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  • 1
    Publication Date: 1996-06-21
    Description: Adenosine triphosphate (ATP)-sensitive potassium (KATP) channels couple the cellular metabolic state to electrical activity and are a critical link between blood glucose concentration and pancreatic insulin secretion. A mutation in the second nucleotide-binding fold (NBF2) of the sulfonylurea receptor (SUR) of an individual diagnosed with persistent hyperinsulinemic hypoglycemia of infancy generated KATP channels that could be opened by diazoxide but not in response to metabolic inhibition. The hamster SUR, containing the analogous mutation, had normal ATP sensitivity, but unlike wild-type channels, inhibition by ATP was not antagonized by adenosine diphosphate (ADP). Additional mutations in NBF2 resulted in the same phenotype, whereas an equivalent mutation in NBF1 showed normal sensitivity to MgADP. Thus, by binding to SUR NBF2 and antagonizing ATP inhibition of KATP++ channels, intracellular MgADP may regulate insulin secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nichols, C G -- Shyng, S L -- Nestorowicz, A -- Glaser, B -- Clement, J P 4th -- Gonzalez, G -- Aguilar-Bryan, L -- Permutt, M A -- Bryan, J -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1785-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Washington University School of Medicine, St. Louis, Missouri 63110, USA. cnichols@cellbio.wustl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650576" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Diphosphate/*metabolism/pharmacology ; Adenosine Triphosphate/*metabolism/pharmacology ; Amino Acid Sequence ; Animals ; Cell Line, Transformed ; Cercopithecus aethiops ; Cricetinae ; Diazoxide/pharmacology ; Humans ; Hyperinsulinism/genetics ; Hypoglycemia/genetics ; Insulin/*secretion ; Islets of Langerhans/metabolism ; Molecular Sequence Data ; Patch-Clamp Techniques ; Point Mutation ; Potassium Channels/drug effects/genetics/*metabolism ; *Potassium Channels, Inwardly Rectifying ; Receptors, Drug/drug effects/genetics/*metabolism ; Rubidium/metabolism ; Sulfonylurea Receptors ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-15
    Description: One of the first steps in neovascularization is dissolution of the basement membrane at the point of endothelial outgrowth. An assay was developed to determine whether basement membrane collagens (types IV and V) are degraded by endothelial cells migrating toward a chemotactic stimulus. Fetal bovine endothelial cells were placed on one side of a filter containing the collagen substrate, and a chemoattractant derived from retinal extracts was placed on the opposite side. Degradation of both type IV and type V collagens was observed when the retinal factor was placed on the side of the filter opposite the endothelial cells. Metalloproteinases that cleaved type IV and type V collagens could be extracted from the endothelial cells with detergents. Such endothelial cell-associated (possibly membrane-bound) proteinases may locally disrupt the basement membrane and facilitate the outgrowth of capillary sprouts toward the angiogenic stimulus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kalebic, T -- Garbisa, S -- Glaser, B -- Liotta, L A -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):281-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6190230" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Basement Membrane/*metabolism ; Cattle ; Cell Movement ; Chemotaxis ; Collagen/*metabolism ; Endothelium/metabolism ; Neovascularization, Pathologic ; Retina/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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