Document Detail


Evidence for phospholipases from Trypanosoma cruzi active on phosphatidylinositol and inositolphosphoceramide.
MedLine Citation:
PMID:  10600641     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 (3)H-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 monoalkylglycerolipids 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-chloromercuriphenylsulphonic 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.
Authors:
L E Bertello; M J Alves; W Colli; R M de Lederkremer
Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  345 Pt 1     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  2000 Jan 
Date Detail:
Created Date:  2000-02-14     Completed Date:  2000-02-14     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  77-84     Citation Subset:  IM    
Affiliation:
CIHIDECAR, Departamento de Química Orgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, 1428 Buenos Aires, Argentina.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Cell-Free System
Enzyme Inhibitors / pharmacology
Glycosphingolipids / metabolism*
Phosphatidylinositol Diacylglycerol-Lyase
Phosphatidylinositols / metabolism*
Phospholipases / antagonists & inhibitors,  metabolism*
Phospholipases A / antagonists & inhibitors,  metabolism
Substrate Specificity
Trypanosoma cruzi / enzymology*
Type C Phospholipases / antagonists & inhibitors,  metabolism
Chemical
Reg. No./Substance:
0/Enzyme Inhibitors; 0/Glycosphingolipids; 0/Phosphatidylinositols; 0/inositolphosphoceramides; EC 3.1.-/Phospholipases; EC 3.1.1.-/Phospholipases A; EC 3.1.4.-/Type C Phospholipases; EC 4.6.1.13/Phosphatidylinositol Diacylglycerol-Lyase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Influence of spermine on intestinal maturation of the glycoprotein glycosylation process in neonatal...
Next Document:  Characterization of class II apurinic/apyrimidinic endonuclease activities in the human malaria para...