The oligomeric structure of high molecular weight adiponectin
Open Access
- 30 January 2007
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 581 (5) , 809-814
- https://doi.org/10.1016/j.febslet.2007.01.046
Abstract
There is great interest in the structure of adiponectin as its oligomeric state may specify its biological activities. It occurs as a trimer, a hexamer and a high molecular weight complex. Epidemiological data indicate that the high molecular weight form is significant with low serum levels in type 2 diabetics but to date, has not been well‐defined. To resolve this issue, characterization of this oligomer from bovine serum and 3T3‐L1 adipocytes by sedimentation equilibrium centrifugation and gel electrophoresis respectively, was carried out, revealing that it is octadecameric. Further studies by dynamic light scattering and electron microscopy established that bovine and possibly mouse high molecular weight adiponectin is C1q‐like in structure.Keywords
This publication has 34 references indexed in Scilit:
- Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndromeJournal of Clinical Investigation, 2006
- Mice Lacking Adiponectin Show Decreased Hepatic Insulin Sensitivity and Reduced Responsiveness to Peroxisome Proliferator-activated Receptor γ AgonistsJournal of Biological Chemistry, 2006
- Different effects of adiponectin isoforms in human monocytic cellsJournal of Leukocyte Biology, 2006
- Proteomic and functional characterization of endogenous adiponectin purified from fetal bovine serumProteomics, 2004
- Impaired Multimerization of Human Adiponectin Mutants Associated with DiabetesJournal of Biological Chemistry, 2003
- Oligomerization State-dependent Activation of NF-κB Signaling Pathway by Adipocyte Complement-related Protein of 30 kDa (Acrp30)Journal of Biological Chemistry, 2002
- Identification and Adipocyte Differentiation-dependent Expression of the Unique Disialic Acid Residue in an Adipose Tissue-specific Glycoprotein, Adipo QJournal of Biological Chemistry, 2001
- Electron microscopy of the complement protein C1q from the bullfrog, Rana catesbeianaEuropean Journal of Immunology, 1983
- Gross conformation of C1q: a subcomponent of the first component of complementBiochemistry, 1978
- Accessible area, packing volumes and interaction surfaces of globular proteinsNature, 1976