PMID: 23236605

 

    Legend: Gene, Sites

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

Abstract :

1. 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
2. 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
3. Interestingly, the lack of N-glycans increased AIM lipolytic activity through enhancing AIM incorporation into adipocytes
4. Although human AIM contains no N-glycan, attachment of N-glycans increased AIM secretion
5. Thus, the N-glycosylation plays important roles in the secretion and lipolytic function of AIM

Output (sent_index, trigger, protein, sugar, site):

• 1. N-glycosylation, , -, -, sites
• 2. N-glycans, , -, the first and second scavenger receptor cysteine-rich domains, domains
• 2. N-glycosylation, , -, -, sites
• 2. contains, , AIM, two N-glycans, -
• 4. contains, , AIM, no N-glycan, -

Output(Part-Of) (sent_index, protein, site):

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX
FAS	14104	1
fatty acid synthase	14104	1