adiponectinbinding

Adiponectinbinding denotes the set of molecular interactions between adiponectin, a hormone produced mainly by adipose tissue, and its cellular receptors and binding partners. Adiponectin exists in multiple forms, including trimers, hexamers, and high‑molecular-weight multimers, as well as a globular fragment. The form can influence how and where binding occurs and which signaling pathways are engaged.

The primary adiponectin binding partners are the receptors AdipoR1 and AdipoR2. AdipoR1 is enriched in skeletal muscle and has a higher affinity for globular adiponectin, while AdipoR2 is more prominent in the liver and prefers full-length adiponectin. Binding of adiponectin to these receptors activates signaling cascades that promote metabolic regulation, notably through activation of AMP-activated protein kinase (AMPK) and PPAR-α pathways. A key feature of adiponectin receptor signaling is ceramidase activity, which shifts lipid metabolism by converting ceramide to sphingosine and then sphingosine-1-phosphate, contributing to improved insulin sensitivity and fatty-acid oxidation.

In addition to AdipoR1 and AdipoR2, the glycoprotein T‑cadherin (Cadherin-13) can bind adiponectin, particularly its hexameric and high-molecular-weight forms, without directly triggering intracellular signaling. This binding is thought to influence adiponectin distribution and local tissue concentrations, affecting overall adiponectin bioavailability.

Clinical and research relevance: adiponectinbinding is linked to metabolic health, with lower adiponectin levels or impaired receptor binding associated with obesity, type 2 diabetes, and inflammatory states. Studying binding interactions employs binding assays, structural analyses, and receptor knockout or overexpression models to dissect signaling outcomes and therapeutic potential.