Journal article

Sialic Acid Modification of Adiponectin Is Not Required for Multimerization or Secretion but Determines Half-Life in Circulation

Ayanthi A Richards, Michelle L Colgrave, Jialiang Zhang, Julie Webster, Fiona Simpson, Elaine Preston, Donna Wilks, Kyle L Hoehn, Matthew Stephenson, Graeme A Macdonald, John B Prins, Gregory J Cooney, Aimin Xu, Jonathan P Whitehead



Adiponectin is an adipocyte-secreted, insulin-sensitizing hormone the circulating levels of which are reduced in conditions of insulin resistance and diabetes. Previous work has demonstrated the importance of posttranslational modifications, such as proline hydroxylation and lysine hydroxylation/glycosylation, in adiponectin oligomerization, secretion, and function. Here we describe the first functional characterization of adiponectin sialylation. Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin. Enzymatic removal of sialic acid or its underlying O-linked s..

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University of Melbourne Researchers