Selective purification and characterization of adiponectin multimer species from human plasma.

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.

authors

Hada Y,Yamauchi T,Waki H,Tsuchida A,Hara K,Yago H,Miyazaki O,Ebinuma H,Kadowaki T

doi

10.1016/j.bbrc.2007.03.004

subject

Has Abstract

pub_date

2007-05-04 00:00:00

pages

487-93

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)00469-X

journal_volume

356

pub_type

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