Annexin II (p36) and p11, which belong to two different families of calcium-binding proteins, are able to form a heterotetrameric protein complex (p36)2(p11)2 called calpactin I. As these proteins were detectable only in the presence of each other in a variety of cell lines, we studied the mechanisms of regulation of cellular levels of annexin II and p11. In cells expressing p11 messenger RNA, p11 protein is undetectable unless annexin II is also expressed. As an example, the hepatoblastoma HepG2 cell line displays no detectable annexin II nor p11 protein, although it expresses p11 mRNA. The overexpression of annexin II by gene transfer into HepG2 cells leads to the up-regulation of the cellular levels of p11 by a post-translational mechanism. In the presence of annexin II, there is no major change in the p11 transcript levels, but the half-life of the p11 protein is increased more than 6-fold. Thus, the degree of expression of annexin II, which varies according to different states of cellular differentiation and transformation, is an essential factor in the regulation of cellular levels of p11.
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January 1996
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January 01 1996
Annexin II up-regulates cellular levels of p11 protein by a post-translational mechanisms Available to Purchase
Alain PUISIEUX;
Alain PUISIEUX
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*To whom correspondence should be addressed.
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Jingwei JI;
Jingwei JI
1Laboratoire d'Oncologie Moléculaire, INSERM CJF 9302, Centre Léon Bérard, 69373 Lyon, France
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Mehmet OZTURK
Mehmet OZTURK
1Laboratoire d'Oncologie Moléculaire, INSERM CJF 9302, Centre Léon Bérard, 69373 Lyon, France
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1996
1996
Biochem J (1996) 313 (1): 51–55.
Citation
Alain PUISIEUX, Jingwei JI, Mehmet OZTURK; Annexin II up-regulates cellular levels of p11 protein by a post-translational mechanisms. Biochem J 1 January 1996; 313 (1): 51–55. doi: https://doi.org/10.1042/bj3130051
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