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

Monoclonal antibody VC1.1 is shown to stain selectively a subpopulation of GABAergic neurons in the rat cerebral cortex. Almost all VC1.1 immunoreactive cells were also GABA-like immunoreactive (GABA-LI) and parvalbumin (PV) immunoreactive, whereas they were about 30% and 65% of GABA-LI and PV-positive cells in the parietal cortex and about 13% and 32% in the occipital cortex, respectively. Although a few VC1.1 positive cells showed somatostatin-like and/or cholecystokinin-like immunoreactivities, they were exceptional (less than 1% of VC1.1 positive cells). Furthermore about 90% of VC1.1 positive cells were also stained with a lectin, Vicia villosa agglutinin, with a specific affinity for terminal N-acetylgalactosamine.
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PMID:Monoclonal antibody VC1.1 selectively stains a population of GABAergic neurons containing the calcium-binding protein parvalbumin in the rat cerebral cortex. 259 17

The 22-residue somatostatin (SST-22) from channel catfish, purified by an improved method, is shown to be a glycopeptide. This represents the first report of a glycosylated somatostatin. Multiple forms of SST-22 exist with the major form containing 1 mol of galactose and 1 mol of N-acetylgalactosamine/mol of peptide attached via an O-glycosidic linkage to Thr-5. The position of the carbohydrate was determined by trapping the reactive peptide following beta-elimination of the carbohydrate with [35S]beta-mercaptoethanol followed by sequencing of the radiolabeled protein. All forms of SST-22 that have been purified are identical in amino acid composition. The heterogeneity resides in the carbohydrate portion of the glycopeptide with at least one of the minor forms containing sialic acid. The sequence for SST-22 obtained by automated Edman degradation is Asp X Asn X Thr X Val X Thr X Ser X Lys X Pro X Leu X Asn X Cys X Met X Asn X Tyr X Phe X Trp X Lys X Ser X Arg X Thr X Ala X Cys. This sequence differs at positions 5 and 19 from that published by Oyama et al. (Oyama, H., Bradshaw, R. A., Bates, O.J., and Permutt, A. (1980) J. Biol. Chem. 255, 2251-2254). The amino acid sequence reported here is identical to that deduced from the cDNA. The mass ion of SST-22 was determined by fast atom bombardment/mass spectrometry and shown to be 2943 +/- 1 (m/z). The observed mass ion is consistent with the molecular weight predicted from the amino acid sequence plus 1 mol of galactose and 1 mol of N-acetylgalactosamine.
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PMID:Structure of the 22-residue somatostatin from catfish. An O-glycosylated peptide having multiple forms. 614 20

The subpopulations were compared of neurons in human dorsal root ganglia (DRG), as substance P, identified by somatostatin, Glycine max lectin (SBA) specific to terminal N-acetylgalactosamine, and Ulex europaeus I agglutinin (UEA-I) specific to L-fucose. The lectins and neuropeptides all bound to neurons of small diameter. Furthermore, the majority of the SBA binding neurons or somatostatin positive neurons were also UEA-I binding neurons. However, SBA binding neurons were not colocalized with somatostatin or substance P. Less than 20% of substance P positive neurons showed colocalization with L-fucosyl residues, and approximately 10% of L-fucosyl residues showed colocalization with substance P. Our results suggest that both L-fucose and terminal N-acetylgalactosamine containing neurons in the human DRG are subjected to different subpopulations from substance P or somatostatin positive neurons.
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PMID:Differential localization of lectin binding sites and neuropeptides in human dorsal root ganglia. 753 Nov 91

Mucous cells and enteroendocrine cells of the pyloric region of the ruin lizard (Podarcis sicula campestris De Betta) have been examined by lectin histochemical and immunohistochemical methods. Binding to five plant lectins (Canavalia ensiformis, Con A; Triticum vulgare, wheat germ, WGL; Lotus tetragonolobus, winged pea, WPL; Glycine max, soybean, SBL; Arachis hypogaea, peanut, PNL) was performed to characterize glycoconjugates in the secretory products of superficial and glandular mucous cells. Lectin histochemistry revealed the presence of N-acetyl-D-galactosamine, D-galactose and N-acetyl-D-glucosamine in the pyloric superficial cells. Mucous glandular cells mainly contained neutral glycoproteins with terminal residues of galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosamine. These cells did not react with Con A after periodate oxidation-sodium borohydride reduction (Paradoxical Con A staining). In the pyloric glands three different types of endocrine cells were identified immunohistochemically: gastrin-, serotonin- and somatostatin-immunoreactive cells; VIP-, bombesin- or cholecystokinin-immunoreactive cells have not been found in the pyloric mucosa.
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PMID:Immunohistochemical investigations on the pyloric glands of the ruin lizard (Podarcis sicula campestris de Betta). 791 80

We have studied the mechanism of soybean agglutinin (SBA) mediated cholecystokinin (CCK) release in enriched cultured cholecystokinin-secreting cells. 12-O-Tetradecanoylphorbol-13-acetate 1 mM significantly stimulated release of CCK-like-immunoreactivity (CCK-LI) by 55%+/-17% (p < 0.05), which was blocked by the protein kinase C inhibitor staurosporine 100 nM. Forskolin 10 mM stimulated CCK-LI by 82%+/-12% (p < 0.05) and this was inhibited by somatostatin 1 nM. 1-Phenylalanine 20 mM and Bay K 8644 1 mM stimulated CCK-LI by 69%+/-22% and 60%+/-19% respectively (p < 0.05), these responses were completely abolished by the L-type calcium channel antagonist verapamil 10 mM. SBA 10 and 100 microg/ml stimulated CCK-LI by 65%+/-22% and 74%+/-24% respectively (p < 0.05). The effect of SBA was inhibited by verapamil and N-acetylgalactosamine. We conclude that SBA stimulates CCK-LI through calcium flux via L-type calcium channels.
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PMID:Soybean agglutinin stimulated cholecystokinin release from cultured rabbit jejunal cells requires calcium influx via L-type calcium channels. 986 61

The glycopeptide hormone catfish somatostatin (somatostatin-22) has the amino acid sequence H-Asp-Asn-Thr-Val-Thr-Ser-Lys-Pro-Leu-Asn-Cys-Met-Asn-Tyr-Phe-Trp-Lys-Se r-Arg-Thr-Ala-Cys-OH; it includes a cyclic disulfide connecting the two Cys residues, and the major naturally occurring glycoform contains D-GalNAc and D-Gal O-glycosidically linked to Thr5. The linear sequence was assembled smoothly starting with an Fmoc-Cys(Trt)-PAC-PEG-PS support, using stepwise Fmoc solid-phase chemistry. In addition to the nonglycosylated peptide, two glycosylated forms of somatostatin-22 were accessed by incorporating as building blocks, respectively, Nalpha-Fmoc-Thr(Ac3-alpha-D-GalNAc)-OH and Nalpha-Fmoc-Thr(Ac4-beta-D-Gal-(1-->3)-Ac2-alpha-D-GalNAc)-O H. Acidolytic deprotection/cleavage of these peptidyl-resins with trifluoroacetic acid/scavenger cocktails gave the corresponding acetyl-protected glycopeptides with free sulfhydryl functions. Deacetylation, by methanolysis in the presence of catalytic sodium methoxide, was followed by mild oxidation at pH 7, mediated by Nalpha-dithiasuccinoyl (Dts)-glycine, to provide the desired monomeric cyclic disulfides. The purified peptides were tested for binding affinities to a panel of cloned human somatostatin receptor subtypes; in several cases, presence of the disaccharide moiety resulted in 2-fold tighter binding.
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PMID:Chemical synthesis and receptor binding of catfish somatostatin: a disulfide-bridged beta-D-Galp-(1-->3)-alpha-D-GalpNAc O-glycopeptide. 1066 64