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Heterogeneity of metalloprotease expression in Trypanosoma cruzi

Published online by Cambridge University Press:  06 April 2009

C. M. Lowndes ,
M. C. Bonaldo ,
N. Thomaz  and
S. Goldenberg
C. M. Lowndes
Affiliation:
Departamento de Epidemiologia, Escola Nacional de Saúde Pública; Função Oswaldo Cruz, Avenida Brasil 4365, 21040–900, Rio de Janeiro, RJ, Brazil
M. C. Bonaldo
Affiliation:
Departamento de Bioquimica e Biologia Molecular
N. Thomaz
Affiliation:
Departamento de Protozoologia, Institute Oswaldo Cruz
S. Goldenberg
Affiliation:
Departamento de Bioquimica e Biologia Molecular
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Summary

Expression of metalloprotease activities during metacyclogenesis of a series of strains and clones of Trypanosoma cruzi was investigated using SDS-polyacrylamide gel electrophoresis with a range of different co-polymerized proteolytic substrates. A complex pattern of metalloprotease expression, with considerable quantitative and qualitative variability between strains and life-cycle stages, was apparent. This is in contrast to previously published data, and data presented in this study, which demonstrate a high degree of conservation of expression of cysteine proteases in different strains and clones of T. cruzi. All the metalloprotease activities identified partitioned into the detergent phase of a Triton X-114 extract, suggesting that they are membrane-bound. Developmental regulation of expression during metacyclogenesis, either in terms of quantity, or in terms of difference in relative amounts of different isoforms, was apparent for all isolates studied except CL14. However, a clearly metacyclic-specific/metacyclic-enriched metalloprotease was detected only in T. cruzi Dm28c and 383, and our results demonstrate that a metacyclic-specific metalloprotease common to all isolates of the parasite could not be detected, at least at this level of analysis.

Keywords

Trypanosoma cruzimetacyclogenesismetalloproteasescysteine proteasesheterogeneity
Type
Research Article
Information
Parasitology , Volume 112 , Issue 4 , April 1996 , pp. 393 - 399
Copyright
Copyright © Cambridge University Press 1996

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