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Papers In Press, published online ahead of print March 20, 2002
Dept. Biochem. Mol. Biol. in Disease, Atomic Bomb Disease Inst., Nagasaki Univ. Sch. Med., Nagasaki 852-8523
Corresponding Author: y-ihara{at}net.nagasaki-u.ac.jp
Calreticulin is a Ca2+-binding molecular chaperone of the lumen of the endoplasmic reticulum. Calreticulin has been shown to be essential for cardiac and neural development in mice, but the mechanism by which it functions in cell differentiation is not fully understood. To examine the role of calreticulin in cardiac differentiation, the calreticulin gene was introduced into rat cardiac myoblast H9c2 cells, and the effect of calreticulin overexpression on cardiac differentiation was examined. On culture in a differentiation medium containing fetal calf serum (1%) and retinoic acid (10 nM), cells transfected with the calreticulin gene were highly susceptible to apoptosis compared with controls. In the gene-transfected cells, protein kinase B/Akt signaling was significantly suppressed during the differentiation. Furthermore, PP2A, a Ser/Thr protein phosphatase, was significantly upregulated implying a suppression of Akt signaling due to dephosphorylation of Akt by the upregulated PP2A via the regulation of Ca2+ homeostasis. Thus, an overexpression of calreticulin promotes the differentiation-dependent apoptosis in H9c2 cells by suppressing the Akt signaling pathway. These findings indicate a novel mechanism in which cytoplasmic Akt signaling is modulated to cause apoptosis by a resident protein of the endoplasmic reticulum, calreticulin.
J. Biol. Chem, 10.1074/jbc.M112377200
Submitted on December 26, 2001
Revised on March 20, 2002
Accepted on March 20, 2002
Overexpression of calreticulin modulates protein kinase B /Akt signaling to promote apoptosis during cardiac differentiation of cardiomyoblast H9c2 cells
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