Evidence for association of an ATP-stimulatable Ca(2+)-independent phospholipase A2 from pancreatic islets and HIT insulinoma cells with a phosphofructokinase-like protein

Biochemistry
Sasanka RamanadhamJohn Turk

Abstract

Glucose-induced insulin secretion from pancreatic islets requires metabolism of glucose within islet beta-cells, and ATP has attracted interest as a messenger of glucose metabolism within beta-cells. Glucose-induced insulin secretion from islets and HIT insulinoma cells is accompanied by activation of an ATP-stimulatable Ca(2+)-independent phospholipase A2 (ASCI-PLA2) enzyme, the catalytic activity of which resides in a 40 kDa protein. An analogous PLA2 enzyme in myocardium was recently found to consist of a complex of a 40 kDa catalytic protein with a tetramer of an isoform of the glycolytic enzyme phosphofructokinase (PFK). Association of the PFK isoform with the myocardial PLA2 catalytic protein was found to confer ATP sensitivity onto the enzyme complex. Here we demonstrate that the majority of HIT cell and islet ASCI-PLA2 catalytic activity elutes from a gel filtration column in a region corresponding to 400 kDa, suggesting that the 40 kDa beta-cell ASCI-PLA2 catalytic protein exists as part of a larger molecular mass complex. Islet and HIT cell ASCI-PLA2 activities were immunoprecipitated by antibodies directed against PFK, and the immunoprecipitates contained 40 and 85 kDa proteins which correspond to the molecular masse...Continue Reading

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Citations

Jul 9, 1999·Biochimica Et Biophysica Acta·S E BarbourC L Deal
Nov 27, 2009·American Journal of Physiology. Cell Physiology·Juan LiDonald D Denson
Mar 28, 1997·The Journal of Biological Chemistry·J TangS S Jones
May 30, 2015·Journal of Lipid Research·Sasanka RamanadhamXiaoyong Lei
Dec 13, 2000·The Journal of Biological Chemistry·D D DensonD C Eaton
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Jan 31, 1997·The Journal of Biological Chemistry·E RocheM Prentki
Jan 14, 1999·The American Journal of Physiology·D D DensonD C Eaton

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