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J. Biochem, 2004, Vol. 136, No. 3 399-405
© 2004 The Japanese Biochemical Society

CELL

Cleavage of Calnexin Caused by Apoptotic Stimuli: Implication for the Regulation of Apoptosis

Takenori Takizawa1,*, Chizuru Tatematsu1, Kimi Watanabe1, Kanefusa Kato1 and Yoshinobu Nakanishi2

1 Department of Molecular Neurobiology, Institute for Developmental Research, Aichi Human Service Center, Kasugai 480-0392; and 2 Graduate School of Medical Science, Kanazawa University, Kanazawa 920-0934

Calnexin is an endoplasmic reticulum (ER)-resident molecular chaperone that plays an essential role in the correct folding of membrane proteins. We found that calnexin is subjected to partial cleavage in apoptotic mouse cells. Both ER stress–inducing and ER stress–non-inducing apoptotic stimuli caused the cleavage of calnexin, indicating that this event does not always occur downstream of ER stress. The inhibition of caspases that target the amino acid sequence DXXD abrogated calnexin cleavage in apoptotic stimulus-treated cells. In addition, disruption of one of two DXXD sequences located in the cytoplasmic domain caused calnexin to escape cleavage during apoptosis. Furthermore, calnexin was cleaved in vitro by recombinant caspase-3 or caspase-7. Finally, the overexpression of a presumed cleavage product of calnexin partly inhibited apoptosis. These results collectively suggest that caspase-3 or caspase-7 cleaves calnexin, whose cleaved product leads to the attenuation of apoptosis.

* To whom correspondence should be addressed. Tel: +81-568-88-0829 ext 3582, Fax: +81-568-88-0829, E-mail: takizawa{at}inst-hsc.jp


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