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Title Protein phosphorylation in pancreatic islets induced by 3-phosphoglycerate and 2-phosphoglycerate
Creator/Author Pek, S.B. ; Usami, Masaru ; Bilir, N. ; Fischer-Bovenkerk, C. ; Ueda, Tetsufumi (Univ. of Michigan, Ann Arbor (USA))
Publication Date1990 Jun 01
OSTI IdentifierOSTI ID: 5393586
Other Number(s)ISSN0027-8424; CODEN: PNASA
Resource TypeJournal Article
Resource RelationProceedings of the National Academy of Sciences of the United States of America ; Vol/Issue: 87:11
Subject550201 -- Biochemistry-- Tracer Techniques; CARBOHYDRATES-- BIOCHEMISTRY;PANCREAS-- GLYCOLYSIS;PROTEINS-- AUTORADIOGRAPHY; AMP;ATP;DOSE-RESPONSE RELATIONSHIPS;ELECTROPHORESIS;INSULIN;METABOLITES;PHORBOL ESTERS;PHOSPHORUS 32;PHOSPHORYLATION;RATS;SECRETION
Related SubjectANIMALS;BETA DECAY RADIOISOTOPES;BETA-MINUS DECAY RADIOISOTOPES;BODY;CARCINOGENS;CHEMICAL REACTIONS;CHEMISTRY;DAYS LIVING RADIOISOTOPES;DIGESTIVE SYSTEM;ENDOCRINE GLANDS;ESTERS;GLANDS;HORMONES;ISOTOPES;LIGHT NUCLEI;MAMMALS;METABOLISM;NUCLEI;NUCLEOTIDES;ODD-ODD NUCLEI;ORGANIC COMPOUNDS;ORGANS;PEPTIDE HORMONES;PHOSPHORUS ISOTOPES;PROTEINS;RADIOISOTOPES;RODENTS;VERTEBRATES
Description/Abstract The authors have shown previously that 3-phosphoglycerate, which is a glycolytic metabolite of glucose, induces protein phosphorylation in bovine and rat brain and in rat heart, kidney, liver, lung, and whole pancreas.^Since glycolytic metabolism of glucose is of paramount importance in insulin release, they considered the possibility that 3-phosphoglycerate may act as a coupling factor, and they searched for evidence for the existence of 3-phosphoglycerate-dependent protein phosphorylation systems in freshly isolated normal rat pancreatic islets.^Membrane and cytosol fractions were incubated with ({gamma}-{sup 32}P)ATP and appropriate test substances and were subjected to NaDodSO{sub 4}/PAGE and autoradiography.^As little as 0.005 mM 3-phosphoglycerate or 2-phosphoglycerate stimulated the phosphorylation of 65-kDa cytosol protein by as early as 0.25 min.^The phosphate bond of the 65-kDa phosphoprotein was sufficiently stable to withstand dialysis; the radioactivity could not be chased out by subsequent exposure to ATP, ADP, 3-phosphoglycerate, or 2,3-bisphosphoglycerate.^Moreover, cAMP, cGMP, phorbol 12-myristate 13-acetate, or calcium failed to stimulate the phosphorylation of the 65-kDa protein.^Phosphoglycerate-dependent protein phosphorylation in islets may have relevance to stimulation of insulin secretion.
Country of PublicationUnited States
LanguageEnglish
FormatPages: 4294-4298
System Entry Date2001 May 13

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