细胞内
化学
细胞生物学
增强子
生物化学
基因
生物
基因表达
作者
Shweta Tyagi,Jean‐Philippe Salier,Sunil K. Lal
标识
DOI:10.1006/abbi.2001.2745
摘要
α-1-Microglobulin (A1M) and bikunin are two plasma glycoproteins encoded by an α-1-microglobulin/bikunin precursor (AMBP) gene. Despite their lack of any structural or functional relationship, both A1M and bikunin originate from AMBP cleavage by a furin-like protease that releases the two mature molecules. The AMBP gene maintains a tight control over its expression by a unique enhancer, which is controlled by several hepatocyte-enriched nuclear factors; however, the mechanisms of regulation of the intracellular levels of the AMBP protein are currently unknown. We report the ability of the AMBP protein to self-associate and form a dimer in a yeast environment using the yeast two-hybrid system and an in vitro dimerization assay. We also show that the A1M protein binds to its precursor protein, AMBP, whereas bikunin does not. This observation warrants further investigations for a dimerization-dependent intracellular control that AMBP may be involved in. The relevance of AMBP dimerization and its possible biological significance are postulated.
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