Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin

• Published in: The Journal of biological chemistry Vol. 278; no. 41; pp. 40352 - 40363
• Main Authors: Waki, Hironori, Yamauchi, Toshimasa, Kamon, Junji, Ito, Yusuke, Uchida, Shoko, Kita, Shunbun, Hara, Kazuo, Hada, Yusuke, Vasseur, Francis, Froguel, Philippe, Kimura, Satoshi, Nagai, Ryozo, Kadowaki, Takashi
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 10.10.2003
• Subjects: 3T3 Cells; Adiponectin; Amino Acid Sequence; Animals; Base Sequence; Diabetes Mellitus - blood; Diabetes Mellitus - genetics; Disulfides - chemistry; DNA, Complementary - genetics; Female; Genetics; Human genetics; Humans; In Vitro Techniques; Intercellular Signaling Peptides and Proteins; Life Sciences; Male; Mice; Models, Molecular; Molecular Sequence Data; Molecular Structure; Molecular Weight; Mutagenesis, Site-Directed; Mutation; Protein Structure, Quaternary; Proteins - chemistry; Proteins - genetics; Recombinant Proteins - chemistry; Recombinant Proteins - genetics

Adiponectin is an adipocyte-derived hormone, which has been shown to play important roles in the regulation of glucose and lipid metabolism. Eight mutations in human adiponectin have been reported, some of which were significantly related to diabetes and hypoadiponectinemia, but the molecular mechan...