Evidence for phospholipases from Trypanosoma cruzi active on phosphatidylinositol and inositolphosphoceramide

被引:23
作者
Bertello, LE
Alves, MJM
Colli, W
de Lederkremer, RM
机构
[1] Univ Buenos Aires, Fac Ciencias Exactas & Nat, Dept Quim Organ, CIHIDECAR, RA-1428 Buenos Aires, DF, Argentina
[2] Univ Sao Paulo, Dept Bioquim, Inst Quim, BR-05599970 Sao Paulo, Brazil
关键词
ceramide; glycoinositolphospholipids; inositol-phosphoceramide; phospholipases A; phospholipase C;
D O I
10.1042/0264-6021:3450077
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The lipid moiety in the glycosylphosphatidylinositol anchors of glycoproteins of Trypanosoma cruzi consists of an alkylacylglycerol, a lysoalkylglycerol or a ceramide. Previously, we showed that the inositolphosphoceramides (IPCs) are the major components in the precursor inositolphospholipids of epimastigote and trypomastigote forms. Using H-3-labelled subfractions of IPC, phosphatidylinositol (PI) and glycoinositolphospholipids (GIPLs) as substrates with a cell-free system, we now demonstrate the association of at least five enzyme activities with the trypanosomal membranous particulate material. These include: phospholipase A(1) and phospholipase A(2), enzymes that release free fatty acid from the PI and GIPLs; an acyltransferase responsible for the acylation of the generated monoacyl or monoalkylglycero-lipids with endogenous unlabelled fatty acid; two activities of phospholipase C, one releasing ceramide from IPC and the other alkylacylglycerol, alkylglycerol or diacylglycerol from PI. The neutral lipids were also generated on incubation of the GIPLs. The phospholipase C activities were inhibited by p-chloro-mercuriphenylsulphonic acid, as reported for other PI phospholipases C. An IPC-fatty-acid hydrolase, releasing fatty acid from the labelled IPC, was also observed. The enzyme activities reported in the present study may be acting in remodelling reactions leading to the anchor of the mature glycoproteins of T. cruzi.
引用
收藏
页码:77 / 84
页数:8
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