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Titolo:
LIPID-METABOLISM IN TRYPANOSOMA-BRUCEI - UTILIZATION OF MYRISTATE ANDMYRISTOYLLYSOPHOSPHATIDYLCHOLINE FOR MYRISTOYLATION OF GLYCOSYL PHOSPHATIDYLINOSITOLS
Autore:
WERBOVETZ KA; ENGLUND PT;
Indirizzi:
JOHNS HOPKINS UNIV,SCH MED,DEPT BIOL CHEM BALTIMORE MD 21205
Titolo Testata:
Biochemical journal
, volume: 318, anno: 1996,
parte:, 2
pagine: 575 - 581
SICI:
0264-6021(1996)318:<575:LIT-UO>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
VARIANT SURFACE GLYCOPROTEIN; FATTY-ACID-BINDING; AFRICAN TRYPANOSOMES; MEMBRANE ANCHOR; BIOSYNTHESIS; PROTEIN; ALBUMIN; PLASMA; BLOOD; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
K.A. Werbovetz e P.T. Englund, "LIPID-METABOLISM IN TRYPANOSOMA-BRUCEI - UTILIZATION OF MYRISTATE ANDMYRISTOYLLYSOPHOSPHATIDYLCHOLINE FOR MYRISTOYLATION OF GLYCOSYL PHOSPHATIDYLINOSITOLS", Biochemical journal, 318, 1996, pp. 575-581

Abstract

Myristate is the exclusive fatty acid species in the glycosyl phosphatidylinositol (GPI) anchor of the Trypanosoma brucei variant surface glycoprotein (VSG). [H-3]Myristate can be incorporated into T. brucei GPIs by two distinct processes known as fatty acid remodelling and myristate exchange. Myristoyllysophosphatidylcholine (M-LPC) can also serve as a myristate donor for VSG in trypanosomes [Bowes, Samad, Jiang, Weaver and Mellors (1993) J. Biol. Chem. 268, 13885-13892]. We have studied in detail the myristoylation of GPIs using a [H-3]M-LPC substrate. Labelling of VSG and free GPIs by [H-3]M-LPC in cultured trypanosomes occurred at the same rate as with [H-3]myristate. Concurrent with GPI labelling, there was rapid hydrolysis of[H-3]M-LPC to generate extracellular [H-3]myristate. Experiments in a trypanosomal cell-free system indicated that GPI labelling by fatty acid remodelling and myristateexchange was also equally efficient with [H-3]M-LPC and [H-3]myristate. Furthermore, both ATP and CoA are required for the myristoylation of GPIs by [H-3]M-LPC. These experiments suggest that GPI myristoylation from M-LPC involves hydrolysis of M-LPC to free myristate. To address the physiological importance of myristate and M-LPC in VSG myristoylation, we radiolabelled trypanosomes in vivo with both substrates in medium containing serum,and found that [H-3]myristate labelled VSG and GPIs more efficiently. Thus, VSG myristoylation by free myristate may be favoured in bloodstream trypanosome infections.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 09:46:54