BIOMAT Database Logo BIOMAT Database Logo

Inhibition of human pancreatic islet insulin release by receptor-selective somatostatin analogs directed to somatostatin receptor subtype 5. 1999

Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Diabetes Research Center, Vrije Universiteit Brussel, Brussels, Belgium.

Somatostatin (SS)-14 and SS28 are produced by pancreatic D cells and gut mucosa and inhibit pancreatic islet insulin and glucagon release. There are five distinct SS receptor (SSTR) subtypes, namely SSTR1-5, which show different affinities for SS14 and SS28. In order to identify the subtype responsible for inhibition of insulin release by human B cells, SSTR-selective SS analogs were tested in isolated human islets. Glucose-stimulated insulin secretion in human islets incubated for 1 hr at 20 mM glucose, and in islets cultured for 24 hr at a near-physiological (6.1 mM) glucose concentration, was inhibited (<50% of the control) by SSTR5-specific analogs and by SS14 and SS28. SS14, SS28, and different SSTR5 preferential analogs also inhibited islet amyloid polypeptide release during the 24-hr culture. On the other hand, a group of SSTR2-selective analogs failed to inhibit insulin release. Analysis by reverse transcription-polymerase chain reaction indicated that human islets express similar amounts of SSTR2 and SSTR5 mRNAs, while human pancreatic ductal cells express much lower levels of these mRNAs. In conclusion, our data suggest that SSTR5 is an important mediator of the insulin inhibitory action of SS in cultured human islets.

UI MeSH Term Description Entries
D007328 Insulin A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1). Iletin,Insulin A Chain,Insulin B Chain,Insulin, Regular,Novolin,Sodium Insulin,Soluble Insulin,Chain, Insulin B,Insulin, Sodium,Insulin, Soluble,Regular Insulin
D007515 Islets of Langerhans Irregular microscopic structures consisting of cords of endocrine cells that are scattered throughout the PANCREAS among the exocrine acini. Each islet is surrounded by connective tissue fibers and penetrated by a network of capillaries. There are four major cell types. The most abundant beta cells (50-80%) secrete INSULIN. Alpha cells (5-20%) secrete GLUCAGON. PP cells (10-35%) secrete PANCREATIC POLYPEPTIDE. Delta cells (~5%) secrete SOMATOSTATIN. Islands of Langerhans,Islet Cells,Nesidioblasts,Pancreas, Endocrine,Pancreatic Islets,Cell, Islet,Cells, Islet,Endocrine Pancreas,Islet Cell,Islet, Pancreatic,Islets, Pancreatic,Langerhans Islands,Langerhans Islets,Nesidioblast,Pancreatic Islet
D009842 Oligopeptides Peptides composed of between two and twelve amino acids. Oligopeptide
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010456 Peptides, Cyclic Peptides whose amino acid residues are linked together forming a circular chain. Some of them are ANTI-INFECTIVE AGENTS; some are biosynthesized non-ribosomally (PEPTIDE BIOSYNTHESIS, NON-RIBOSOMAL). Circular Peptide,Cyclic Peptide,Cyclic Peptides,Cyclopeptide,Orbitide,Circular Peptides,Cyclopeptides,Orbitides,Peptide, Circular,Peptide, Cyclic,Peptides, Circular
D010879 Piperazines Compounds that are derived from PIPERAZINE.
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000682 Amyloid A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease. Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
D013004 Somatostatin A 14-amino acid peptide named for its ability to inhibit pituitary GROWTH HORMONE release, also called somatotropin release-inhibiting factor. It is expressed in the central and peripheral nervous systems, the gut, and other organs. SRIF can also inhibit the release of THYROID-STIMULATING HORMONE; PROLACTIN; INSULIN; and GLUCAGON besides acting as a neurotransmitter and neuromodulator. In a number of species including humans, there is an additional form of somatostatin, SRIF-28 with a 14-amino acid extension at the N-terminal. Cyclic Somatostatin,Somatostatin-14,Somatotropin Release-Inhibiting Hormone,SRIH-14,Somatofalk,Somatostatin, Cyclic,Somatotropin Release-Inhibiting Factor,Stilamin,Somatostatin 14,Somatotropin Release Inhibiting Factor,Somatotropin Release Inhibiting Hormone
D017481 Receptors, Somatostatin Cell surface proteins that bind somatostatin and trigger intracellular changes which influence the behavior of cells. Somatostatin is a hypothalamic hormone, a pancreatic hormone, and a central and peripheral neurotransmitter. Activated somatostatin receptors on pituitary cells inhibit the release of growth hormone; those on endocrine and gastrointestinal cells regulate the absorption and utilization of nutrients; and those on neurons mediate somatostatin's role as a neurotransmitter. Receptors, Somatotropin Release Inhibiting Hormone,Somatostatin Receptors,Receptors, SRIH,SRIH Receptors,Somatostatin Receptor,Receptor, Somatostatin

Related Publications

Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Specific inhibition of rat pancreatic insulin or glucagon release by receptor-selective somatostatin analogs.
November 1994, Biochemical and biophysical research communications,
Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Selective somatostatin receptor 5 inhibition improves hepatic insulin sensitivity.
February 2023, Pharmacology research & perspectives,
Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Selective inhibition of glucagon and insulin secretion by somatostatin analogs.
January 1979, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Somatostatin receptors in pituitary and development of somatostatin receptor subtype-selective analogs.
April 2003, Endocrine,
Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Dopamine receptor subtype 2 and somatostatin receptor subtype 5 expression influences somatostatin analogs effects on human somatotroph pituitary adenomas in vitro.
October 2005, Journal of molecular endocrinology,
Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Inhibition by somatostatin of insulin release from isolated pancreatic islets.
June 1975, FEBS letters,
Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Expression of somatostatin receptor subtype 1-5 genes in human pancreatic cancer.
February 1998, Journal of the National Cancer Institute,
Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Down-regulation of pancreatic and duodenal homeobox-1 by somatostatin receptor subtype 5: a novel mechanism for inhibition of cellular proliferation and insulin secretion by somatostatin.
January 2014, Frontiers in physiology,
Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Subtype-selective expression of the five somatostatin receptors (hSSTR1-5) in human pancreatic islet cells: a quantitative double-label immunohistochemical analysis.
January 1999, Diabetes,
Y Zambre, and Z Ling, and M C Chen, and X Hou, and C W Woon, and M Culler, and J E Taylor, and D H Coy, and C Van Schravendijk, and F Schuit, and D G Pipeleers, and D L Eizirik
Re: Expression of somatostatin receptor subtype 1-5 genes in human pancreatic cancer.
June 1998, Journal of the National Cancer Institute,
Copied contents to your clipboard!