Author： Matsushima-Nishiwaki R. Shidoji Y. Nishiwaki S. Moriwaki H. Muto Y.
Publisher： Elsevier
ISSN： 0006-291X
Source： Biochemical and Biophysical Research Communications, Vol.225, Iss.3, 1996-08, pp. : 946-951
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Abstract
Recently, we have found two major physiological forms of retinoid X receptor alpha (RXRalpha): the mature 54 kDa RXRalpha and the truncated 44 kDa RXRalpha lacking a portion of N-terminal A/B domain in human and rodent livers. In this communication, we show that m-calpain was active to digest 54 kDa RXRalpha in the human hepatoma-derived cell line, HuH7, nuclei to 44 kDa fragment through 47 kDa intermediate in vitro. Although both proteolytic fragments were revealed by anti-RXRalpha antibody against its E-domain, neither fragment reacted with anti-RXRalpha antibody specific for A/B domain. The profile of the calpain-induced proteolytic fragmentation of RXRalpha was almost identical to that of endogenous RXRalpha in nonmalignant human and normal mouse liver nuclei. This is the first demonstration that RXRalpha is a substrate for m-calpain, strongly suggesting that the enzyme might also be involved in post-translational modification of the receptor in hepatocytes.
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