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Blood, 1 March 2002, Vol. 99, No. 5, pp. 1850-1852
BRIEF REPORT
Calpain is a signal transducer and activator of transcription
(STAT) 3 and STAT5 protease
Atsushi Oda,
Hiroshi Wakao, and
Hiroyoshi Fujita
From the Laboratory of Environmental Biology,
Department of Preventive Medicine, Hokkaido University School of
Medicine, Sapporo, and the Helix Research Institute, Chiba, Japan.
Truncation of signal transducer and activator of transcription
(STAT) 5 at the carboxy-terminal domain, either by genetic engineering
or by proteolytic cleavage, results in generation of dominant-negative
forms. A nuclear serine protease expressed in the myeloid precursor
cells is known to mediate this cleavage, but other proteases
responsible for this reaction were unknown. We found that calpain, a
ubiquitously expressed cysteine protease, also trims STAT5 in vivo and
in vitro, within the carboxy-terminal domain. Nuclear element is not
necessary for calpain-mediated STAT5 cleavage, since this process
occurs in platelets. We also found that STAT3 is a substrate for
calpain in vivo and in vitro, indicating that calpain-mediated cleavage
is a common feature of STAT3 and STAT5. Thus, our study reveals a novel
pathway for posttranslational modification of STAT3 and STAT5.
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