title: Modification of N-glycosylation modulates the secretion and  lipolytic function   of apoptosis inhibitor of macrophage (AIM).
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.
authors.affiliation: Laboratory of Molecular Biomedicine for Pathogenesis, Center for Disease Biology and Integrative Medicine, Faculty of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.
authors.forename: Mayumi
authors.initials: M
authors.lastname: Mori
authors.forename: Hiroki
authors.initials: H
authors.lastname: Kimura
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Iwamura
authors.forename: Satoko
authors.initials: S
authors.lastname: Arai
authors.forename: Toru
authors.initials: T
authors.lastname: Miyazaki
mesh_terms: D000818:Animals; D051017:Apoptosis Regulatory Proteins; D006031:Glycosylation; D057809:HEK293 Cells; D006801:Humans; D008066:Lipolysis; D051379:Mice; D016297:Mutagenesis, Site-Directed; D011134:Polysaccharides / Q000378:metabolism; D051116:Receptors, Scavenger; D051122:Scavenger Receptors, Class B / Q000235:genetics / Q000378:metabolism*
chemical_list: D051017:Apoptosis Regulatory Proteins; C492821:CD5L protein, human; D011134:Polysaccharides; D051116:Receptors, Scavenger; D051122:Scavenger Receptors, Class B