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Title: The effects of a plant proteinase inhibitor from Enterolobium contortisiliquum on human tumor cell lines
Authors: Nakahata, Adriana Miti [UNIFESP]
Mayer, Barbara
Ries, Christian
Andrade de Paula, Claudia Alessandra [UNIFESP]
Karow, Marisa
Neth, Peter
Sampaio, Misako U. [UNIFESP]
Jochum, Marianne
Oliva, Maria Luiza V. [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Univ Munich
Keywords: cancer
Kunitz inhibitors
matrix metalloproteinases
mesenchymal stem cells
plant proteinases
Issue Date: 1-Apr-2011
Publisher: Walter de Gruyter & Co
Citation: Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 392, n. 4, p. 327-336, 2011.
Abstract: Supplementary to the efficient inhibition of trypsin, chymotrypsin, plasma kallikrein, and plasmin already described by the EcTI inhibitor from Enterolobium contortisiliquum, it also blocks human neutrophil elastase (K(iapp)=4.3 nM) and prevents phorbol ester (PMA)-stimulated activation of matrix metalloproteinase (MMP)-2 probably via interference with membrane-type 1 (MT1)-MMP. Moreover, plasminogen-induced activation of proMMP-9 and processing of active MMP-2 was also inhibited. Furthermore, the effect of EcTI on the human cancer cell lines HCT116 and HT29 (colorectal), SkBr-3 and MCF-7 (breast), K562 and THP-1 (leukemia), as well as on human primary fibroblasts and human mesenchymal stem cells (hMSCs) was studied. EcTI inhibited in a concentration range of 1.0-2.5 mu M rather specifically tumor cell viability without targeting primary fibroblasts and hMSCs. Taken together, our data indicate that the polyspecific proteinase inhibitor EcTI prevents proMMP activation and is cytotoxic against tumor cells without affecting normal tissue remodeling fibroblasts or regenerative hMSCs being an important tool in the studies of tumor cell development and dissemination.
ISSN: 1431-6730
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