Internalization of glucagon-like peptide-1(7-36)amide in rat insulinoma cells. 1989

R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
Dept. of Internal Medicine, Philipps University of Marburg, Federal Republic of Germany.

Glucagon-like peptide-1(7-36)amide [GLP-1(7-36)amide] is supposed to be an important physiologic incretin. Recently, high affinity receptors for GLP-1(7-36)amide have been demonstrated on rat insulinoma-derived RINm5F cells. The present study examined the internalization and degradation of the GLP-1-receptor complex. Internalization of the peptide was time- and temperature-dependent. At 37 degrees C binding and internalization was rapid. At 60 min 35% of 125I-labeled GLP-1(7-36)amide was internalized. Incubation in the presence of increasing concentrations of non-labeled GLP-1(7-36)amide resulted in a decrease of internalization of 125I-labeled peptide indicating that this process is saturable. Incubation in the presence of 0.2 mM chloroquine, an inhibitor of intracellular hormone degradation, resulted in intracellular accumulation of 125I-GLP-1(7-36)amide. HPLC-supported analysis of cell content after internalization of 125I-GLP-1(7-36)amide during a 60-min incubation period at 37 degrees C revealed an elution profile showing two maxima of radioactivity: one represented intact labeled GLP-1(7-36)amide, the other an intracellular degradation product of the peptide. Chloroquine caused a 5-fold increase of the peak representing intact 125I-GLP-1(7-36)amide thus demonstrating inhibition of degradation of labelled peptide. Furthermore, a 4-fold increase of the other peak occurred possibly mirroring a delay of release of degradation products by chloroquine. It was excluded that chloroquine is able to interfere with GLP-1(7-36)amide-binding to its receptor.

UI MeSH Term Description Entries
D007340 Insulinoma A benign tumor of the PANCREATIC BETA CELLS. Insulinoma secretes excess INSULIN resulting in HYPOGLYCEMIA. Adenoma, beta-Cell,Insuloma,beta-Cell Tumor,Adenoma, beta Cell,Adenomas, beta-Cell,Insulinomas,Insulomas,Tumor, beta-Cell,Tumors, beta-Cell,beta Cell Tumor,beta-Cell Adenoma,beta-Cell Adenomas,beta-Cell Tumors
D007516 Adenoma, Islet Cell A benign tumor of the pancreatic ISLET CELLS. Usually it involves the INSULIN-producing PANCREATIC BETA CELLS, as in INSULINOMA, resulting in HYPERINSULINISM. Islet Cell Tumor,Islet of Langerhans Tumor,Nesidioblastoma,Pancreatic Islet Cell Tumors,Island Cell Tumor,Adenomas, Islet Cell,Island Cell Tumors,Islet Cell Adenoma,Islet Cell Adenomas,Islet Cell Tumors,Langerhans Tumor Islet,Nesidioblastomas,Tumor Islet, Langerhans,Tumor, Island Cell,Tumor, Islet Cell,Tumors, Island Cell,Tumors, Islet Cell
D007700 Kinetics The rate dynamics in chemical or physical systems.
D010190 Pancreatic Neoplasms Tumors or cancer of the PANCREAS. Depending on the types of ISLET CELLS present in the tumors, various hormones can be secreted: GLUCAGON from PANCREATIC ALPHA CELLS; INSULIN from PANCREATIC BETA CELLS; and SOMATOSTATIN from the SOMATOSTATIN-SECRETING CELLS. Most are malignant except the insulin-producing tumors (INSULINOMA). Cancer of Pancreas,Pancreatic Cancer,Cancer of the Pancreas,Neoplasms, Pancreatic,Pancreas Cancer,Pancreas Neoplasms,Pancreatic Acinar Carcinoma,Pancreatic Carcinoma,Acinar Carcinoma, Pancreatic,Acinar Carcinomas, Pancreatic,Cancer, Pancreas,Cancer, Pancreatic,Cancers, Pancreas,Cancers, Pancreatic,Carcinoma, Pancreatic,Carcinoma, Pancreatic Acinar,Carcinomas, Pancreatic,Carcinomas, Pancreatic Acinar,Neoplasm, Pancreas,Neoplasm, Pancreatic,Neoplasms, Pancreas,Pancreas Cancers,Pancreas Neoplasm,Pancreatic Acinar Carcinomas,Pancreatic Cancers,Pancreatic Carcinomas,Pancreatic Neoplasm
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011956 Receptors, Cell Surface Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands. Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D002738 Chloroquine The prototypical antimalarial agent with a mechanism that is not well understood. It has also been used to treat rheumatoid arthritis, systemic lupus erythematosus, and in the systemic therapy of amebic liver abscesses. Aralen,Arechine,Arequin,Chingamin,Chlorochin,Chloroquine Sulfate,Chloroquine Sulphate,Khingamin,Nivaquine,Sulfate, Chloroquine,Sulphate, Chloroquine
D002851 Chromatography, High Pressure Liquid Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed. Chromatography, High Performance Liquid,Chromatography, High Speed Liquid,Chromatography, Liquid, High Pressure,HPLC,High Performance Liquid Chromatography,High-Performance Liquid Chromatography,UPLC,Ultra Performance Liquid Chromatography,Chromatography, High-Performance Liquid,High-Performance Liquid Chromatographies,Liquid Chromatography, High-Performance
D004763 Glucagon-Like Peptides Peptides derived from proglucagon which is also the precursor of pancreatic GLUCAGON. Despite expression of proglucagon in multiple tissues, the major production site of glucagon-like peptides (GLPs) is the INTESTINAL L CELLS. GLPs include glucagon-like peptide 1, glucagon-like peptide 2, and the various truncated forms. Enteroglucagon,Enteroglucagons,Glucagon-Like Peptide,Glucagon-Like Polypeptide,Gut Glucagon,Glucagon-Like Polypeptides,Glucagon Like Peptide,Glucagon Like Peptides,Glucagon Like Polypeptide,Glucagon Like Polypeptides,Glucagon, Gut,Peptide, Glucagon-Like,Polypeptide, Glucagon-Like
D005934 Glucagon A 29-amino acid pancreatic peptide derived from proglucagon which is also the precursor of intestinal GLUCAGON-LIKE PEPTIDES. Glucagon is secreted by PANCREATIC ALPHA CELLS and plays an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1511) Glucagon (1-29),Glukagon,HG-Factor,Hyperglycemic-Glycogenolytic Factor,Proglucagon (33-61),HG Factor,Hyperglycemic Glycogenolytic Factor

Related Publications

R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
March 1988, The Journal of endocrinology,
R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
March 1989, Annals of clinical biochemistry,
R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
August 1990, Journal of molecular endocrinology,
R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
January 1994, Digestion,
R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
October 1998, Molecular neurobiology,
R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
November 1989, Brain research,
R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
July 1996, Acta physiologica Scandinavica,
R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
March 1992, Neuropeptides,
R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
May 1992, Molecular and cellular endocrinology,
R Göke, and G Richter, and B Göke, and M Trautmann, and R Arnold
January 1997, Peptides,
Copied contents to your clipboard!