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J. Biol. Chem., Vol. 280, Issue 18, 18341-18347, May 6, 2005
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From the
Genome Research Centre and the Departments of Biochemistry and **Medicine, the University of Hong Kong, Hong Kong, China and the ¶Center for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland 1001, New Zealand
Adiponectin, an adipocyte-specific secretory protein, is present in serum as three oligomeric complexes. Apart from its roles as an anti-diabetic and anti-atherogenic hormone, adiponectin has been implicated as an important regulator of cell growth and tissue remodeling. Here we show that some of these functions might be mediated by the specific interactions of adiponectin with several important growth factors. Among six different growth factors examined, adiponectin was found to bind with platelet-derived growth factor BB (PDGF-BB), basic fibroblast growth factor (FGF), and heparin-binding epidermal growth factor-like growth factor (HB EGF) with distinct affinities. The bindings of adiponectin with these growth factors are oligomerization-dependent. PDGF-BB bound to the high molecular weight (HMW) and middle molecular weight (MMW) complexes, but not to the low molecular weight (LMW) complex of adiponectin. Basic FGF preferentially interacted with the HMW form, whereas HB EGF bound to all three forms with comparable affinities. These three growth factors did not compete with each other for their bindings to adiponectin, suggesting the involvement of distinct binding sites. The interactions of adiponectin with PDGF-BB, basic FGF, and HB EGF precluded the bindings to their respective membrane receptors and attenuated the DNA synthesis and cell proliferation induced by these growth factors. Small interfering RNA-mediated down-regulation of adiponectin receptors did not affect the suppressive effects of adiponectin on cell proliferation stimulated by these growth factors. These data collectively suggest that the oligomeric complexes of adiponectin can modulate the biological actions of several growth factors by controlling their bioavailability at a pre-receptor level and that this effect might partly account for the anti-atherogenic, anti-angiogenic, and anti-proliferative functions of adiponectin.
Received for publication, February 1, 2005
* This work was supported by grants from the Marsden funds of the Royal Society of New Zealand (to Y. W.), Hong Kong Research Council Grant HKU 7486/04M (to A. X.), and a research and conference grant from the University of Hong Kong (to K. S. L. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
|| To whom correspondence should be addressed: Genome Research Center, Faculty of Medicine Bldg., the University of Hong Kong, 21 Sasson Rd., Pokfulam, Hong Kong Special Administrative Region, China. Tel.: 852-28199848; Fax: 852-28185653; E-mail: yuwanghk{at}hkucc.hku.hk.
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