Modification of N-glycosylation modulates the secretion and lipolytic function of apoptosis inhibitor of macrophage (AIM) |
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Authors: | Mayumi MoriHiroki Kimura Yoshihiro IwamuraSatoko Arai Toru Miyazaki |
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Institution: | Laboratory of Molecular Biomedicine for Pathogenesis, Center for Disease Biology and Integrative Medicine, Faculty of Medicine, The University of Tokyo, Tokyo 113-0033, Japan |
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Abstract: | The mouse macrophage-derived apoptosis inhibitor of macrophage (AIM), which is incorporated into adipocytes and induces lipolysis by suppressing fatty acid synthase (FAS) activity, possesses three potential N-glycosylation sites. Inactivation of N-glycosylation sites revealed that mouse AIM contains two N-glycans in the first and second scavenger receptor cysteine-rich domains, and that depletion of N-glycans decreased AIM secretion from producing cells. Interestingly, the lack of N-glycans increased AIM lipolytic activity through enhancing AIM incorporation into adipocytes. Although human AIM contains no N-glycan, attachment of N-glycans increased AIM secretion. Thus, the N-glycosylation plays important roles in the secretion and lipolytic function of AIM.Structured summary of protein interactionsAIMphysically interacts with FAS by anti tag coimmunoprecipitation (View interaction) |
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Keywords: | AIM apoptosis inhibitor of macrophage SRCR scavenger receptor cysteine-rich FSP27 fat-specific protein 27 TLR toll-like receptor FAS fatty acid synthase QPCR quantitative RT-PCR IL-6 interleukin-6 Saa-3 serum amyloid A-3 DEX dexamethasone IBMX isobutylmethylxanthine |
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