Examining Adiponectin’s Interaction with Basic Fibroblast Growth Factor to Understand its Regulatory Effects on Angiogenesis

Cody McCullough


Angiogenesis is the process of forming blood vessels from pre-existing ones. Importantly, it is known that uncontrolled angiogenesis is an underlying cause of many types of cancers and other diseases. As such, understanding its regulation is vital in drug research where the goal is to target such devastating illnesses. One very crucial regulator of angiogenesis is basic fibroblast growth factor (bFGF), which itself has been shown to be regulated by the protein adiponectin. Adiponectin is a protein which is specifically secreted from adipocytes, or fat cells. It has been shown to regulate the biological activity of several growth factors, including bFGF, by interfering with their bioavailability at a pre-receptor level. It is this interference that may explain adiponectin’s inhibitory functions of angiogenesis. In this study, we wished to examine the binding interactions of both full-length and globular region recombinant human adiponectin independently with recombinant human bFGF to better understand adiponectin’s association. Through the use of Surface Plasmon Resonance (SPR) we show that the kinetic interactions of fulllength human adiponectin, and of just the isolated globular region, each with bFGF are remarkably similar. This suggests that most if not all of the binding interactions are mediated through the head groups of adiponectin, which is a novel finding. These results may aid in a better understanding of the molecular and structural basis of adiponectin’s interactions with bFGF as well as other growth factors that are crucial regulators of angiogenesis. Moreover, the novel findings of the binding action of adiponectin with bFGF may lead to further research of adiponectin as an anti-angiogenic therapeutic drug.


Adiponectin, Anti-angiogenesis, Basic Fibroblast Growth Factor

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