Title |
Identifying N-linked glycan moiety and motifs in the cysteine-rich domain critical for N-glycosylation and intracellular trafficking of SR-AI and MARCO
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Published in |
Journal of Biomedical Science, February 2016
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DOI | 10.1186/s12929-016-0244-5 |
Pubmed ID | |
Authors |
Huey-Jen Tsay, Yung-Cheng Huang, Yi-Jen Chen, Yun-Hao Lee, Shu-Meng Hsu, Keng-Chang Tsai, Cheng-Ning Yang, Fong-Lee Huang, Feng-Shiun Shie, Lin-Chien Lee, Young-Ji Shiao |
Abstract |
The accumulation of soluble oligomeric amyloid-β peptide (oAβ) proceeding the formation of senile plaques contributes to synaptic and memory deficits in Alzheimer's disease. Our previous studies have indentified scavenger receptor A (SR-A), especially SR-A type I (SR-AI), as prominent scavenger receptors on mediating oAβ clearance by microglia while glycan moiety and scavenger receptor cysteine-rich (SRCR) domain may play the critical role. Macrophage receptor with collagenous structure (MARCO), another member of class A superfamily with a highly conserved SRCR domain, may also play the similar role on oAβ internalization. However, the role of N-glycosylation and SRCR domain of SR-AI and MARCO on oAβ internalization remains unclear. We found that oAβ internalization was diminished in the cells expressing SR-AI harboring mutations of dual N-glycosylation sites (i.e. N120Q-N143Q and N143Q-N184Q) while they were normally surface targeted. Normal oAβ internalization was observed in 10 SR-AI-SRCR and 4 MARCO-SRCR surface targeted mutants. Alternatively, the SRCR mutants at β-sheet and α-helix and on disulfide bone formation obstructed receptor's N-glycosylation and surface targeting. Our study reveals that N-glycan moiety is more critical than SRCR domain for SR-A-mediated oAβ internalization. |
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Demographic breakdown
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