Effects of sialic acid and sialoglycoconjugates on cytosolic phospholipases A2 from bovine brain.
Two forms of Ca(2+)-independent cytosolic phospholipases A2 were separated by Sephadex G-75 column chromatography. N-Acetylneuraminic acid, gangliosides, and sialoglycoproteins inhibited both phospholipases A2 in a concentration dependent manner, but colominic acid, poly(2,8-N-acetylneuraminic acid), had no effect on enzymic activities. Interactions between phospholipases A2 and sialoglycoconjugates may be involved in the translocation of phospholipases A2 from cytosol to plasma membrane during receptor stimulation.
Yang
H C
HC
Department of Medical Biochemistry, Ohio State University, Columbus 43210.
Farooqui
A A
AA
Horrocks
L A
LA
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D002850:Chromatography, Gel; D005732:Gangliosides / Q000494:pharmacology*; D006001:Glycoconjugates / Q000494:pharmacology; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D019158:N-Acetylneuraminic Acid; D010741:Phospholipases A / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D011134:Polysaccharides / Q000494:pharmacology; D012794:Sialic Acids / Q000494:pharmacology*; D012795:Sialoglycoproteins / Q000494:pharmacology*
D005732:Gangliosides; D006001:Glycoconjugates; D007527:Isoenzymes; D011134:Polysaccharides; D012794:Sialic Acids; D012795:Sialoglycoproteins; C014420:colominic acid; D010741:Phospholipases A; D019158:N-Acetylneuraminic Acid