Abstract:
: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.
journal_name
J Cell Biochemjournal_title
Journal of cellular biochemistryauthors
Torres C,Li M,Walter R,Sierra Fdoi
10.1002/1097-4644(20010101)80:1<11::aid-jcb20>3.3.subject
Has Abstractpub_date
2000-09-18 00:00:00pages
11-23issue
1eissn
0730-2312issn
1097-4644pii
10.1002/1097-4644(20010101)80:1<11::AID-JCB20>3.0.journal_volume
80pub_type
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