobin called <a href="/wiki/Hemoglobin_S" class="mw-redirect" title="Hemoglobin S">hemoglobin S</a> instead, which form chains that cause <a href="/wiki/Red_blood_cell" title="Red blood cell">red blood cells</a> to change their shape from round to <a href="/wiki/Sickle" title="Sickle">sickle</a>-shaped.<sup id="cite_ref-NIH_Sicklecelldisease_35-0" class="reference"><a href="#cite_note-NIH_Sicklecelldisease-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> These defective red blood cells have a much shorter life span than normal red blood cells (10–20 days compared to up to 120 days).<sup id="cite_ref-Hopkins_36-0" class="reference"><a href="#cite_note-Hopkins-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup> They also have a greater tendency to clump together and block small <a href="/wiki/Blood_vessel" title="Blood vessel">blood vessels</a>, preventing blood supply to tissues and organs. This leads to the so-called <i><a href="/wiki/Vaso-occlusive_crisis" title="Vaso-occlusive crisis">vaso-occlusive crisis</a></i>, which is a hallmark of the disease.<sup id="cite_ref-Deepa2013_37-0" class="reference"><a href="#cite_note-Deepa2013-37"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup> If fetal hemoglobin remains relatively high after birth, the number of painful episodes decreases in patients with sickle-cell disease and they have a better prognosis.<sup id="cite_ref-Idow2011_38-0" class="reference"><a href="#cite_note-Idow2011-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> Fetal hemoglobin's role in reducing disease severity comes from its ability to disrupt the formation of hemoglobin S chains within red blood cells.<sup id="cite_ref-Ma2007_39-0" class="reference"><a href="#cite_note-Ma2007-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> Interestingly, while higher levels of hemoglobin F were associated with improvement of some symptoms, including the frequency of painful episodes, leg ulcers and the general severity of the disease, it had no correlation to others. A few examples are <a href="/wiki/Priapism" title="Priapism">priapism</a>, stroke and systemic blood pressure.<sup id="cite_ref-Idowu2011_34-1" class="reference"><a href="#cite_note-Idowu2011-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> As hemoglobin F are only produced by some red blood cells, in different quantities, only a subpopulation of cells are protected against sickling. It could be that the symptoms that high hemoglobin F doesn't prevent are quite sensitive to the rupture of the sickled non-F cells.<sup id="cite_ref-Idowu2011_34-2" class="reference"><a href="#cite_note-Idowu2011-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> </p><p><a href="/wiki/Hydroxyurea" class="mw-redirect" title="Hydroxyurea">Hydroxyurea</a> is a chemical that promotes the production of fetal hemoglobin and reduces the premature rupturing of red blood cells.<sup id="cite_ref-pmid18458272_6-1" class="reference"><a href="#cite_note-pmid18458272-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid7715639_40-0" class="reference"><a href="#cite_note-pmid7715639-40"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup> Combination therapy with hydroxyurea and recombinant <a href="/wiki/Erythropoietin" title="Erythropoietin">erythropoietin</a> — rather than treatment with hydroxyurea alone — has been shown to further elevate hemoglobin F levels and to promote the development of HbF-containing F-cells.<sup id="cite_ref-pmid7677965_41-0" class="reference"><a href="#cite_note-pmid7677965-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Hemoglobin_F_as_a_marker_for_cancers">Hemoglobin F as a marker for cancers</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=15" title="Edit section: Hemoglobin F as a marker for cancers"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>There have been some studies evaluating the possibility of using hemoglobin F as an indicator of the prognosis for cancer. It has been suggested that elevated concentrations of haemoglobin F can be found in main kinds of solid tumours and blood cancers.<sup id="cite_ref-Wolk1999_42-0" class="reference"><a href="#cite_note-Wolk1999-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup> Examples include acute lymphoblastic leukemia and myeloid leukemia in children, where higher concentrations of hemoglobin F were associated with a worse outcome, including a higher risk of relapse or death.<sup id="cite_ref-Rautonen1990_43-0" class="reference"><a href="#cite_note-Rautonen1990-43"><span class="cite-bracket">[</span>43<span class="cite-bracket">]</span></a></sup> Other cancer types where higher hemoglobin F levels have been observed are transitional cell cancer,<sup id="cite_ref-Wolk2012_44-0" class="reference"><a href="#cite_note-Wolk2012-44"><span class="cite-bracket">[</span>44<span class="cite-bracket">]</span></a></sup> colorectal carcinoma<sup id="cite_ref-Wolk2006_45-0" class="reference"><a href="#cite_note-Wolk2006-45"><span class="cite-bracket">[</span>45<span class="cite-bracket">]</span></a></sup> and various types of blastomas.<sup id="cite_ref-Wolk2007_46-0" class="reference"><a href="#cite_note-Wolk2007-46"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup> In fact, in several types of blastomas, including neuroblastoma and retinoblastoma (affecting the nerve cells and the eyes, respectively), F-cells were found in newly formed blood vessels and spaces in between tumour cells. Clusters of F-cells were also present in the <a href="/wiki/Bone_marrow" title="Bone marrow">bone marrow</a> of some of these patients.<sup id="cite_ref-Wolk2007_46-1" class="reference"><a href="#cite_note-Wolk2007-46"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup> Interestingly, hemoglobin F is not directly produced by tumour cells, but seems to be induced by the biological environment of the cancer in nearby blood cells. A reason suggested for this increase in hemoglobin F is that it may favor cancer growth by providing better oxygen supply to the developing cancerous cells.<sup id="cite_ref-Wolk2012_44-1" class="reference"><a href="#cite_note-Wolk2012-44"><span class="cite-bracket">[</span>44<span class="cite-bracket">]</span></a></sup> In adults, increased hemoglobin F production is thought to be caused by factors leading to the activation of the gene coding for the γ subunit, such as <a href="/wiki/DNA_demethylation" title="DNA demethylation">DNA demethylation</a> (which can activate normally silent genes and is a hallmark of cancer).<sup id="cite_ref-David2015_47-0" class="reference"><a href="#cite_note-David2015-47"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=16" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist"> <div class="mw-references-wrap mw-references-columns"><ol class="references"> <li id="cite_note-David_1998-1"><span class="mw-cite-backlink">^ <a href="#cite_ref-David_1998_1-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-David_1998_1-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFLinch1998" class="citation book cs1">Linch D (1998). <a rel="nofollow" class="external text" href="https://www.sciencedirect.com/science/article/pii/B0122267656001031"><i>Encyclopedia of Immunology</i></a> (second ed.). 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href="/w/index.php?title=Fetal_hemoglobin&action=edit&section=17" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a rel="nofollow" class="external text" href="http://sickle.bwh.harvard.edu/hemoglobinopathy.html">Hemoglobinopathies</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20040609153506/http://arbl.cvmbs.colostate.edu/hbooks/pathphys/reprod/placenta/transport.html">Transport across the placenta</a></li> <li><a rel="nofollow" class="external text" href="http://www.ascaa.org/">American Sickle Cell Anemia Association</a></li> <li><a rel="nofollow" class="external text" href="http://www.sicklecelldisease.org">SCDAA: Break The Sickle Cycle</a></li> <li><a rel="nofollow" class="external text" href="http://sickle.bwh.harvard.edu/hbsynthesis.html">Hemoglobin synthesis</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20020203114057/http://ntri.tamuk.edu/homepage-ntri/lectures/protein/hemoglobin/hempage.html">Hemoglobin structure and function (archived February 3, 2002</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20091029025455/http://fha.maryland.gov/genetics/hemo_f.cfm">Hemoglobin F fact sheet (archived October 29, 2009)</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20030330064928/http://www.isat.jmu.edu/users/klevicca/ISAT454/FetalHb.doc">Fetal hemoglobin (doc file; archived March 30 2003)</a></li> <li><a rel="nofollow" class="external text" href="http://sickle.bwh.harvard.edu/hyguid.html">Hydroxyurea in sickle-cell disease</a> (archived December 28, 2014 at <a rel="nofollow" class="external autonumber" href="https://web.archive.org/web/20141228112837/http://sickle.bwh.harvard.edu/hyguid.html">[2]</a>)</li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20150329032048/http://scinfo.org/the-management-of-sickle-cell-disease-4th-ed/special-topics-chapter-26-fetal-hemoglobin-induction">Chapter 26 Fetal Hemoglobin Induction; Management of Sickle-Cell Disease 4th Edition 2002 (NIH Publication No. 02-2117)</a></li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist li{margin:0;display:inline}.mw-parser-output .hlist.inline,.mw-parser-output .hlist.inline dl,.mw-parser-output .hlist.inline ol,.mw-parser-output .hlist.inline ul,.mw-parser-output .hlist dl dl,.mw-parser-output .hlist dl ol,.mw-parser-output .hlist dl ul,.mw-parser-output .hlist ol dl,.mw-parser-output .hlist ol ol,.mw-parser-output .hlist ol ul,.mw-parser-output .hlist ul dl,.mw-parser-output .hlist ul ol,.mw-parser-output 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.navbox-group,.mw-parser-output .navbox-subgroup .navbox-title{background-color:#ddf}.mw-parser-output .navbox-subgroup .navbox-group,.mw-parser-output .navbox-subgroup .navbox-abovebelow{background-color:#e6e6ff}.mw-parser-output .navbox-even{background-color:#f7f7f7}.mw-parser-output .navbox-odd{background-color:transparent}.mw-parser-output .navbox .hlist td dl,.mw-parser-output .navbox .hlist td ol,.mw-parser-output .navbox .hlist td ul,.mw-parser-output .navbox td.hlist dl,.mw-parser-output .navbox td.hlist ol,.mw-parser-output .navbox td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}body.skin--responsive .mw-parser-output .navbox-image img{max-width:none!important}@media print{body.ns-0 .mw-parser-output .navbox{display:none!important}}</style></div><div role="navigation" class="navbox" aria-labelledby="Proteins_that_contain_heme_(hemoproteins)178" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><style data-mw-deduplicate="TemplateStyles:r1239400231">.mw-parser-output .navbar{display:inline;font-size:88%;font-weight:normal}.mw-parser-output .navbar-collapse{float:left;text-align:left}.mw-parser-output .navbar-boxtext{word-spacing:0}.mw-parser-output .navbar ul{display:inline-block;white-space:nowrap;line-height:inherit}.mw-parser-output .navbar-brackets::before{margin-right:-0.125em;content:"[ "}.mw-parser-output .navbar-brackets::after{margin-left:-0.125em;content:" ]"}.mw-parser-output .navbar li{word-spacing:-0.125em}.mw-parser-output .navbar a>span,.mw-parser-output .navbar a>abbr{text-decoration:inherit}.mw-parser-output .navbar-mini abbr{font-variant:small-caps;border-bottom:none;text-decoration:none;cursor:inherit}.mw-parser-output .navbar-ct-full{font-size:114%;margin:0 7em}.mw-parser-output .navbar-ct-mini{font-size:114%;margin:0 4em}html.skin-theme-clientpref-night .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}@media(prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}}@media print{.mw-parser-output .navbar{display:none!important}}</style><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Hemeproteins" title="Template:Hemeproteins"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Hemeproteins" title="Template talk:Hemeproteins"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Hemeproteins" title="Special:EditPage/Template:Hemeproteins"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Proteins_that_contain_heme_(hemoproteins)178" style="font-size:114%;margin:0 4em"><a href="/wiki/Protein" title="Protein">Proteins</a> that contain <a href="/wiki/Heme" title="Heme">heme</a> (<a href="/wiki/Hemoprotein" title="Hemoprotein">hemoproteins</a>)</div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Globin" title="Globin">Globins</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Hemoglobin" title="Hemoglobin">Hemoglobin</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">Subunits</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><i>Alpha locus on <a href="/wiki/Chromosome_16" title="Chromosome 16">16</a>:</i></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><i>α</i> <ul><li><a href="/wiki/Hemoglobin_subunit_alpha" title="Hemoglobin subunit alpha">HBA1</a></li> <li><a href="/wiki/Hemoglobin,_alpha_2" title="Hemoglobin, alpha 2">HBA2</a></li> <li><a href="/wiki/HBAP1" title="HBAP1">pseudo</a></li></ul></li> <li><i>ζ</i> <ul><li><a href="/wiki/Hemoglobin_subunit_zeta" title="Hemoglobin subunit zeta">HBZ</a></li></ul></li> <li><i>θ</i> <ul><li><a href="/wiki/HBQ1" title="HBQ1">HBQ1</a></li></ul></li> <li><i>μ</i> <ul><li><a href="/wiki/Mu_hemoglobin" title="Mu hemoglobin">HBM</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><i><a href="/wiki/Human_%CE%B2-globin_locus" title="Human β-globin locus">Beta locus</a> on <a href="/wiki/Chromosome_11" title="Chromosome 11">11</a>:</i></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><i>β</i> <ul><li><a href="/wiki/Hemoglobin_subunit_beta" title="Hemoglobin subunit beta">HBB</a></li></ul></li> <li><i>δ</i> <ul><li><a href="/wiki/HBD" title="HBD">HBD</a></li></ul></li> <li><i>γ</i> <ul><li><a href="/wiki/HBG1" title="HBG1">HBG1</a></li> <li><a href="/wiki/HBG2" title="HBG2">HBG2</a></li></ul></li> <li><i>ε</i> <ul><li><a href="/wiki/HBE1" title="HBE1">HBE1</a></li></ul></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Tetrameric_protein" title="Tetrameric protein">Tetramers</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><i>stages of <br />development:</i></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">Embryonic</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Embryonic_hemoglobin" title="Embryonic hemoglobin">HbE Gower 1</a> (ζ<sub>2</sub>ε<sub>2</sub>)</li> <li><a href="/wiki/Embryonic_hemoglobin" title="Embryonic hemoglobin">HbE Gower 2</a> (α<sub>2</sub>ε<sub>2</sub>)</li> <li><a href="/wiki/Embryonic_hemoglobin" title="Embryonic hemoglobin">HbE Portland I</a> (ζ<sub>2</sub>γ<sub>2</sub>)</li> <li><a href="/wiki/Embryonic_hemoglobin" title="Embryonic hemoglobin">HbE Portland II</a> (ζ<sub>2</sub>β<sub>2</sub>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Fetal</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a class="mw-selflink selflink">HbF/Fetal</a> (α<sub>2</sub>γ<sub>2</sub>)</li> <li><a href="/wiki/Hemoglobin_A" title="Hemoglobin A">HbA</a> (α<sub>2</sub>β<sub>2</sub>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Adult</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Hemoglobin_A" title="Hemoglobin A">HbA</a> (α<sub>2</sub>β<sub>2</sub>)</li> <li><a href="/wiki/Hemoglobin_A2" title="Hemoglobin A2">HbA<sub>2</sub></a> (α<sub>2</sub>δ<sub>2</sub>)</li> <li><a class="mw-selflink selflink">HbF/Fetal</a> (α<sub>2</sub>γ<sub>2</sub>)</li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><i>pathology:</i></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Alpha-thalassemia" title="Alpha-thalassemia">HbH</a> (β<sub>4</sub>)</li> <li><a href="/wiki/Hemoglobin_Barts" title="Hemoglobin Barts">Barts</a> (γ<sub>4</sub>)</li> <li><a href="/wiki/HbD" class="mw-redirect" title="HbD">HbD</a> (α<sub>2</sub>β<sup>D</sup><sub>2</sub>)</li> <li><a href="/wiki/Sickle_cell_disease" title="Sickle cell disease">HbS</a> (α<sub>2</sub>β<sup>S</sup><sub>2</sub>)</li> <li><a href="/wiki/Hemoglobin_C" title="Hemoglobin C">HbC</a> (α<sub>2</sub>β<sup>C</sup><sub>2</sub>)</li> <li><a href="/wiki/Hemoglobin_E" title="Hemoglobin E">HbE</a> (α<sub>2</sub>β<sup>E</sup><sub>2</sub>)</li> <li><a href="/wiki/Hemoglobin_O" title="Hemoglobin O">HbO</a> (α<sub>2</sub>β<sup>O</sup><sub>2</sub>)</li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Compounds</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Carboxyhemoglobin" title="Carboxyhemoglobin">Carboxyhemoglobin</a></li> <li><a href="/wiki/Carbaminohemoglobin" title="Carbaminohemoglobin">Carbaminohemoglobin</a></li> <li><a href="/wiki/Hemoglobin" title="Hemoglobin">Oxyhemoglobin</a>/<a href="/wiki/Deoxyhemoglobin" class="mw-redirect" title="Deoxyhemoglobin">Deoxyhemoglobin</a></li> <li><a href="/wiki/Sulfhemoglobinemia" title="Sulfhemoglobinemia">Sulfhemoglobin</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other human</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycated_hemoglobin" title="Glycated hemoglobin">Glycated hemoglobin</a></li> <li><a href="/wiki/Methemoglobin" title="Methemoglobin">Methemoglobin</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Nonhuman</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Erythrocruorin" title="Erythrocruorin">Chlorocruorin</a></li> <li><a href="/wiki/Erythrocruorin" title="Erythrocruorin">Erythrocruorin</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><i>human:</i></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Myoglobin" title="Myoglobin">Myoglobin</a> <ul><li><a href="/wiki/Metmyoglobin" title="Metmyoglobin">Metmyoglobin</a></li></ul></li> <li><a href="/wiki/Neuroglobin" title="Neuroglobin">Neuroglobin</a></li> <li><a href="/wiki/Cytoglobin" title="Cytoglobin">Cytoglobin</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><i>plant:</i></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Leghemoglobin" title="Leghemoglobin">Leghemoglobin</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Cytochrome" title="Cytochrome">Cytochrome</a> <ul><li><a href="/wiki/Cytochrome_b" title="Cytochrome b">Cytochrome b</a></li> <li><a href="/wiki/Cytochrome_P450" title="Cytochrome P450">Cytochrome P450</a></li></ul></li> <li><a href="/wiki/Methemalbumin" title="Methemalbumin">Methemalbumin</a></li></ul> </div></td></tr><tr><td class="navbox-abovebelow" colspan="2" style="background: transparent; padding: 0px;"><div><i>see also <a href="/wiki/Template:Disorders_of_globin_and_globulin_proteins" title="Template:Disorders of globin and globulin proteins">disorders of globin and globulin proteins</a></i></div></td></tr></tbody></table></div>    </div><noscript><img src="https://login.wikimedia.org/wiki/Special:CentralAutoLogin/start?useformat=desktop&type=1x1&usesul3=0" alt="" width="1" height="1" style="border: none; position: absolute;"></noscript> <div class="printfooter" data-nosnippet="">Retrieved from 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