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)

Salmon (Oncorhynchus kisutch) somatostatin (sSS; 4 or 8 ng/g body wt) or synthetic Gillichthys urotensin II (UII; 2 or 4 ng/g body wt) were injected intraperitoneally into juvenile freshwater coho salmon. Both sSS and UII caused a dose-dependent increase in plasma free fatty acids (FFA) which diminished with time. sSS induced an initial (1 hr) transient hyperglycemia. By contrast, UII tended to induce hypoglycemia, this effect being significant 5 hr after injection of the higher dose. Both sSS and UII depressed plasma insulin titers 1 hr after injection. By 3 hr, the sSS-associated insulin depression was no longer observed. UII treatment induced a hyperinsulinemia which was present 3 and 5 hr after peptide administration. Although no decreases in liver total lipid concentration or in mesenteric fat total tissue mass were observed, lipolytic enzyme activity within each depot was significantly enhanced by both peptides. Neither sSS nor UII altered 3H2O incorporation into fatty acids or neutral lipids. However, enhanced lipogenesis, particularly by UII, was indicated by increased NADPH production resulting from glucose-6-phosphate dehydrogenase activity. Both sSS and UII enhanced glucose mobilization, as indicated by decreased liver glycogen content and increased liver glucose-6-phosphatase activity. UII, but not sSS, stimulated glycogen synthetase activity. These results suggest that both sSS and UII stimulate hyperlipidemia by enhancing depot lipase activity and that although both factors are potentially gluconeogenetic, sSS seems to be glycogenolytic and hyperglycemic, whereas UII may channel glucose to FFA synthesis.
 ...
PMID:Effects of somatostatin-25 and urotensin II on lipid and carbohydrate metabolism of coho salmon, Oncorhynchus kisutch. 288 97

Two peptides with urotensin II (UII = smooth muscle stimulating) activity have been isolated from urophyses of the sucker, Catostomus commersoni. The amino acid sequences of the two peptides, designated UIIA and UIIB, are as follows: UIIA, H-Gly-Ser-Gly-Ala-Asp-Cys-Phe-Trp-Lys-Tyr-Cys-Val-OH; UIIB, H-Gly-Ser-Asn-Thr-Glu-Cys-Phe-Trp-Lys-Tyr-Cys-Val-OH. These peptides have the part sequence Cys-Phe-Trp-Lys-Tyr-Cys-Val in common with the UII peptide from Gillichthys mirabilis and the part-sequence Phe-Trp-Lys in common with somatostatin.
 ...
PMID:Isolation and amino acid sequence of two urotensin II peptides from Catostomus commersoni urophyses. 613 58

1. Human urotensin-II (hU-II), a cyclic undecapeptide, is amongst the most potent mammalian vasoconstrictors identified, suggesting that hU-II and its G-protein-coupled receptor (UT) may regulate cardiovascular homeostasis. Such a hypothesis would benefit greatly from the development of selective UT antagonists. 2. Although the somatostatin (SST) antagonist SB-710411 (Cpa-c[D-Cys-Pal-D-Trp-Lys-Val-Cys]-Cpa-amide) is purported to block U-II-induced contractions in rat isolated aorta, little is known about its specific pharmacological properties. 3. SB-710411 (10 micro M) inhibited hU-II-induced contraction in rat isolated aorta causing a significant, parallel shift in the agonist concentration-response curve (pK(b) 6.28+/-0.11; n=8) with no suppression of the E(max). In contrast, SB-710411 did not alter the contractile actions of angiotensin-II, phenylephrine, or KCl. Paradoxically, however, SB-710411 potentiated the contractile response to endothelin-1 (pEC(50) 8.02+/-0.16 and 8.54+/-0.11, P<0.01; n=8). Rather than being specific toSB-710411, this phenomenon appears to be related to somatostatin receptor affinity and not intrinsic activity since the SST agonist somatostatin-14 and antagonist cyclo-somatostatin also potentiated endothelin-1-induced contraction. 4. SB-710411 (10 micro M) did not inhibit carbachol, sodium nitroprusside, IBMX, isoprenaline, and levcromakalim-induced reversal of tone established with noradrenaline. In contrast, however, SB-710411 significantly inhibited the reversal of tone established with endothelin-1 using the same vasorelaxants. 5. In summary, although SB-710411 inhibits the vasoconstrictor actions of hU-II in a competitive, surmountable manner, it also possesses additional pharmacological actions. Thus, whilst the present study is amongst the first to detail the properties of a functional U-II receptor antagonist, the data suggest caution be used when assessing data generated utilizing this moiety and other SST analogues.
 ...
PMID:Pharmacological characterization of SB-710411 (Cpa-c[D-Cys-Pal-D-Trp-Lys-Val-Cys]-Cpa-amide), a novel peptidic urotensin-II receptor antagonist. 1235 26

The UII and urotensin II-related peptide (URP) genes belong to the same superfamily as the somatostatin gene. It has been previously shown that somatostatin activates the UII-receptor (UTR). In contrast, the possible interaction between UII and URP and somatostatin receptors has remained scarcely analyzed. Herein, we have investigated the effects of UII and URP on cell proliferation and free cytosolic Ca2+ concentration ([Ca2+]i) in CHO-K1 cells stably expressing the porcine somatostatin receptor subtypes sst2 and sst5. Results show that both UII and URP induce stimulation of cell proliferation mediated by sst2 receptors and UII provokes inhibition of cell proliferation mediated by sst5 receptors. UII and URP also provoked an increase of [Ca2+]i in both sst2- and sst5-transfected cells. Together, our present data demonstrate that UII and URP directly activate sst2 and sst5 and thus mimic the effect of somatostatin on its cognate receptors.
 ...
PMID:Urotensin II and urotensin II-related peptide activate somatostatin receptor subtypes 2 and 5. 1828 30

Cortistatin (CST) is a neuropeptide from the somatostatin (SRIF)/urotensin (UII) family named after its predominantly cortical expression and ability to depress cortical activity, which was discovered a decade ago. In vitro assays show CST is able to bind all five cloned somatostatin receptors and shares many pharmacological and functional properties with SRIF. However, distinct from SRIF, CST has been shown to induce slow-wave sleep, reduce locomotor activity, and activate cation selective currents not responsive to somatostatin. Different lines of evidence also indicate that CST, like SRIF, is involved in learning and memory processes. CST-14 may also function as an endogenous anti-convulsant. In addition to its role in cortical synchronization, CST-14 has emerged as an important mediator of immunity and inflammation. This review will cover some of the basic properties of CST in the brain, and will discuss new data on the role of CST in cortical activity.
 ...
PMID:Cortistatin--functions in the central nervous system. 1837 74

Somatostatin (SST) and its receptors (sst) make up a molecular family with unique functional complexity and versatility. Widespread distribution and frequent coexpression of sst subtypes underlies the multiplicity of (patho)physiological processes controlled by SST (central nervous system functions, endocrine and exocrine secretion, cell proliferation). This complexity is clearly reflected in the intricate evolutionary development of this molecular family. Recent studies postulate the existence of an ancestral somatostatin/urotensin II (SST/UII) gene, which originated two ancestral, SST and UII, genes by local duplication. Subsequently, segment duplication would have originated two diverging SST genes in both fish (SS1/SS2) and tetrapods [(SST/cortistatin(CST))]. SST/CST actions are mediated by a family of GPCRs (sst1-5) encoded by five different genes. sst1-4 sequences are highly conserved compared with sst5, suggesting unique evolutionary and functional relevance for the latter. Indeed, we recently identified novel truncated but functional sst5 variants in several species, which may help to explain part of the complexity of the SST/CST/sst family. Comparative and phylogenetic analysis of this molecular family would enhance our understanding of its paradigmatic evolutionary complexity and functional versatility.
 ...
PMID:Somatostatin and its receptors from fish to mammals. 2063 32