Other Types of Amyloidosis - Amyloidosis Research Consortium

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class="s1">Some types are hereditary meaning that it is caused by a faulty gene that runs in families, while </span><span class="s2">others</span><span class="s3"> are</span><span class="s1"> acquired during life.</span></p> <p class="p1"><span class="s1">Each type of amyloidosis is referred to as “A” for amyloid followed by an abbreviation for the abnormal protein that misfolds and deposits as amyloid in various tissues and organs throughout the body.</span></p> <p class="p1"><span class="s2">While there</span><span class="s1"> are no specific treatments for these types of amyloidosis,</span> <span class="s1">supportive treatment may help to reduce symptoms, improve organ function and enhance quality of life.</span></p> <p class="p2"><span class="s1">ARC is committed to supporting the development of treatments for the less common types of amyloidosis. For us to be able to drive research, we need to gather as much information from patients with these types of amyloidosis. By signing up to our clinical trial finder tool, we will be able to better advocate for you. <a href="http://www.myamyloidosispathfinder.org" target="_blank" rel="noopener">Join now</a></span></p> <p><strong>Other types of systemic amyloidosis include:</strong></p> </div> <div class="col-md-5 col-lg-4 offset-lg-1"> <div class="contact-box"> <h5>Contact Our Specialist Team</h5> <p>We're here to help you.</p> <span href=""><i class="fa fa-phone" aria-hidden="true"></i> (617) 467-5170</span> <a href="mailto:support@arci.org"><i class="fa fa-envelope-o" aria-hidden="true"></i> support@arci.org</a> </div> </div> </div> </div> </div> <div class="block-accordion block-padding"> <div class="container"> <div class="accordion-item"> <div class="accordion-header"> <div class="accordion-title">AA Amyloidosis</div> <div class="toggle-icon"> <span class="icon"></span> <span class="icon"></span> </div> </div> <div class="accordion-content"> <p>AA amyloidosis occurs in a small number of patients who have experienced a long-standing inflammatory or infectious disease in which excessive amounts of a protein called Serum Amyloid A (SAA) are produced as a biproduct of the normal immune response. For reasons that are unknown, SAA proteins at some point become misfolded and deposit as amyloid. While these misfolded proteins mostly affect the kidneys, they can sometimes affect the liver and spleen as well. Treatment for AA amyloidosis is geared towards controlling the problems associated with the underlying inflammatory or infectious disease. Improvements in treatments for inflammatory diseases and chronic infections have led to a decline in AA amyloidosis in recent years, especially in developed countries.</p> </div> </div> <div class="accordion-item"> <div class="accordion-header"> <div class="accordion-title">ALECT2 Amyloidosis</div> <div class="toggle-icon"> <span class="icon"></span> <span class="icon"></span> </div> </div> <div class="accordion-content"> <p>ALECT2 amyloidosis is a recently recognized form of amyloidosis involving a protein called leukocyte chemotactic factor 2 (LECT2) which normally circulates in the blood and helps repair damaged tissue by attracting white blood cells. The underlying reason which causes LECT2 proteins to become abnormal and misfold is currently unknown. Excessive amounts of the LECT2 protein are not produced in patients and there have not been any mutations in the LECT2 gene identified thus far. ALECT2 amyloidosis appears to be more common in the elderly population of certain ethnic groups including those of Mexican, Native American, Punjabi, North African and Middle Eastern descent. This type of amyloid deposits have been most commonly found in the kidneys; however, they may also be found in the liver, adrenal glands and spleen. Experts believe that ALECT2 amyloidosis is underdiagnosed and may be a more common cause of kidney failure than currently suspected. While there are currently no existing treatments for this type of amyloidosis, research continues to grow in this area.</p> </div> </div> <div class="accordion-item"> <div class="accordion-header"> <div class="accordion-title">Aß2M Amyloidosis</div> <div class="toggle-icon"> <span class="icon"></span> <span class="icon"></span> </div> </div> <div class="accordion-content"> <p>Aß2M amyloidosis is a type of amyloidosis that is normally associated with patients who have been on kidney dialysis for more than five years. It is caused by the progressive build-up of the beta 2 microglobulin (Aß2M) protein, which is not effectively cleared by dialysis. Over time, the Aß2M proteins become abnormal, misfold and deposit as amyloid, primarily around the bones and joints. As modern dialysis procedures have improved, Aß2M amyloidosis is becoming much less common.</p> </div> </div> <div class="accordion-item"> <div class="accordion-header"> <div class="accordion-title">Apolipoprotein Amyloidosis</div> <div class="toggle-icon"> <span class="icon"></span> <span class="icon"></span> </div> </div> <div class="accordion-content"> <p>Apolipoprotein amyloidosis is caused by one of several proteins belonging to a family of proteins called apolipoproteins, which normally play important roles in the transport and metabolism of cholesterol and fat in the body. There are currently five types of apolipoprotein amyloidosis known to form, most of which are hereditary – caused by a fault or mutation in the respective apolipoprotein gene, which is transmitted from parents to their offspring. This genetic mutation results in an abnormal apolipoprotein that is unstable and misfolds to form amyloid deposits in various tissues and organs, depending on the type of apolipoprotein. The types of apolipoprotein which are known to form amyloid include: Apolipoprotein amyloidosis is caused by one of several proteins belonging to a family of proteins called apolipoproteins, which normally play important roles in the transport and metabolism of cholesterol and fat in the body. There are currently five types of apolipoprotein amyloidosis known to form, most of which are hereditary – caused by a fault or mutation in the respective apolipoprotein gene, which is transmitted from parents to their offspring. This genetic mutation results in an abnormal apolipoprotein that is unstable and misfolds to form amyloid deposits in various tissues and organs, depending on the type of apolipoprotein. The types of apolipoprotein which are known to form amyloid include:</p> <ul> <li>Apolipoprotein A-I (AApoA-I) – affects the heart, liver and peripheral nervous system</li> <li>Apolipoprotein A-II (AApoA-II) – primarily affects the kidneys</li> <li>Apolipoprotein A-IV (AApoA-IV) – affects the kidneys and heart</li> <li>Apolipoprotein C-II (AApoC-II) – primarily affects the kidneys</li> <li>Apolipoprotein C-III (AApoC-III) – primarily affects the kidneys</li> </ul> </div> </div> <div class="accordion-item"> <div class="accordion-header"> <div class="accordion-title">Hereditary Fibrinogen Amyloidosis</div> <div class="toggle-icon"> <span class="icon"></span> <span class="icon"></span> </div> </div> <div class="accordion-content"> <p>Hereditary fibrinogen (AFib) amyloidosis is caused by a fault or mutation in the hereditary fibrinogen alpha chain gene, passed down from parents to their offspring. Fibrinogen forms in the liver and plays a central role in blood clotting. Mutations in the fibrinogen gene give rise to an abnormal fibrinogen protein, which then misfolds and aggregates to form amyloid deposits. To date, 16 mutations in the fibrinogen alpha chain gene have been identified, which cause hereditary fibrinogen amyloidosis. All mutations cause amyloidosis and primarily affect the kidneys. While there are currently no existing treatments for this type of amyloidosis, research continues to grow in this area.</p> </div> </div> <div class="accordion-item"> <div class="accordion-header"> <div class="accordion-title">Hereditary Gelsolin Amyloidosis</div> <div class="toggle-icon"> <span class="icon"></span> <span class="icon"></span> </div> </div> <div class="accordion-content"> <p>Hereditary gelsolin (AGel) amyloidosis is caused by a fault or mutation in the hereditary gelsolin gene, passed down from parents to their offspring. Gelsolin is found in the cytoskeleton and helps provide shape and structure for cells. Mutations in the gelsolin gene produce abnormal gelsolin proteins that are unstable and misfold to form amyloid deposits in the cranial nerves (emerging from the brain), eyes, skin and kidneys. This type of amyloidosis originated in Finland and has since been reported in other countries. Thus far, four different mutations in the gelsolin gene have been identified, which cause amyloidosis. While there are currently no existing treatments for this type of amyloidosis, research continues to grow in this area.</p> </div> </div> <div class="accordion-item"> <div class="accordion-header"> <div class="accordion-title">Hereditary Lysozyme Amyloidosis</div> <div class="toggle-icon"> <span class="icon"></span> <span class="icon"></span> </div> </div> <div class="accordion-content"> <p>Hereditary lysozyme (ALys) amyloidosis is caused by a fault or mutation in the hereditary lysozyme gene, passed down from parents to their offspring. Lysozyme, an enzyme found in tears and mucus, plays an important role in reducing infections by breaking down bacterial cell walls. Mutations in the lysozyme gene produce abnormal lysozyme proteins, which misfold and aggregate to form amyloid deposits. There are currently a total of nine different mutations known to cause ALys amyloidosis; depending on the mutant gene, a variety of organs are affected, including the kidneys, digestive system and exocrine glands (tear, salivary and sweat glands). While there are currently no existing treatments for this type of amyloidosis, research continues to grow in this area.</p> </div> </div> </div> </div> <div class="block-page-links block-padding"> <div class="container"> <div class="row no-wrap"> <div class="col-md-6 col-lg col-xl margin-bottom"> <a class="page-link-container" href="/wild-type-amyloidosis/" style="background-color: #175b72"> <div class="page-link-padding"> <div class="link-title"><b>Wild-Type Amyloidosis</b></div> <div class="button-text">Find out more about wild-type amyloidosis</div> </div> </a> </div> <div class="col-md-6 col-lg col-xl margin-bottom"> <a class="page-link-container" href="/hereditary-attr-amyloidosis/" style="background-color: #83b951"> <div class="page-link-padding"> <div class="link-title"><b>Hereditary ATTR Amyloidosis</b></div> <div class="button-text">Find out more about hATTR amyloidosis</div> </div> </a> </div> <div class="col-md-6 col-lg col-xl margin-bottom"> <a class="page-link-container" href="/al-amyloidosis/" style="background-color: #209298"> <div class="page-link-padding"> <div class="link-title"><b>AL<br>Amyloidosis</b></div> <div class="button-text">Find out more about AL amyloidosis</div> </div> </a> </div> </div> </div> </div> </div> <script type="text/javascript" src="https://www.google.com/recaptcha/api.js?hl=en"></script> <footer id="colophon" class="site-footer"> <div class="container width-100sm"> <div class="row"> <div class="col-md-10 offset-md-1"> <div class="row">  <div class="col-sm-4 vert-line"> <a href="https://arci.org/events/" title="Events"> <img src="https://arci.org/wp-content/uploads/2024/07/Calendar-icon-orange.svg" alt="" /> <p class="titles"> Events </p> <p class="sub-text"> Check out upcoming conferences, webinars and fundraisers </p> </a> </div> <div class="col-sm-4 vert-line"> <a href="https://arci.org/patients-and-caregivers/treatment-centers-clinical-trials/" title="My Amyloidosis Pathfinder"> <img src="https://arci.org/wp-content/uploads/2018/06/Resources-icon.svg" alt="" /> <p class="titles"> My Amyloidosis Pathfinder </p> <p class="sub-text"> Find personalized treatment centers and clinical trials </p> </a> </div> <div class="col-sm-4 vert-line"> <a href="https://arci.org/researchers-and-healthcare-professionals/resources/" title="Resources"> <img src="https://arci.org/wp-content/uploads/2018/06/Publications-icon.svg" alt="" /> <p class="titles"> Resources </p> <p class="sub-text"> View ARC's library of resources and publications </p> </a> </div> </div> </div> </div> <div class="row newsletter"> <div class="col-12"> <p>Get the latest amyloidosis news and research from ARC.</p> <a href="https://arci.org/newsletter/" title="Join our newsletter">Join our newsletter</a> </div> </div> <div class="row socials"> <div class="col-12"> <ul> <li> <a href="https://www.facebook.com/amyloidosisresearchconsortium" target="_blank"> <i class="fa fa-facebook" aria-hidden="true"></i> </a> </li> <li> <a href="https://twitter.com/Amyloidosis_ARC" target="_blank"> <i class="fa fa-twitter" aria-hidden="true"></i> </a> </li> <li> <a href="https://www.youtube.com/channel/UCD_A4cq_YW4ggWTzlJygJvg" target="_blank"> <i class="fa fa-youtube" aria-hidden="true"></i> </a> </li> <li> <a href="mailto:arc@arci.org" title="email"> <i class="fa fa-envelope-o" aria-hidden="true"></i> </a> </li> </ul> </div> </div> </div> </footer> <div class="container footer2"> <div class="row"> <div class="col-12"> <img src="https://arci.org/wp-content/themes/arc/img/logo-footer.png" alt="" /> <div class="menu-footer-container"><ul id="menu-footer" class="menu"><li id="menu-item-1730" class="menu-item menu-item-type-post_type menu-item-object-page menu-item-1730"><a href="https://arci.org/donate/">Donate</a></li> <li id="menu-item-99" class="menu-item menu-item-type-post_type menu-item-object-page menu-item-99"><a href="https://arci.org/privacy/">Privacy</a></li> </ul></div> <p class="uppercase">AMYLOIDOSIS RESEARCH CONSORTIUM, INC.<br> 320 Nevada Street, Suite 210 Newton, MA 02460 USA | 617-467-5170<br> <a href="mailto:arc@arci.org" title="email arc@arci.org">arc@arci.org</a></p> <p>ARC is a 501(c)(3) nonprofit organization. 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