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Neuropeptides typically bind to [[G protein-coupled receptor]]s (GPCRs) to modulate neural activity and other tissues like the gut, muscles, and heart. Neuropeptides are synthesized from large precursor proteins which are cleaved and post-translationally processed then packaged into dense core [[Vesicle (biology and chemistry)|vesicles]]. Neuropeptides are often co-released with other neuropeptides and [[neurotransmitters]] in a single neuron, yielding a multitude of effects. Once released, neuropeptides can diffuse widely to affect a broad range of targets. Neuropeptides are extremely ancient and highly diverse chemical messengers. [[Placozoa|Placozoans]] such as ''[[Trichoplax]]'', extremely basal animals which do not possess neurons, use peptides for cell-to-cell communication in a way similar to the neuropeptides of higher animals. == Examples == {{Unreferenced section|date=February 2024}} Peptide signals play a role in information processing that is different from that of conventional neurotransmitters, and many appear to be particularly associated with specific behaviours. For example, [[oxytocin]] and [[vasopressin]] have striking and specific effects on social behaviours, including maternal behaviour and pair bonding. [[Crustacean Cardioactive Peptide|CCAP]] has several functions including regulating heart rate, [[allatostatin]] and [[proctolin]] regulate food intake and growth, [[bursicon]] controls tanning of the cuticle and [[corazonin]] has a role in cuticle pigmentation and moulting. == Synthesis == Neuropeptides are synthesized from inactive [[Protein precursor|precursor proteins]] called prepropeptides.<ref name=":3">{{cite book | vauthors = Mains RE, Eipper BA |chapter=The Neuropeptides |chapter-url=https://www.ncbi.nlm.nih.gov/books/NBK28247/ |title=Basic Neurochemistry |date=1999 |publisher=Lippincott-Raven |isbn=978-0-397-51820-3 |edition=6th }}</ref> Prepropeptides contain sequences for a family of distinct peptides and often contain duplicated copies of the same peptides, depending on the organism.<ref name="Evolution of neuropeptide signallin">{{cite journal | vauthors = Elphick MR, Mirabeau O, Larhammar D | title = Evolution of neuropeptide signalling systems | journal = The Journal of Experimental Biology | volume = 221 | issue = Pt 3 | pages = jeb151092 | date = February 2018 | pmid = 29440283 | pmc = 5818035 | doi = 10.1242/jeb.151092 }}</ref> In addition to the precursor peptide sequences, prepropeptides also contain a signal peptide, spacer peptides, and cleavage sites.<ref name=":6">{{Cite web|title=nEUROSTRESSPEP: Insect Neuropeptides|url=http://www.neurostresspep.eu/diner/insectneuropeptides|access-date=2021-08-25|website=www.neurostresspep.eu}}</ref> The signal peptide sequence guides the protein to the secretory pathway, starting at the [[endoplasmic reticulum]]. The signal peptide sequence is removed in the endoplasmic reticulum, yielding a propeptide. The propeptide travels to the [[Golgi apparatus]] where it is proteolytically cleaved and processed into multiple peptides. Peptides are packaged into dense core vesicles, where further cleaving and processing, such as C-terminal amidation, can occur. Dense core vesicles are transported throughout the neuron and can release peptides at the synaptic cleft, cell body, and along the axon.<ref name=":3" /><ref name=":4">{{cite journal | vauthors = Hökfelt T, Bartfai T, Bloom F | title = Neuropeptides: opportunities for drug discovery | journal = The Lancet. Neurology | volume = 2 | issue = 8 | pages = 463–472 | date = August 2003 | pmid = 12878434 | doi = 10.1016/S1474-4422(03)00482-4 | s2cid = 23326450 }}</ref><ref name=":5">{{cite journal | vauthors = Russo AF | title = Overview of Neuropeptides: Awakening the Senses? | journal = Headache | volume = 57 | issue = Suppl 2 | pages = 37–46 | date = May 2017 | pmid = 28485842 | pmc = 5424629 | doi = 10.1111/head.13084 }}</ref><ref name=":1">{{cite journal | vauthors = Nässel DR, Zandawala M | title = Recent advances in neuropeptide signaling in Drosophila, from genes to physiology and behavior | journal = Progress in Neurobiology | volume = 179 | pages = 101607 | date = August 2019 | pmid = 30905728 | doi = 10.1016/j.pneurobio.2019.02.003 | s2cid = 84846652 }}</ref> == Mechanism == Neuropeptides are released by dense core vesicles after [[depolarization]] of the cell. Compared to classical [[neurotransmitter]] signaling, neuropeptide signaling is more sensitive. Neuropeptide receptor affinity is in the nanomolar to micromolar range while neurotransmitter affinity is in the micromolar to millimolar range. Additionally, dense core vesicles contain a small amount of neuropeptide (3 - 10mM) compared to synaptic vesicles containing neurotransmitters (e.g. 100mM for acetylcholine).<ref name=":8">{{Cite book | vauthors = Mains RE, Eipper BA |date=1999 | chapter = The Neuropeptides | chapter-url=https://www.ncbi.nlm.nih.gov/books/NBK28247/ | title = Basic Neurochemistry: Molecular, Cellular and Medical Aspects. 6th edition |publisher=Lippincott-Raven |language=en}}</ref> Evidence shows that neuropeptides are released after high-frequency firing or bursts, distinguishing dense core vesicle from synaptic vesicle release.<ref name=":4" /> Neuropeptides utilize volume transmission and are not reuptaken quickly, allowing diffusion across broad areas (nm to mm) to reach targets. Almost all neuropeptides bind to [[G protein-coupled receptor]]s (GPCRs), inducing second messenger cascades to modulate neural activity on long time-scales.<ref name=":3" /><ref name=":4" /><ref name=":5" /> Expression of neuropeptides in the nervous system is diverse. Neuropeptides are often co-released with other neuropeptides and neurotransmitters, yielding a diversity of effects depending on the combination of release.<ref name=":5" /><ref name=":0" /> For example, [[vasoactive intestinal peptide]] is typically co-released with acetylcholine.<ref name=":9">{{cite journal | vauthors = Dori I, Parnavelas JG | title = The cholinergic innervation of the rat cerebral cortex shows two distinct phases in development | journal = Experimental Brain Research | volume = 76 | issue = 2 | pages = 417–423 | date = July 1989 | pmid = 2767193 | doi = 10.1007/BF00247899 | s2cid = 19504097 }}</ref> Neuropeptide release can also be specific. In ''Drosophila'' larvae, for example, eclosion hormone is expressed in just two neurons.<ref name=":1" /> == Receptor targets == Most neuropeptides act on G-protein coupled receptors (GPCRs). Neuropeptide-GPCRs fall into two families: rhodopsin-like and the secretin class.<ref>{{cite journal | vauthors = Brody T, Cravchik A | title = Drosophila melanogaster G protein-coupled receptors | journal = The Journal of Cell Biology | volume = 150 | issue = 2 | pages = F83–F88 | date = July 2000 | pmid = 10908591 | pmc = 2180217 | doi = 10.1083/jcb.150.2.f83 }}</ref> Most peptides activate a single GPCR, while some activate multiple GPCRs (e.g. AstA, AstC, DTK).<ref name=":0">{{cite journal | vauthors = Nässel DR, Winther AM | title = Drosophila neuropeptides in regulation of physiology and behavior | journal = Progress in Neurobiology | volume = 92 | issue = 1 | pages = 42–104 | date = September 2010 | pmid = 20447440 | doi = 10.1016/j.pneurobio.2010.04.010 | s2cid = 24350305 }}</ref> Peptide-GPCR binding relationships are highly conserved across animals. Aside from conserved structural relationships, some peptide-GPCR functions are also conserved across the animal kingdom. For example, neuropeptide F/neuropeptide Y signaling is structurally and functionally conserved between insects and mammals.<ref name=":0" /> Although peptides mostly target metabotropic receptors, there is some evidence that neuropeptides bind to other receptor targets. Peptide-gated ion channels (FMRFamide-gated sodium channels) have been found in snails and Hydra.<ref>{{cite journal | vauthors = Dürrnagel S, Kuhn A, Tsiairis CD, Williamson M, Kalbacher H, Grimmelikhuijzen CJ, Holstein TW, Gründer S | display-authors = 6 | title = Three homologous subunits form a high affinity peptide-gated ion channel in Hydra | journal = The Journal of Biological Chemistry | volume = 285 | issue = 16 | pages = 11958–11965 | date = April 2010 | pmid = 20159980 | pmc = 2852933 | doi = 10.1074/jbc.M109.059998 | doi-access = free }}</ref> Other examples of non-GPCR targets include: insulin-like peptides and tyrosine-kinase receptors in ''Drosophila'' and atrial natriuretic peptide and eclosion hormone with membrane-bound guanylyl cyclase receptors in mammals and insects.<ref>{{cite journal | vauthors = Chang JC, Yang RB, Adams ME, Lu KH | title = Receptor guanylyl cyclases in Inka cells targeted by eclosion hormone | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 106 | issue = 32 | pages = 13371–13376 | date = August 2009 | pmid = 19666575 | pmc = 2726410 | doi = 10.1073/pnas.0812593106 | doi-access = free | bibcode = 2009PNAS..10613371C }}</ref> == Actions == Due to their modulatory and diffusive nature, neuropeptides can act on multiple time and spatial scales. Below are some examples of neuropeptide actions: === Co-release === Neuropeptides are often co-released with other neurotransmitters and neuropeptides to modulate synaptic activity. [[Synaptic vesicle]]s and dense core vesicles can have differential activation properties for release, resulting in context-dependent co-release combinations.<ref>{{cite journal | vauthors = Nässel DR | title = Substrates for Neuronal Cotransmission With Neuropeptides and Small Molecule Neurotransmitters in ''Drosophila'' | journal = Frontiers in Cellular Neuroscience | volume = 12 | pages = 83 | date = 2018-03-23 | pmid = 29651236 | pmc = 5885757 | doi = 10.3389/fncel.2018.00083 | doi-access = free }}</ref><ref>{{cite journal | vauthors = van den Pol AN | title = Neuropeptide transmission in brain circuits | journal = Neuron | volume = 76 | issue = 1 | pages = 98–115 | date = October 2012 | pmid = 23040809 | pmc = 3918222 | doi = 10.1016/j.neuron.2012.09.014 }}</ref><ref>{{cite journal | vauthors = Nusbaum MP, Blitz DM, Swensen AM, Wood D, Marder E | title = The roles of co-transmission in neural network modulation | language = English | journal = Trends in Neurosciences | volume = 24 | issue = 3 | pages = 146–154 | date = March 2001 | pmid = 11182454 | doi = 10.1016/S0166-2236(00)01723-9 | s2cid = 8994646 }}</ref> For example, insect [[motor neuron]]s are [[glutamatergic]] and some contain dense core vesicles with [[proctolin]]. At low frequency activation, only glutamate is released, yielding fast and rapid excitation of the muscle. At high frequency activation however, dense core vesicles release proctolin, inducing prolonged contractions.<ref>{{cite journal | vauthors = Adams ME, O'Shea M | title = Peptide cotransmitter at a neuromuscular junction | journal = Science | volume = 221 | issue = 4607 | pages = 286–289 | date = July 1983 | pmid = 6134339 | doi = 10.1126/science.6134339 | bibcode = 1983Sci...221..286A }}</ref> Thus, neuropeptide release can be fine-tuned to modulate synaptic activity in certain contexts. Some regions of the nervous system are specialized to release distinctive sets of peptides. For example, the hypothalamus and the pituitary gland release peptides (e.g. TRH, GnRH, CRH, SST) that act as hormones<ref>{{Cite web|title=The Nobel Prize in Physiology or Medicine 1977|url=https://www.nobelprize.org/prizes/medicine/1977/press-release/|access-date=2021-12-15|website=NobelPrize.org|language=en-US}}</ref><ref>{{cite journal | vauthors = Childs GV, Westlund KN, Tibolt RE, Lloyd JM | title = Hypothalamic regulatory peptides and their receptors: cytochemical studies of their role in regulation at the adenohypophyseal level | journal = Journal of Electron Microscopy Technique | volume = 19 | issue = 1 | pages = 21–41 | date = September 1991 | pmid = 1660066 | doi = 10.1002/jemt.1060190104 }}</ref> In one subpoplation of the [[arcuate nucleus]] of the [[hypothalamus]], three [[anorectic]] peptides are co-expressed: [[α-melanocyte-stimulating hormone]] (α-MSH), [[galanin-like peptide]], and [[cocaine-and-amphetamine-regulated transcript]] (CART), and in another subpopulation two [[orexigenic]] peptides are co-expressed, [[neuropeptide Y]] and [[agouti-related peptide]] (AGRP).<ref>{{cite journal | vauthors = Lau J, Farzi A, Qi Y, Heilbronn R, Mietzsch M, Shi YC, Herzog H | title = CART neurons in the arcuate nucleus and lateral hypothalamic area exert differential controls on energy homeostasis | journal = Molecular Metabolism | volume = 7 | pages = 102–118 | date = January 2018 | pmid = 29146410 | pmc = 5784325 | doi = 10.1016/j.molmet.2017.10.015 }}</ref> These peptides are all released in different combinations to signal hunger and satiation cues.<ref>{{cite journal | vauthors = Luckman SM, Lawrence CB | title = Anorectic brainstem peptides: more pieces to the puzzle | journal = Trends in Endocrinology and Metabolism | volume = 14 | issue = 2 | pages = 60–65 | date = March 2003 | pmid = 12591175 | doi = 10.1016/S1043-2760(02)00033-4 | s2cid = 25055675 }}</ref> The following is a list of neuroactive peptides co-released with other neurotransmitters. Transmitter names are shown in bold. '''[[Norepinephrine]]''' (noradrenaline). In neurons of the A2 cell group in the [[nucleus of the solitary tract]]), norepinephrine co-exists with: * [[Galanin]] * [[Enkephalin]] * [[Neuropeptide Y]] '''[[gamma-Aminobutyric acid|GABA]]''' * [[Somatostatin]] (in the [[hippocampus]]) * [[Cholecystokinin]] * [[Neuropeptide Y]] (in the [[arcuate nucleus]]) '''[[Acetylcholine]]''' * [[Vasoactive intestinal peptide|VIP]] * [[Substance P]] '''[[Dopamine]]''' * [[Cholecystokinin]] * [[Neurotensin]] * [[Glucagon-like peptide-1]] (in the [[nucleus accumbens]]) '''[[Epinephrine]]''' (adrenaline) * [[Neuropeptide Y]] * [[Neurotensin]] '''[[Serotonin]]''' (5-HT) * [[Substance P]] * [[Thyrotropin-releasing hormone|TRH]] * [[Enkephalin]] Some neurons make several different peptides. For instance, [[vasopressin]] co-exists with [[dynorphin]] and [[galanin]] in magnocellular neurons of the [[supraoptic nucleus]] and [[paraventricular nucleus]], and with [[Corticotropin-releasing hormone|CRF]] (in parvocellular neurons of the [[paraventricular nucleus]]) [[Oxytocin]] in the [[supraoptic nucleus]] co-exists with [[enkephalin]], [[dynorphin]], [[cocaine-and amphetamine regulated transcript]] (CART) and [[cholecystokinin]]. == Evolution of Neuropeptide Signaling == [[Peptide]]s are ancient signaling systems that are found in almost all animals on Earth.<ref name=":2">{{cite journal | vauthors = Schoofs L, De Loof A, Van Hiel MB | title = Neuropeptides as Regulators of Behavior in Insects | journal = Annual Review of Entomology | volume = 62 | pages = 35–52 | date = January 2017 | pmid = 27813667 | doi = 10.1146/annurev-ento-031616-035500 | url = https://lirias.kuleuven.be/handle/123456789/632231 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Jékely G | title = The chemical brain hypothesis for the origin of nervous systems | journal = Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences | volume = 376 | issue = 1821 | pages = 20190761 | date = March 2021 | pmid = 33550946 | doi = 10.1098/rstb.2019.0761 | pmc = 7935135 }}</ref> Genome sequencing reveals evidence of neuropeptide genes in [[Cnidaria]], [[Ctenophora]], and [[Placozoa]], some of oldest living animals with nervous systems or neural-like tissues.<ref>{{cite journal | vauthors = Sachkova MY, Nordmann EL, Soto-Àngel JJ, Meeda Y, Górski B, Naumann B, Dondorp D, Chatzigeorgiou M, Kittelmann M, Burkhardt P | display-authors = 6 | title = Neuropeptide repertoire and 3D anatomy of the ctenophore nervous system | journal = Current Biology | volume = 31 | issue = 23 | pages = 5274–5285.e6 | date = December 2021 | pmid = 34587474 | doi = 10.1016/j.cub.2021.09.005 | s2cid = 238210404 | doi-access = free | bibcode = 2021CBio...31E5274S }}</ref><ref>{{cite journal | vauthors = Takahashi T, Takeda N | title = Insight into the molecular and functional diversity of cnidarian neuropeptides | journal = International Journal of Molecular Sciences | volume = 16 | issue = 2 | pages = 2610–2625 | date = January 2015 | pmid = 25625515 | pmc = 4346854 | doi = 10.3390/ijms16022610 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Mirabeau O, Joly JS | title = Molecular evolution of peptidergic signaling systems in bilaterians | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 110 | issue = 22 | pages = E2028–E2037 | date = May 2013 | pmid = 23671109 | pmc = 3670399 | doi = 10.1073/pnas.1219956110 | bibcode = 2013PNAS..110E2028M | doi-access = free }}</ref><ref name="Evolution of neuropeptide signallin"/> Recent studies also show genomic evidence of neuropeptide processing machinery in metazoans and [[choanoflagellate]]s, suggesting that neuropeptide signaling may predate the development of nervous tissues.<ref>{{cite journal | vauthors = Yañez-Guerra LA, Thiel D, Jékely G | title = Premetazoan Origin of Neuropeptide Signaling | journal = Molecular Biology and Evolution | volume = 39 | issue = 4 | pages = msac051 | date = April 2022 | pmid = 35277960 | doi = 10.1093/molbev/msac051 | pmc = 9004410 }}</ref> Additionally, [[Ctenophora|Ctenophore]] and [[Placozoa]] neural signaling is entirely peptidergic and lacks the major amine [[neurotransmitter]]s such as acetylcholine, dopamine, and serotonin.<ref>{{cite journal | vauthors = Varoqueaux F, Williams EA, Grandemange S, Truscello L, Kamm K, Schierwater B, Jékely G, Fasshauer D | display-authors = 6 | title = High Cell Diversity and Complex Peptidergic Signaling Underlie Placozoan Behavior | journal = Current Biology | volume = 28 | issue = 21 | pages = 3495–3501.e2 | date = November 2018 | pmid = 30344118 | doi = 10.1016/j.cub.2018.08.067 | s2cid = 53044824 | doi-access = free | bibcode = 2018CBio...28E3495V }}</ref><ref name=":2" /> This also suggests that neuropeptide signaling developed before amine neurotransmitters. == Research history == In the early 1900s, chemical messengers were crudely extracted from whole animal brains and tissues and studied for their physiological effects. In 1931, von Euler and Gaddum, used a similar method to try and isolate acetylcholine but instead discovered a peptide substance that induced physiological changes including muscle contractions and depressed blood pressure. These effects were not abolished using atropine, ruling out the substance as acetylcholine. <ref name=":7">{{cite journal |vauthors=V Euler US, Gaddum JH |date=June 1931 |title=An unidentified depressor substance in certain tissue extracts |journal=The Journal of Physiology |volume=72 |issue=1 |pages=74–87 |doi=10.1113/jphysiol.1931.sp002763 |pmc=1403098 |pmid=16994201}}</ref><ref name=":9" /> In insects, [[proctolin]] was the first neuropeptide to be isolated and sequenced.<ref>{{cite book |doi=10.1016/B978-012369442-3/50030-1 |chapter=Proctolin in Insects |title=Handbook of Biologically Active Peptides |year=2006 | vauthors = Lange AB, Orchard I |pages=177–181 |isbn=9780123694423 }}</ref><ref>{{cite journal | vauthors = Starratt AN, Brown BE | title = Structure of the pentapeptide proctolin, a proposed neurotransmitter in insects | journal = Life Sciences | volume = 17 | issue = 8 | pages = 1253–1256 | date = October 1975 | pmid = 576 | doi = 10.1016/0024-3205(75)90134-4 }}</ref> In 1975, Alvin Starratt and Brian Brown extracted the peptide from hindgut muscles of the cockroach and found that its application enhanced muscle contractions. While Starratt and Brown initially thought of proctolin as an excitatory neurotransmitter, proctolin was later confirmed as a neuromodulatory peptide.<ref>{{cite book |doi=10.1016/B978-0-12-801028-0.00067-2 |chapter=Proctolin |title=Handbook of Hormones |year=2016 | vauthors = Tanaka Y |isbn=9780128010280 }}</ref> [[David de Wied]] first used the term "neuropeptide" in the 1970s to delineate peptides derived from the nervous system.<ref name=":6" /><ref name=":8" /> == References == {{reflist}} == External links == {{commons}} {{wiktionary|neuropeptide}} * [https://www.journals.elsevier.com/neuropeptides ''Neuropeptides'' Journal] * [http://isyslab.info/NeuroPep/ Neuropeptides reference website (a comprehensive neuropeptide database)] * [http://www.morganclaypool.com/toc/npe/1/1 ''Neuropeptides'' eBook series] * [http://www.wormbook.org/chapters/www_neuropeptides/neuropeptides.html Neuropeptide chapter in the C. elegans Wormbook] excellent, and very accessible, discussion of 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