Molecular interactions of Leishmania promastigote surface protease with human alpha 2-macroglobulin.

Abstract:

:The interaction of Leishmania promastigote surface protease (PSP) with the plasmatic protease inhibitor alpha 2-macroglobulin (alpha 2M) was investigated. In plasma, solubilized PSP forms covalent complexes only with alpha 2M, at the exclusion of other protease inhibitors. The formation of complexes is accompanied by the proteolytic cleavage of the alpha 2M subunit and by the transition from the 'slow' to the 'fast' form of alpha 2M. The proteolytic activity of solubilized PSP on azocasein is inhibited by alpha 2M. In contrast, we found no evidence for a specific interaction of alpha 2M with the surface of promastigotes and PSP proteolytic activity on intact cells was not inhibited by alpha 2M.

journal_name

Mol Biochem Parasitol

authors

Heumann D,Burger D,Vischer T,de Colmenares M,Bouvier J,Bordier C

doi

10.1016/0166-6851(89)90043-1

subject

Has Abstract

pub_date

1989-02-01 00:00:00

pages

67-72

issue

1

eissn

0166-6851

issn

1872-9428

pii

0166-6851(89)90043-1

journal_volume

33

pub_type

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