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Somatostatin
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<h2 id="nomenclature">Nomenclature</h2> <p>Synonyms of "somatostatin" include: </p> <ul><li>growth hormone–inhibiting hormone (GHIH)</li> <li>growth hormone release–inhibiting hormone (GHRIH)</li> <li>somatotropin release–inhibiting factor (SRIF)</li> <li>somatotropin release–inhibiting hormone (SRIH)</li></ul> <h2 id="production">Production</h2> <h3>Digestive system</h3> <p>Somatostatin is secreted by <a href="/facts/Delta_cells/dS2tDQVx">delta cells</a> at several locations in the digestive system, namely the <a href="/facts/Pyloric_antrum/920mWuBz">pyloric antrum</a>, the <a href="/facts/Duodenum/IAIgHBmq">duodenum</a> and the <a href="/facts/Pancreatic_islets/PJVtM7MY">pancreatic islets</a>.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> </p><p>Somatostatin released in the <a href="/facts/Pyloric_antrum/920mWuBz">pyloric antrum</a> travels via the portal venous system to the heart, then enters the systemic circulation to reach the locations where it will exert its inhibitory effects. In addition, somatostatin release from delta cells can act in a <a href="/facts/Paracrine/V8eVwG9z">paracrine</a> manner.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> </p><p>In the stomach, somatostatin acts directly on the acid-producing <a href="/facts/Parietal_cells/jS1nXJnw">parietal cells</a> via a G-protein coupled receptor (which inhibits adenylate cyclase, thus effectively antagonising the stimulatory effect of histamine) to reduce acid secretion.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> Somatostatin can also indirectly decrease stomach acid production by preventing the release of other hormones, including <a href="/facts/Gastrin/C4a4VSbz">gastrin</a> and <a href="/facts/Histamine/Vfjda665">histamine</a> which effectively slows down the digestive process. </p> <h3>Brain</h3> <table><tbody><tr><td></td><td></td></tr></tbody></table> <p>Somatostatin is produced by <a href="/facts/Neuroendocrine/7GVp7Gn9">neuroendocrine</a> neurons of the <a href="/facts/Ventromedial_nucleus/KDqI7zcx">ventromedial nucleus</a> of the <a href="/facts/Hypothalamus/lCkNt1bM">hypothalamus</a>. These neurons project to the <a href="/facts/Median_eminence/99rzqoG8">median eminence</a>, where somatostatin is released from neurosecretory nerve endings into the <a href="/facts/Hypophyseal_portal_system/gNpabWYT">hypothalamohypophysial system</a> through neuron axons. Somatostatin is then carried to the <a href="/facts/Anterior_pituitary_gland/uUj4jzRq">anterior pituitary gland</a>, where it inhibits the secretion of <a href="/facts/Growth_hormone/SLEJ1fws">growth hormone</a> from <a href="/facts/Somatotrope/05Vx6XyG">somatotrope</a> cells. The somatostatin neurons in the periventricular nucleus mediate negative feedback effects of <a href="/facts/Growth_hormone/SLEJ1fws">growth hormone</a> on its own release; the somatostatin neurons respond to high circulating concentrations of growth hormone and somatomedins by increasing the release of somatostatin, so reducing the rate of secretion of growth hormone. </p><p>Somatostatin is also produced by several other populations that project centrally, i.e., to other areas of the brain, and somatostatin receptors are expressed at many different sites in the brain. In particular, populations of somatostatin neurons occur in the <a href="/facts/Arcuate_nucleus/lnbnpPtW">arcuate nucleus</a>,<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> the <a href="/facts/Hippocampus/X7CqbP8X">hippocampus</a>,<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> and the brainstem <a href="/facts/Nucleus_of_the_solitary_tract/Y4dywjvH">nucleus of the solitary tract</a>. </p> <h2 id="functions">Functions</h2> <p>Somatostatin is classified as an <a href="/facts/Inhibitory/Jfm13Wkn">inhibitory</a> hormone,<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> and is induced by low pH. Its actions are spread to different parts of the body. Somatostatin release is inhibited by the <a href="/facts/Vagus_nerve/cKQR0rLm">vagus nerve</a>.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a> </p> <h3>Anterior pituitary</h3> <p>In the <a href="/facts/Anterior_pituitary_gland/uUj4jzRq">anterior pituitary gland</a>,the virulent strain on the endocrine disrupting effects of somatostatin are: </p> <ul><li>Inhibiting the release of growth hormone (GH)<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a> (thus opposing the effects of <a href="/facts/Growth_hormone%E2%80%93releasing_hormone/CMbSE1PE">growth hormone–releasing hormone</a> (GHRH))</li> <li>Inhibiting the release of <a href="/facts/Thyroid-stimulating_hormone/w8ettSpY">thyroid-stimulating hormone</a> (TSH)<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a></li> <li>Inhibiting <a href="/facts/Adenylyl_cyclase/WnCSuV96">adenylyl cyclase</a> in parietal cells</li> <li>Inhibiting the release of <a href="/facts/Prolactin/NcdqrzFU">prolactin</a> (PRL)</li></ul> <h3>Gastrointestinal system</h3> <ul><li>Somatostatin is homologous with <a href="/facts/CORT/neerB06Y">cortistatin</a> (see <a href="/facts/Somatostatin_family/xoAHQkdE">somatostatin family</a>) and suppresses the release of <a href="/facts/Gastrointestinal_hormone/FM8hM78n">gastrointestinal hormones</a></li> <li>Decreases the rate of gastric emptying, and reduces smooth muscle contractions and blood flow within the intestine<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a></li> <li>Suppresses the release of pancreatic hormones <ul><li>Somatostatin release is triggered by the beta cell peptide urocortin3 (Ucn3) to inhibit <a href="/facts/Insulin/oXG0myt1">insulin</a> release.<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a><a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a></li> <li>Inhibits the release of glucagon<a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a><a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a></li></ul></li> <li>Suppresses the exocrine secretory action of the pancreas</li></ul> <h2 id="synthetic-substitutes">Synthetic substitutes</h2> <p><a href="/facts/Octreotide/A7su7kgD">Octreotide</a> (brand name Sandostatin, <a href="/facts/Novartis/jDregKez">Novartis Pharmaceuticals</a>) is an <a href="/facts/Peptide/C4ltc7UG">octapeptide</a> that mimics natural somatostatin pharmacologically, though is a more potent inhibitor of growth hormone, glucagon, and insulin than the natural hormone, and has a much longer <a href="/facts/Half-life/kGVH8BAB">half-life</a> (about 90 minutes, compared to 2–3 minutes for somatostatin). Since it is absorbed poorly from the gut, it is administered parenterally (subcutaneously, intramuscularly, or intravenously). It is indicated for <a href="/facts/Symptomatic_treatment/zQlnUC9x">symptomatic treatment</a> of <a href="/facts/Carcinoid_syndrome/wtu2tTjM">carcinoid syndrome</a> and <a href="/facts/Acromegaly/caqcbMmM">acromegaly</a>.<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a><a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a> It is also finding increased use in polycystic diseases of the liver and kidney. </p><p><a href="/facts/Lanreotide/CWaLcGN9">Lanreotide</a> (Somatuline, <a href="/facts/Ipsen/0bKHWlUx">Ipsen Pharmaceuticals</a>) is a medication used in the management of acromegaly and symptoms caused by neuroendocrine tumors, most notably carcinoid syndrome. It is a long-acting <a href="/facts/Structural_analog/3aysWSVG">analog</a> of somatostatin, like octreotide. It is available in several countries, including the United Kingdom, Australia, and Canada, and was approved for sale in the United States by the Food and Drug Administration on August 30, 2007. </p><p><a href="/facts/Pasireotide/MlycKY4l">Pasireotide</a>, sold under the brand name Signifor, is an <a href="/facts/Orphan_drug/96judAS6">orphan drug</a> approved in the United States and the European Union for the treatment of <a href="/facts/Cushing%27s_disease/HqfLkI5J">Cushing's disease</a> in patients who fail or are ineligible for surgical therapy. It was developed by <a href="/facts/Novartis/jDregKez">Novartis</a>. Pasireotide is somatostatin <a href="/facts/Analog_(chemistry)/3aysWSVG">analog</a> with a 40-fold increased affinity to <a href="/facts/Somatostatin_receptor_5/07mWKuo5">somatostatin receptor 5</a> compared to other somatostatin analogs. </p> <h2 id="evolutionary-history">Evolutionary history</h2> <p>Six somatostatin genes have been discovered in <a href="/facts/Vertebrates/tT54FSTT">vertebrates</a>. The current proposed history as to how these six genes arose is based on the three whole-genome duplication events that took place in vertebrate evolution along with local duplications in <a href="/facts/Teleost/1YULPGW5">teleost</a> fish. An ancestral somatostatin gene was duplicated during the first whole-genome duplication event (1R) to create <i>SS1</i> and <i>SS2</i>. These two genes were duplicated during the second whole-genome duplication event (2R) to create four new somatostatin genes:<i>SS1, SS2, SS3</i>, and one gene that was lost during the evolution of vertebrates. <a href="/facts/Tetrapods/vWpAxzAW">Tetrapods</a> retained <i>SS1</i> (also known as <i>SS-14</i> and <i>SS-28</i>) and <i>SS2</i> (also known as <a href="/facts/Cortistatin_(neuropeptide)/neerB06Y">cortistatin</a>) after the split in the <a href="/facts/Sarcopterygii/7Glajr07">Sarcopterygii</a> and <a href="/facts/Actinopterygii/3PNaXXmJ">Actinopterygii</a> lineage split. In <a href="/facts/Teleost/1YULPGW5">teleost</a> fish, <i>SS1, SS2</i>, and <i>SS3</i> were duplicated during the third whole-genome duplication event (3R) to create <i>SS1, SS2, SS4, SS5,</i> and two genes that were lost during the evolution of teleost fish. <i>SS1</i> and <i>SS2</i> went through local duplications to give rise to <i>SS6</i> and <i>SS3</i>.<a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a> </p> <h2 id="see-also">See also</h2> <ul><li>FK962</li> <li><a href="/facts/Hypothalamic%E2%80%93pituitary%E2%80%93somatic_axis/0GoSBl18">Hypothalamic–pituitary–somatic axis</a></li> <li><a href="/facts/Octreotide/A7su7kgD">Octreotide</a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Florio T, Schettini G (September 2001). "[Somatostatin and its receptors. Role in the control of cell proliferation]". <i>Minerva Endocrinologica</i>. 26 (3): 91–102. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11753230">11753230</a>.</li> <li>Yamada Y, Reisine T, Law SF, Ihara Y, Kubota A, Kagimoto S, et al. (December 1992). <a href="https://doi.org/10.1210%2Fmend.6.12.1337145">"Somatostatin receptors, an expanding gene family: cloning and functional characterization of human SSTR3, a protein coupled to adenylyl cyclase"</a>. <i>Molecular Endocrinology</i>. 6 (12): 2136–42. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1210%2Fmend.6.12.1337145">10.1210/mend.6.12.1337145</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1337145">1337145</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:28499704">28499704</a>.</li> <li>Yamada Y, Post SR, Wang K, Tager HS, Bell GI, Seino S (January 1992). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC48214">"Cloning and functional characterization of a family of human and mouse somatostatin receptors expressed in brain, gastrointestinal tract, and kidney"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 89 (1): 251–5. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1992PNAS...89..251Y">1992PNAS...89..251Y</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.89.1.251">10.1073/pnas.89.1.251</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC48214">48214</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1346068">1346068</a>.</li> <li>Brazeau P, Vale W, Burgus R, Ling N, Butcher M, Rivier J, et al. (January 1973). "Hypothalamic polypeptide that inhibits the secretion of immunoreactive pituitary growth hormone". <i>Science</i>. 179 (4068): 77–9. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1973Sci...179...77B">1973Sci...179...77B</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1126%2Fscience.179.4068.77">10.1126/science.179.4068.77</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/4682131">4682131</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:10997771">10997771</a>.</li> <li>Shen LP, Pictet RL, Rutter WJ (August 1982). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC346717">"Human somatostatin I: sequence of the cDNA"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 79 (15): 4575–9. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1982PNAS...79.4575S">1982PNAS...79.4575S</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.79.15.4575">10.1073/pnas.79.15.4575</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC346717">346717</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/6126875">6126875</a>.</li> <li>Shen LP, Rutter WJ (April 1984). "Sequence of the human somatostatin I gene". <i>Science</i>. 224 (4645): 168–71. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1984Sci...224..168S">1984Sci...224..168S</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1126%2Fscience.6142531">10.1126/science.6142531</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/6142531">6142531</a>.</li> <li>Montminy MR, Goodman RH, Horovitch SJ, Habener JF (June 1984). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC345502">"Primary structure of the gene encoding rat preprosomatostatin"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 81 (11): 3337–40. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1984PNAS...81.3337M">1984PNAS...81.3337M</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.81.11.3337">10.1073/pnas.81.11.3337</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC345502">345502</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/6145156">6145156</a>.</li> <li>Zabel BU, Naylor SL, Sakaguchi AY, Bell GI, Shows TB (November 1983). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC390100">"High-resolution chromosomal localization of human genes for amylase, proopiomelanocortin, somatostatin, and a DNA fragment (D3S1) by in situ hybridization"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 80 (22): 6932–6. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1983PNAS...80.6932Z">1983PNAS...80.6932Z</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.80.22.6932">10.1073/pnas.80.22.6932</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC390100">390100</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/6196780">6196780</a>.</li> <li>Panetta R, Greenwood MT, Warszynska A, Demchyshyn LL, Day R, Niznik HB, et al. (March 1994). "Molecular cloning, functional characterization, and chromosomal localization of a human somatostatin receptor (somatostatin receptor type 5) with preferential affinity for somatostatin-28". <i>Molecular Pharmacology</i>. 45 (3): 417–27. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7908405">7908405</a>.</li> <li>Demchyshyn LL, Srikant CB, Sunahara RK, Kent G, Seeman P, Van Tol HH, et al. (June 1993). "Cloning and expression of a human somatostatin-14-selective receptor variant (somatostatin receptor 4) located on chromosome 20". <i>Molecular Pharmacology</i>. 43 (6): 894–901. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8100352">8100352</a>.</li> <li>Kaupmann K, Bruns C, Hoyer D, Seuwen K, Lübbert H (September 1993). <a href="https://doi.org/10.1016%2F0014-5793%2893%2980296-7">"Distribution and second messenger coupling of four somatostatin receptor subtypes expressed in brain"</a>. <i>FEBS Letters</i>. 331 (1–2): 53–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0014-5793%2893%2980296-7">10.1016/0014-5793(93)80296-7</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8405411">8405411</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:22557713">22557713</a>.</li> <li>Aguila MC, Rodriguez AM, Aguila-Mansilla HN, Lee WT (May 1996). <a href="https://doi.org/10.1210%2Fendo.137.5.8612489">"Somatostatin antisense oligodeoxynucleotide-mediated stimulation of lymphocyte proliferation in culture"</a>. <i>Endocrinology</i>. 137 (5): 1585–90. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1210%2Fendo.137.5.8612489">10.1210/endo.137.5.8612489</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8612489">8612489</a>.</li> <li>Sharma K, Patel YC, Srikant CB (December 1996). <a href="https://doi.org/10.1210%2Fmend.10.12.8961277">"Subtype-selective induction of wild-type p53 and apoptosis, but not cell cycle arrest, by human somatostatin receptor 3"</a>. <i>Molecular Endocrinology</i>. 10 (12): 1688–96. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1210%2Fmend.10.12.8961277">10.1210/mend.10.12.8961277</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8961277">8961277</a>.</li> <li>Dournaud P, Boudin H, Schonbrunn A, Tannenbaum GS, Beaudet A (February 1998). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6792775">"Interrelationships between somatostatin sst2A receptors and somatostatin-containing axons in rat brain: evidence for regulation of cell surface receptors by endogenous somatostatin"</a>. <i>The Journal of Neuroscience</i>. 18 (3): 1056–71. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1523%2FJNEUROSCI.18-03-01056.1998">10.1523/JNEUROSCI.18-03-01056.1998</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6792775">6792775</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9437026">9437026</a>.</li> <li>Barnea A, Roberts J, Ho RH (January 1999). "Evidence for a synergistic effect of the HIV-1 envelope protein gp120 and brain-derived neurotrophic factor (BDNF) leading to enhanced expression of somatostatin neurons in aggregate cultures derived from the human fetal cortex". <i>Brain Research</i>. 815 (2): 349–57. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0006-8993%2898%2901098-1">10.1016/S0006-8993(98)01098-1</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9878821">9878821</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:21793593">21793593</a>.</li> <li>Ferone D, van Hagen PM, van Koetsveld PM, Zuijderwijk J, Mooy DM, Lichtenauer-Kaligis EG, et al. (January 1999). <a href="https://doi.org/10.1210%2Fendo.140.1.6398">"In vitro characterization of somatostatin receptors in the human thymus and effects of somatostatin and octreotide on cultured thymic epithelial cells"</a>. <i>Endocrinology</i>. 140 (1): 373–80. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1210%2Fendo.140.1.6398">10.1210/endo.140.1.6398</a>. <a href="/facts/Hdl_(identifier)/rdebSxmC">hdl</a>:<a href="https://hdl.handle.net/1765%2F8996">1765/8996</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9886848">9886848</a>.</li> <li>Brakch N, Lazar N, Panchal M, Allemandou F, Boileau G, Cohen P, et al. (February 2002). "The somatostatin-28(1-12)-NPAMAP sequence: an essential helical-promoting motif governing prosomatostatin processing at mono- and dibasic sites". <i>Biochemistry</i>. 41 (5): 1630–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1021%2Fbi011928m">10.1021/bi011928m</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11814357">11814357</a>.</li> <li>Oomen SP, van Hennik PB, Antonissen C, Lichtenauer-Kaligis EG, Hofland LJ, Lamberts SW, et al. (February 2002). <a href="https://doi.org/10.1016%2FS0301-472X%2801%2900772-X">"Somatostatin is a selective chemoattractant for primitive (CD34(+)) hematopoietic progenitor cells"</a>. <i>Experimental Hematology</i>. 30 (2): 116–25. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0301-472X%2801%2900772-X">10.1016/S0301-472X(01)00772-X</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11823046">11823046</a>.</li> <li>Simonetti M, Di BC (February 2002). "Structural motifs in the maturation process of peptide hormones. The somatostatin precursor. I. A CD conformational study". <i>Journal of Peptide Science</i>. 8 (2): 66–79. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fpsc.370">10.1002/psc.370</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11860030">11860030</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:20438890">20438890</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li>Overview of all the structural information available in the <a href="/facts/Protein_Data_Bank/oUhq4ABD">PDB</a> for <a href="/facts/UniProt/lfDDHjAl">UniProt</a>: <i><a href="https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P61278">P61278</a></i> (Somatostatin) at the <a href="/facts/PDBe-KB/p1WX7lPH">PDBe-KB</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>"somatostatin". Encyclopædia Britannica. Encyclopædia Britannica Online. Encyclopædia Britannica Inc., 2016. Web. 04 mag. 2016 <http://www.britannica.com/science/somatostatin>. <a href="http://www.britannica.com/science/somatostatin" target="_blank">http://www.britannica.com/science/somatostatin</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Nelson DL, Cox M, Hoskins AA (2021). Lehninger Principles of Biochemistry (Eighth ed.). New York, NY: Macmillan Learning. ISBN 978-1-319-22800-2. OCLC 1243000176. The binding of somatostatin to its receptor in the pancreas leads to activation of an inhibitory G protein, or Gi, structurally homologous to Gs, that inhibits adenylyl cyclase and lowers [cAMP]. In this way, somatostatin inhibits the secretion of several hormones, including glucagon <a href="978-1-319-22800-2" target="_blank">978-1-319-22800-2</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Costoff A. "Sect. 5, Ch. 4: Structure, Synthesis, and Secretion of Somatostatin". Endocrinology: The Endocrine Pancreas. Medical College of Georgia. p. 16. Archived from the original on April 5, 2008. Retrieved 2008-02-19. <a href="https://web.archive.org/web/20080405060426/http://www.lib.mcg.edu/edu/eshuphysio/program/section5/5ch4/s5ch4_16.htm" target="_blank">https://web.archive.org/web/20080405060426/http://www.lib.mcg.edu/edu/eshuphysio/program/section5/5ch4/s5ch4_16.htm</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>"somatostatin preproprotein [Homo sapiens]". NCBI Reference Sequence. National Center for Biotechnology Information Support Center (NCBI). <a href="https://www.ncbi.nlm.nih.gov/protein/NP_001039" target="_blank">https://www.ncbi.nlm.nih.gov/protein/NP_001039</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Liu Y, Lu D, Zhang Y, Li S, Liu X, Lin H (September 2010). "The evolution of somatostatin in vertebrates". Gene. 463 (1–2): 21–8. doi:10.1016/j.gene.2010.04.016. PMID 20472043. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Liu Y, Lu D, Zhang Y, Li S, Liu X, Lin H (September 2010). "The evolution of somatostatin in vertebrates". Gene. 463 (1–2): 21–8. doi:10.1016/j.gene.2010.04.016. PMID 20472043. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Gahete MD, Cordoba-Chacón J, Duran-Prado M, Malagón MM, Martinez-Fuentes AJ, Gracia-Navarro F, et al. (July 2010). "Somatostatin and its receptors from fish to mammals". Annals of the New York Academy of Sciences. 1200 (1): 43–52. Bibcode:2010NYASA1200...43G. doi:10.1111/j.1749-6632.2010.05511.x. PMID 20633132. S2CID 23346102. <a href="https://zenodo.org/record/1450988" target="_blank">https://zenodo.org/record/1450988</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>"Entrez Gene: Somatostatin". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=6750" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=6750</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Shen LP, Pictet RL, Rutter WJ (August 1982). "Human somatostatin I: sequence of the cDNA". Proceedings of the National Academy of Sciences of the United States of America. 79 (15): 4575–9. Bibcode:1982PNAS...79.4575S. doi:10.1073/pnas.79.15.4575. PMC 346717. PMID 6126875. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC346717" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC346717</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Shen LP, Rutter WJ (April 1984). "Sequence of the human somatostatin I gene". Science. 224 (4645): 168–71. Bibcode:1984Sci...224..168S. doi:10.1126/science.6142531. PMID 6142531. <a href="/wiki/Bibcode_(identifier)" target="_blank">/wiki/Bibcode_(identifier)</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Boron WF, Boulpaep EL (2012). Medical Physiology (2nd ed.). Philadelphia, PA: Elsevier. ISBN 9781437717532. <a href="9781437717532" target="_blank">9781437717532</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> <li id="fn:12"><p>Boron WF, Boulpaep EL (2012). Medical Physiology (2nd ed.). Philadelphia, PA: Elsevier. ISBN 9781437717532. <a href="9781437717532" target="_blank">9781437717532</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li> <li id="fn:13"><p>Boron WF, Boulpaep EL (2012). Medical Physiology (2nd ed.). Philadelphia, PA: Elsevier. ISBN 9781437717532. <a href="9781437717532" target="_blank">9781437717532</a> <a href="#fnref:13" class="footnote-back-ref">↩</a></p></li> <li id="fn:14"><p>Minami S, Kamegai J, Sugihara H, Suzuki N, Wakabayashi I (April 1998). "Growth hormone inhibits its own secretion by acting on the hypothalamus through its receptors on neuropeptide Y neurons in the arcuate nucleus and somatostatin neurons in the periventricular nucleus". Endocrine Journal. 45 (Suppl): S19 – S26. doi:10.1507/endocrj.45.Suppl_S19. PMID 9790225. <a href="https://doi.org/10.1507%2Fendocrj.45.Suppl_S19" target="_blank">https://doi.org/10.1507%2Fendocrj.45.Suppl_S19</a> <a href="#fnref:14" class="footnote-back-ref">↩</a></p></li> <li id="fn:15"><p>Stefanelli T, Bertollini C, Lüscher C, Muller D, Mendez P (March 2016). "Hippocampal Somatostatin Interneurons Control the Size of Neuronal Memory Ensembles". Neuron. 89 (5): 1074–1085. doi:10.1016/j.neuron.2016.01.024. PMID 26875623. <a href="https://doi.org/10.1016%2Fj.neuron.2016.01.024" target="_blank">https://doi.org/10.1016%2Fj.neuron.2016.01.024</a> <a href="#fnref:15" class="footnote-back-ref">↩</a></p></li> <li id="fn:16"><p>Costoff A. "Sect. 5, Ch. 4: Structure, Synthesis, and Secretion of Somatostatin". Endocrinology: The Endocrine Pancreas. Medical College of Georgia. p. 16. Archived from the original on April 5, 2008. Retrieved 2008-02-19. <a href="https://web.archive.org/web/20080405060426/http://www.lib.mcg.edu/edu/eshuphysio/program/section5/5ch4/s5ch4_16.htm" target="_blank">https://web.archive.org/web/20080405060426/http://www.lib.mcg.edu/edu/eshuphysio/program/section5/5ch4/s5ch4_16.htm</a> <a href="#fnref:16" class="footnote-back-ref">↩</a></p></li> <li id="fn:17"><p>Holst JJ, Skak-Nielsen T, Orskov C, Seier-Poulsen S (August 1992). "Vagal control of the release of somatostatin, vasoactive intestinal polypeptide, gastrin-releasing peptide, and HCl from porcine non-antral stomach". Scandinavian Journal of Gastroenterology. 27 (8): 677–85. doi:10.3109/00365529209000139. PMID 1359631. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:17" class="footnote-back-ref">↩</a></p></li> <li id="fn:18"><p>Bowen R (2002-12-14). "Somatostatin". Biomedical Hypertextbooks. Colorado State University. Retrieved 2008-02-19. <a href="http://www.vivo.colostate.edu/hbooks/pathphys/endocrine/otherendo/somatostatin.html" target="_blank">http://www.vivo.colostate.edu/hbooks/pathphys/endocrine/otherendo/somatostatin.html</a> <a href="#fnref:18" class="footnote-back-ref">↩</a></p></li> <li id="fn:19"><p>First Aid for the USMLE Step 1, 2010. Page 286. <a href="#fnref:19" class="footnote-back-ref">↩</a></p></li> <li id="fn:20"><p>Bowen R (2002-12-14). "Somatostatin". Biomedical Hypertextbooks. Colorado State University. Retrieved 2008-02-19. <a href="http://www.vivo.colostate.edu/hbooks/pathphys/endocrine/otherendo/somatostatin.html" target="_blank">http://www.vivo.colostate.edu/hbooks/pathphys/endocrine/otherendo/somatostatin.html</a> <a href="#fnref:20" class="footnote-back-ref">↩</a></p></li> <li id="fn:21"><p>Costoff A. "Sect. 5, Ch. 4: Structure, Synthesis, and Secretion of Somatostatin". Endocrinology: The Endocrine Pancreas. Medical College of Georgia. p. 17. Archived from the original on March 31, 2008. Retrieved 2008-02-19. <a href="https://web.archive.org/web/20080331235236/http://www.lib.mcg.edu/edu/eshuphysio/program/section5/5ch4/s5ch4_17.htm" target="_blank">https://web.archive.org/web/20080331235236/http://www.lib.mcg.edu/edu/eshuphysio/program/section5/5ch4/s5ch4_17.htm</a> <a href="#fnref:21" class="footnote-back-ref">↩</a></p></li> <li id="fn:22"><p>van der Meulen T, Donaldson CJ, Cáceres E, Hunter AE, Cowing-Zitron C, Pound LD, et al. (July 2015). "Urocortin3 mediates somatostatin-dependent negative feedback control of insulin secretion". Nature Medicine. 21 (7): 769–76. doi:10.1038/nm.3872. PMC 4496282. PMID 26076035. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4496282" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4496282</a> <a href="#fnref:22" class="footnote-back-ref">↩</a></p></li> <li id="fn:23"><p>Costoff A. "Sect. 5, Ch. 4: Structure, Synthesis, and Secretion of Somatostatin". Endocrinology: The Endocrine Pancreas. Medical College of Georgia. p. 17. Archived from the original on March 31, 2008. Retrieved 2008-02-19. <a href="https://web.archive.org/web/20080331235236/http://www.lib.mcg.edu/edu/eshuphysio/program/section5/5ch4/s5ch4_17.htm" target="_blank">https://web.archive.org/web/20080331235236/http://www.lib.mcg.edu/edu/eshuphysio/program/section5/5ch4/s5ch4_17.htm</a> <a href="#fnref:23" class="footnote-back-ref">↩</a></p></li> <li id="fn:24"><p>Nelson DL, Cox M, Hoskins AA (2021). Lehninger Principles of Biochemistry (Eighth ed.). New York, NY: Macmillan Learning. ISBN 978-1-319-22800-2. OCLC 1243000176. The binding of somatostatin to its receptor in the pancreas leads to activation of an inhibitory G protein, or Gi, structurally homologous to Gs, that inhibits adenylyl cyclase and lowers [cAMP]. In this way, somatostatin inhibits the secretion of several hormones, including glucagon <a href="978-1-319-22800-2" target="_blank">978-1-319-22800-2</a> <a href="#fnref:24" class="footnote-back-ref">↩</a></p></li> <li id="fn:25"><p>"Carcinoid Tumors and Syndrome". The Lecturio Medical Concept Library. Retrieved 5 July 2021. <a href="https://www.lecturio.com/concepts/carcinoid-tumors-and-syndrome/" target="_blank">https://www.lecturio.com/concepts/carcinoid-tumors-and-syndrome/</a> <a href="#fnref:25" class="footnote-back-ref">↩</a></p></li> <li id="fn:26"><p>"Acromegaly". NIDDK. April 2012. Archived from the original on 27 August 2016. Retrieved 5 July 2021. <a href="https://www.niddk.nih.gov/health-information/health-topics/endocrine/acromegaly/Pages/fact-sheet.aspx" target="_blank">https://www.niddk.nih.gov/health-information/health-topics/endocrine/acromegaly/Pages/fact-sheet.aspx</a> <a href="#fnref:26" class="footnote-back-ref">↩</a></p></li> <li id="fn:27"><p>Liu Y, Lu D, Zhang Y, Li S, Liu X, Lin H (September 2010). "The evolution of somatostatin in vertebrates". Gene. 463 (1–2): 21–8. doi:10.1016/j.gene.2010.04.016. PMID 20472043. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:27" class="footnote-back-ref">↩</a></p></li> </ol>