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Modulation of the ERK pathway of signal transduction by cysteine proteinase inhibitors
Journal article   Peer reviewed

Modulation of the ERK pathway of signal transduction by cysteine proteinase inhibitors

C Torres, M Li, R Walter and F Sierra
Journal of cellular biochemistry, v 80(1)
18 Sep 2000
PMID: 11029750

Abstract

Amino Acid Sequence Animals Base Sequence Cells, Cultured Cysteine Proteinase Inhibitors - pharmacology DNA Primers Down-Regulation - drug effects Hydrolysis Kinetics Mice Mitogen-Activated Protein Kinases - metabolism Molecular Sequence Data Signal Transduction - drug effects
Cell proliferation requires the coordinate synthesis and degradation of many proteins. In addition to the well-characterized involvement of the proteasome in the degradation of several cell cycle-regulated proteins, it has been established that cysteine proteinases are also involved in the control of cell proliferation, but their role is currently not understood. By using both synthetic cysteine proteinase inhibitors and overexpression of T-kininogen (T-KG), a physiologically relevant cysteine proteinase inhibitor, we show that inhibition of cysteine proteinases results in a severe inhibition of the ERK pathway of signal transduction. Mechanistically, this effect appears to be the result of stabilization of the ERK phosphatase MKP-1, which leads to an enhanced dephosphorylation (and hence inactivation) of ERK molecules. These results are specific to cysteine proteinase inhibitors and are not observed when either serine proteinases or the proteasome are inhibited. We hypothesize that inhibition of cysteine proteinases in vivo leads to a dysregulation of the ERK pathway, which results in an inability of the cell to transmit to the nucleus the signals generated by the presence of growth factors, thus resulting in loss of cell proliferation.

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Collaboration types
Domestic collaboration
International collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
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