Action of lysosomal phospholipase A1 on bis(monoacylglycerol)phosphate.
Bis(monoacylglycerol)phosphate (BMP) in macrophages is known to rapidly turn over its acyl moiety(s) located at primary positions of the glycerols, yet the glycerols and phosphate remain stable within the BMP molecule. Here we examine whether the phospholipase A1 isolated from rat-liver lysosomes is capable of deacylating BMP. By comparison with the precursor of BMP, phosphatidylglycerol, BMP is a very poor substrate for the phospholipase A1. We conclude, therefore, that a direct deacylation of the acyl groups at the primary alcohol level of the glycerol probably does not occur, but postulate that transacylations may occur to account for the removal of the acyl moiety.
Waite
M
M
Department of Biochemistry, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, NC 27157-1016.
Osthoff
G
G
Sisson
P
P
Thuren
T
T
D000818:Animals; D005994:Glycerophosphates / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008247:Lysosomes / Q000201:enzymology*; D010715:Phosphatidylglycerols / Q000378:metabolism; D010741:Phospholipases A / Q000378:metabolism*; D054466:Phospholipases A1; D051381:Rats; D013379:Substrate Specificity
D005994:Glycerophosphates; D010715:Phosphatidylglycerols; D010741:Phospholipases A; D054466:Phospholipases A1