| First Author | Mori M | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 20 | Pages | 3569-74 |
| PubMed ID | 23236605 | Mgi Jnum | J:197958 |
| Mgi Id | MGI:5494939 | Doi | 10.1016/j.febslet.2012.08.017 |
| Citation | Mori M, et al. (2012) Modification of N-glycosylation modulates the secretion and lipolytic function of apoptosis inhibitor of macrophage (AIM). FEBS Lett 586(20):3569-74 |
| abstractText | 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. |
