Modification of N-glycosylation modulates the secretion and lipolytic function of apoptosis inhibitor of macrophage (AIM)

FEBS Lett. 2012 Oct 19;586(20):3569-74. doi: 10.1016/j.febslet.2012.08.017.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis Regulatory Proteins
  • Glycosylation
  • HEK293 Cells
  • Humans
  • Lipolysis*
  • Mice
  • Mutagenesis, Site-Directed
  • Polysaccharides / metabolism
  • Receptors, Scavenger
  • Scavenger Receptors, Class B / genetics
  • Scavenger Receptors, Class B / metabolism*


  • Apoptosis Regulatory Proteins
  • CD5L protein, human
  • Polysaccharides
  • Receptors, Scavenger
  • Scavenger Receptors, Class B