Inhibitory effects of human α2-macroglobulin on Trypanosoma cruzi epimastigote proteinases

Adrián Ramos; M. Sara Remedi; Cecilia Sánchez; Gustavo Bonacci; Miguel A. Vides; Gustavo Chiabrando

doi:10.1016/S0001-706X(97)00110-1

Inhibitory effects of human α2-macroglobulin on Trypanosoma cruzi epimastigote proteinases

Adrián Ramos, M. Sara Remedi, Cecilia Sánchez, Gustavo Bonacci, Miguel A. Vides, Gustavo Chiabrando

Research output: Contribution to journal › Article › peer-review

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Abstract

The inactivation of Trypanosoma cruzi proteinases by human α2-macroglobulin (α2-M), a major plasma proteinase inhibitor was studied. Evidences regarding the interaction between α2-M and proteolytic enzymes contained in crude cell-free extracts of T. cruzi were derived from electrophoretic and enzymatic assays. The former showed conformational and structural changes ocurring in α2M, as judged by the appearance of transformed 'fast' form on native PAGE; generation of bands of ~ 90 kDa on reduced SDS-PAGE and formation of covalent complexes enzyme-inhibitor on SDS-PAGE. On the other hand, the total proteolytic activity on azocasein dropped significantly in the presence of α2-M, although partial activity was still maintained. The proteinases detected as a double band of 44 and 53 kDa on gelatin SDS-PAGE were also inhibited by α2M. Results suggest that the study of specific interactions between α2-M and T. cruzi-proteinases, probably with cruzipain, could be biologically important in the fate of T. cruzi-infection and Chagas' disease.

Original language	English
Pages (from-to)	327-337
Number of pages	11
Journal	Acta Tropica
Volume	68
Issue number	3
DOIs	https://doi.org/10.1016/S0001-706X(97)00110-1
State	Published - Dec 1997

Keywords

Alpha 2-macroglobulin
Proteinases
Trypanosoma cruzi

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10.1016/S0001-706X(97)00110-1

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@article{c4705470c8964f3985270ce72cae1294,

title = "Inhibitory effects of human α2-macroglobulin on Trypanosoma cruzi epimastigote proteinases",

abstract = "The inactivation of Trypanosoma cruzi proteinases by human α2-macroglobulin (α2-M), a major plasma proteinase inhibitor was studied. Evidences regarding the interaction between α2-M and proteolytic enzymes contained in crude cell-free extracts of T. cruzi were derived from electrophoretic and enzymatic assays. The former showed conformational and structural changes ocurring in α2M, as judged by the appearance of transformed 'fast' form on native PAGE; generation of bands of ~ 90 kDa on reduced SDS-PAGE and formation of covalent complexes enzyme-inhibitor on SDS-PAGE. On the other hand, the total proteolytic activity on azocasein dropped significantly in the presence of α2-M, although partial activity was still maintained. The proteinases detected as a double band of 44 and 53 kDa on gelatin SDS-PAGE were also inhibited by α2M. Results suggest that the study of specific interactions between α2-M and T. cruzi-proteinases, probably with cruzipain, could be biologically important in the fate of T. cruzi-infection and Chagas' disease.",

keywords = "Alpha 2-macroglobulin, Proteinases, Trypanosoma cruzi",

author = "Adri{\'a}n Ramos and Remedi, {M. Sara} and Cecilia S{\'a}nchez and Gustavo Bonacci and Vides, {Miguel A.} and Gustavo Chiabrando",

note = "Funding Information: This work was supported by grants from the Consejo de Investigaciones Cient{\'ı}ficas y Tecnol{\'o}gicas de la Provincia de C{\'o}rdoba (CONICOR) and the Secretar{\'ı}a de Ciencia y Tecnolog{\'ı}a de la Universidad Nacional de C{\'o}rdoba (SeCyT). We thank Mrs Y. Medina-Orsingher for language assistance.",

year = "1997",

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doi = "10.1016/S0001-706X(97)00110-1",

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volume = "68",

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T1 - Inhibitory effects of human α2-macroglobulin on Trypanosoma cruzi epimastigote proteinases

AU - Ramos, Adrián

AU - Remedi, M. Sara

AU - Sánchez, Cecilia

AU - Bonacci, Gustavo

AU - Vides, Miguel A.

AU - Chiabrando, Gustavo

N1 - Funding Information: This work was supported by grants from the Consejo de Investigaciones Cientı́ficas y Tecnológicas de la Provincia de Córdoba (CONICOR) and the Secretarı́a de Ciencia y Tecnologı́a de la Universidad Nacional de Córdoba (SeCyT). We thank Mrs Y. Medina-Orsingher for language assistance.

PY - 1997/12

Y1 - 1997/12

N2 - The inactivation of Trypanosoma cruzi proteinases by human α2-macroglobulin (α2-M), a major plasma proteinase inhibitor was studied. Evidences regarding the interaction between α2-M and proteolytic enzymes contained in crude cell-free extracts of T. cruzi were derived from electrophoretic and enzymatic assays. The former showed conformational and structural changes ocurring in α2M, as judged by the appearance of transformed 'fast' form on native PAGE; generation of bands of ~ 90 kDa on reduced SDS-PAGE and formation of covalent complexes enzyme-inhibitor on SDS-PAGE. On the other hand, the total proteolytic activity on azocasein dropped significantly in the presence of α2-M, although partial activity was still maintained. The proteinases detected as a double band of 44 and 53 kDa on gelatin SDS-PAGE were also inhibited by α2M. Results suggest that the study of specific interactions between α2-M and T. cruzi-proteinases, probably with cruzipain, could be biologically important in the fate of T. cruzi-infection and Chagas' disease.

AB - The inactivation of Trypanosoma cruzi proteinases by human α2-macroglobulin (α2-M), a major plasma proteinase inhibitor was studied. Evidences regarding the interaction between α2-M and proteolytic enzymes contained in crude cell-free extracts of T. cruzi were derived from electrophoretic and enzymatic assays. The former showed conformational and structural changes ocurring in α2M, as judged by the appearance of transformed 'fast' form on native PAGE; generation of bands of ~ 90 kDa on reduced SDS-PAGE and formation of covalent complexes enzyme-inhibitor on SDS-PAGE. On the other hand, the total proteolytic activity on azocasein dropped significantly in the presence of α2-M, although partial activity was still maintained. The proteinases detected as a double band of 44 and 53 kDa on gelatin SDS-PAGE were also inhibited by α2M. Results suggest that the study of specific interactions between α2-M and T. cruzi-proteinases, probably with cruzipain, could be biologically important in the fate of T. cruzi-infection and Chagas' disease.

KW - Alpha 2-macroglobulin

KW - Proteinases

KW - Trypanosoma cruzi

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Inhibitory effects of human α2-macroglobulin on Trypanosoma cruzi epimastigote proteinases

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