Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P61278 (somatostatin)
 22,083 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Human skin mast cells, unlike other human mast cells so far studied, released histamine in a concentration-related manner in response to substance P, vasoactive intestinal peptide (VIP) and somatostatin (1 microM to 30 microM). In contrast, eledoisin, physalaemin, neurokinin A, neurokinin B, calcitonin gene-related peptide (CGRP), neurotensin, bradykinin and Lys-bradykinin induced negligible histamine release. 2. The low histamine releasing activity of physalaemin, eledoisin, neurokinin A and neurokinin B relative to substance P suggests that the human skin mast cell activation site is distinct from the tachykinin NK-1, NK-2 or NK-3 receptors described in smooth muscle. 3. The relative potencies of substance P and its fragments SP2-11, SP3-11, SP4-11 and SP1-4 in releasing histamine from human skin mast cells suggests that both the basic N-terminal amino acids and the lipophilic C-terminal portion of substance P are essential for activity. 4. Peptide-induced histamine release, like that induced by compound 48/80, morphine and poly-L-lysine, is rapid, reaching completion in 10-20 s, is largely independent of extracellular calcium but requires intact glycolysis and oxidative phosphorylation. 5. The substance P analogue, [D-Pro4,D-Trp7,9,10] SP4-11 (SPA), not only reduced substance P-induced histamine release in a concentration-related manner but also inhibited that induced by VIP, somatostatin, compound 48/80, poly-L-lysine and morphine but not anti-IgE. 6. The similar characteristics of histamine release induced by substance P, VIP, somatostatin, compound 48/80, poly-L-lysine and morphine suggest that they share a common pathway of activation-secretion coupling distinct from that of IgE-dependent activation. Furthermore, the ability of human skin mast cells to respond to basic non-immunological stimuli including neuropeptides may reflect a specialised function for these cells.
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PMID:Characterization of neuropeptide-induced histamine release from human dispersed skin mast cells. 246 82

The presence, localization and distribution of some regulatory peptides and serotonin were investigated by single and double immunohistochemical methods in the digestive system of two reptiles, Chalcides chalcides and Zonosaurus madascariensis. Both immunoreactive (IR) cells and nerve elements were demonstrated, showing different distributions according to the antisera tested. Similar results were observed in the two saurian species. Chromogranin-SPI-, serotonin-, somatostatin14-, pancreatic polypeptide (PP)-, and gastrin-IR cells were present along the gut epithelium. Cholecystokinin (CCK)-, and insulin-IR cells seemed to be more concentrated in the intestinal portion, while very few glucagon containing cells were observed. Bombesin-IR cells were found in the stomach and they constituted the only endocrine cells of the closed type in the gut. Vasoactive intestinal polypeptide (VIP)-, insulin-, and bombesin-IR nerve terminals were also seen. In the pancreatic duodenal portion of Z madascariensis, the insulin-, glucagon-, PP-, and somatostatin 14-IR cells were present as single elements or grouped in endocrine islets showing a typical topographical distribution. By double immunohistochemical techniques, chromogranin-SPI was found co-localized with the serotonin- and somatostatin-immunoreactivity, but CCK-IR cells were always negative to chromogranin-SP1 antiserum. The present work demonstrates that the chromogranin antiserum is not useful for identifying all the gut endocrine cell types; furthermore, the presence of insulin-immunoreactivity in the endocrine cells is confirmed, and, for the first time, insulin-immunoreactivity is shown in reptilian gut nerve fibres.
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PMID:The gastro-enteric-pancreatic neuroendocrine system in two reptilian species: Chalcides chalcides and Zoonosaurus madascariensis (Sauridae). 917 43

The gene encoding the mouse somatostatin receptor subtype 5 has been isolated from a genomic library and the mRNA start point mapped to position -95 relative to the translational start codon. The promoter region is devoid of TATA and CAAT boxes but contains putative binding sites for AP-1, AP-2 and SP1 and response elements for glucocorticoids (GRE) and phorbol esters (TRE). The encoded receptor protein with a predicted molecular weight of 42.5 kDa is comprised of 385 amino acids and thus contains 22 and 21 amino acids more than rat and human counterparts. The extra amino acids are caused by another translational initiation codon located further upstream. In the region of overlap the mouse somatostatin receptor subtype 5 displays 96.7% sequence identity to the rat and 81.7% to the human homologue. Application of somatostatin-14 and -28 to human embryonic kidney cells expressing the recombinant receptor resulted in the inhibition of forskolin-stimulated adenylyl cyclase with comparable EC50 values. Consistent with the observed sequence relationship, the mouse somatostatin receptor subtype 5 displays a pharmacological profile that resembles the rat homologue more closely than the human counterpart. mRNA for the mouse somatostatin type 5 receptor has been detected in pituitary, kidney, spleen and ovary and, to a lesser extent, in brain, stomach, intestine and thymus but was not observed in heart, pancreas and liver.
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PMID:Cloning, expression, pharmacology and tissue distribution of the mouse somatostatin receptor subtype 5. 963 Mar 98