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PMID: 8335086 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

The lysosomal gp63-related protein in Leishmania mexicana amastigotes is a soluble metalloproteinase with an acidic pH optimum.

FEBS letters ·Vol. 327 ·No. 1 ·1993-07-19 ·Pages 103-7

Ilg T, Harbecke D, Overath P

Abstract

Leishmania mexicana amastigotes express a lysosomal protein, which is antigenically related to the promastigote surface metalloproteinase (gp63). It is shown that the purified gp63-related protein from amastigote is also an active metalloproteinase. The pH-optimum of the enzyme is acidic, similar to lysosomal cysteine proteinases, but distinct from the neutral to basic pH-optimum of the promastigote surface proteinase. This study appears to be the first report on a metalloproteinase with a lysosomal localization.

MeSH Terms
Acids Animals Chromatography, Gel Cysteine Endopeptidases/isolation & purification,metabolism Electrophoresis, Polyacrylamide Gel Enzyme Activation Hydrogen-Ion Concentration Leishmania mexicana/enzymology,metabolism Lysosomes/metabolism Membrane Glycoproteins/isolation & purification,metabolism Metalloendopeptidases/isolation & purification,metabolism Mice Mice, Inbred BALB C Mice, Inbred CBA Proteins/isolation & purification,metabolism Solubility
Chemicals
Acids Membrane Glycoproteins Proteins lysosomal proteins Cysteine Endopeptidases Metalloendopeptidases glycoprotein gp63, Leishmania
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ilg T
Max-Planck-Institut für Biologie, Tübingen, Germany.
Harbecke D
Overath P
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1993-07-19
Pages
103-7
Language
English
Region
England
NLM ID
0155157
Subset
IM
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