Inhibition of protein kinase C activity by the Leishmania donovani lipophosphoglycan.
Purified lipophosphoglycan from Leishmania donovani was found to inhibit the activity of protein kinase C isolated from rat brain. Protein kinase C inhibition by lipophosphoglycan was continuous for 30 minutes. The glycoconjugate was a competitive inhibitor with respect to diolein, a noncompetitive inhibitor with respect to phosphatidylserine, and had no significant effect on protein kinase M and protein kinase A. A possible physiological role of lipophosphoglycan as a negative effector of protein kinase C is suggested.
Department of Biochemistry, University of Kentucky Medical Center, Lexington 40536.
T B
TB
McNeely
S J
SJ
Turco
D000818:Animals; D001921:Brain / Q000201:enzymology; D004187:Disaccharides / Q000302:isolation & purification / Q000494:pharmacology*; D007700:Kinetics; D007893:Leishmania donovani; D008246:Lysophospholipids / Q000302:isolation & purification / Q000494:pharmacology*; D011493:Protein Kinase C / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats
D004187:Disaccharides; D008246:Lysophospholipids; C025449:lysophosphatidylinositol; D011494:Protein Kinases; D011493:Protein Kinase C