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- Title
Modification of N-glycosylation modulates the secretion and lipolytic function of apoptosis inhibitor of macrophage (AIM)
- Authors
Mori, Mayumi; Kimura, Hiroki; Iwamura, Yoshihiro; Arai, Satoko; Miyazaki, Toru
- Abstract
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 interactions: AIM physically interacts with FAS by anti tag coimmunoprecipitation (View interaction)
- Subjects
GLYCOSYLATION; LIPOLYSIS; APOPTOSIS; MACROPHAGES; LABORATORY mice; CYSTEINE
- Publication
FEBS Letters, 2012, Vol 586, Issue 20, p3569
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.08.017