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Proglucagon-Derived Peptides Expression and Secretion in Rat Insulinoma INS-1 Cells.
Front Cell Dev Biol
November 2020
INSERM, U1190, Lille, France.
Article Synopsis
- Rat insulinoma INS-1 cells are studied for insulin secretion and have a subset of bi-hormonal cells that produce both insulin and proglucagon proteins.
- Researchers validated an anti-glucagon antibody that detects various proglucagon-derived peptides in INS-1 cells, helping to analyze their expression.
- The study found that high-glucose treatment reduces both insulin and glucagon levels in INS-1 cells, indicating these cells are better for studying insulin rather than glucagon or glicentin secretion in response to glucose levels.
Cellular and sub-cellular localisation of oxyntomodulin-like immunoreactivity in enteroendocrine cells of human, mouse, pig and rat.
Cell Tissue Res
February 2019
Department of Anatomy & Neuroscience, University of Melbourne, Parkville, VIC, 3010, Australia.
We use a monoclonal antibody against the C-terminal of oxyntomodulin (OXM) to investigate enteroendocrine cells (EEC) in mouse, rat, human and pig. This antibody has cross-reactivity with the OXM precursor, glicentin (Gli) but does not recognise glucagon. The antibody stained EEC in the jejunum and colon of each species.
View Article and Find Full Text PDFThe intestinal distribution pattern of appetite- and glucose regulatory peptides in mice, rats and pigs.
BMC Res Notes
February 2016
NNF Center for Basic Metabolic Research and Department of Biomedical Sciences, Panum Institute, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 12.2, 2200, Copenhagen N, Denmark.
Background: Mice, rats, and pigs are the three most used animal models when studying gastrointestinal peptide hormones; however their distribution from the duodenum to the distal colon has not been characterized systematically across mice, rats and pigs. We therefore performed a comparative distribution analysis of the tissue content of the major appetite- and glucose regulatory peptides: glucose-dependent insulinotropic polypeptide (GIP), glucagon-like peptide-1 (GLP-1), glucagon-like peptide-1 (GLP-2), oxyntomodulin/glicentin, neurotensin, and peptide YY (PYY) from the duodenum to distal colon in mice (n = 9), rats (n = 9) and pigs (n = 8), using validated radioimmunoassays.
Results: GLP-1, GLP-2 and oxyntomodulin/glicentin show similar patterns of distribution within the respective species, but for rats and pigs the highest levels were found in the distal small intestine, whereas for the mouse the highest level was found in the distal colon.
Glicentin-related pancreatic polypeptide inhibits glucose-stimulated insulin secretion from the isolated pancreas of adult male rats.
Physiol Rep
December 2015
School of Biological Sciences, University of Auckland, Auckland, New Zealand The Maurice Wilkins Centre for Molecular BioDiscovery, New Zealand Centre for Advanced Discovery and Experimental Therapeutics, NIHR Manchester Biomedical Research Centre, Central Manchester University Hospitals NHS Foundation Trust, Manchester, UK The Institute of Human Development, University of Manchester, Manchester, UK Department of Pharmacology, Medical Sciences Division, University of Oxford, Oxford, UK
Peptides derived from the glucagon gene Gcg, for example, glucagon and glucagon-like peptide 1 (GLP-1), act as physiological regulators of fuel metabolism and are thus of major interest in the pathogenesis of diseases, such as type-2 diabetes and obesity, and their therapeutic management. Glicentin-related pancreatic polypeptide (GRPP) is a further, 30 amino acid Gcg-derived peptide identified in human, mouse, rat, and pig. However, the potential glucoregulatory function of this peptide is largely unknown.
View Article and Find Full Text PDFTwo dipolar α-helices within hormone-encoding regions of proglucagon are sorting signals to the regulated secretory pathway.
J Biol Chem
May 2014
From the Departments of Medical Biophysics, the Metabolism/Diabetes and Imaging Programs, Lawson Health Research Institute, London, Ontario N6A 4V2, Canada Pathology, and Medicine, University of Western Ontario, London, Ontario N6A 3K7 and
Proglucagon is expressed in pancreatic α cells, intestinal L cells, and some hypothalamic and brainstem neurons. Tissue-specific processing of proglucagon yields three major peptide hormones as follows: glucagon in the α cells and glucagon-like peptides (GLP)-1 and -2 in the L cells and neurons. Efficient sorting and packaging into the secretory granules of the regulated secretory pathway in each cell type are required for nutrient-regulated secretion of these proglucagon-derived peptides.
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