The liver-specific human alpha(1)-microglobulin/bikunin precursor (AMBP) is capable of self-association

alpha-1-Microglobulin (A1M) and bikunin are two plasma glycoproteins encoded by an alpha-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 ma...

Full description

Saved in:
Bibliographic Details
Published in:Archives of biochemistry and biophysics 2002-03, Vol.399 (1), p.66-72
Main Authors: Tyagi, Shweta, Salier, Jean-Philippe, Lal, Sunil K
Format: Article
Language:English
Subjects:
Alpha-Globulins - metabolism
Dimerization
Humans
Liver - chemistry
Membrane Glycoproteins - metabolism
Protein Biosynthesis
Protein Precursors - genetics
Protein Precursors - metabolism
Serum Globulins - genetics
Serum Globulins - metabolism
Transcription, Genetic
Trypsin Inhibitor, Kunitz Soybean
Two-Hybrid System Techniques
Yeasts - genetics
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:alpha-1-Microglobulin (A1M) and bikunin are two plasma glycoproteins encoded by an alpha-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.
ISSN:0003-9861
DOI:10.1006/abbi.2001.2745