Abstract:
:Adiponectin is an adipocyte-derived hormone and known to form several species of multimer, however, the precise components of each multimer have not been fully determined. We purified each multimer adiponectin selectively from human plasma and characterized them by affinity columns using anti-adiponectin, gelatin, or anti-albumin antibody and gel filtration. We found that adiponectin exists as four species of multimers in human plasma. According to their migrating mobility and N-terminal amino acid analysis, we defined them as a trimer, albumin-binding trimer, hexamer, and HMW. Low pH shifted HMW to hexamer, raising the possibility that HMW is a 12 mer or larger multimer. We also showed that HMW had the highest binding activity to the membrane fractions of C2C12 myocytes and activated AMPK most potently. Our results indicate that adiponectin forms diverse multimer species and at least some of the functional properties are dependent on a multimer status.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Hada Y,Yamauchi T,Waki H,Tsuchida A,Hara K,Yago H,Miyazaki O,Ebinuma H,Kadowaki Tdoi
10.1016/j.bbrc.2007.03.004subject
Has Abstractpub_date
2007-05-04 00:00:00pages
487-93issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(07)00469-Xjournal_volume
356pub_type
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