Collagen Q and anti-MuSK autoantibody competitively suppress agrin/LRP4/MuSK signaling View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-11

AUTHORS

Kenji Otsuka, Mikako Ito, Bisei Ohkawara, Akio Masuda, Yu Kawakami, Ko Sahashi, Hiroshi Nishida, Naoki Mabuchi, Akemi Takano, Andrew G. Engel, Kinji Ohno

ABSTRACT

MuSK antibody-positive myasthenia gravis (MuSK-MG) accounts for 5 to 15% of autoimmune MG. MuSK and LRP4 are coreceptors for agrin in the signaling pathway that causes clustering of acetylcholine receptor (AChR). MuSK also anchors the acetylcholinesterase (AChE)/collagen Q (ColQ) complex to the synaptic basal lamina. We previously reported that anti-MuSK antibodies (MuSK-IgG) block binding of ColQ to MuSK and cause partial endplate AChE deficiency in mice. We here analyzed the physiological significance of binding of ColQ to MuSK and block of this binding by MuSK-IgG. In vitro plate-binding assay showed that MuSK-IgG blocked MuSK-LRP4 interaction in the presence of agrin. Passive transfer of MuSK-IgG to Colq-knockout mice attenuated AChR clustering, indicating that lack of ColQ is not the key event causing defective clustering of AChR in MuSK-MG. In three MuSK-MG patients, the MuSK antibodies recognized the first and fourth immunoglobulin-like domains (Ig1 and Ig4) of MuSK. In two other MuSK-MG patients, they recognized only the Ig4 domain. LRP4 and ColQ also bound to the Ig1 and Ig4 domains of MuSK. Unexpectedly, the AChE/ColQ complex blocked MuSK-LRP4 interaction and suppressed agrin/LRP4/MuSK signaling. Quantitative analysis showed that MuSK-IgG suppressed agrin/LRP4/MuSK signaling to a greater extent than ColQ. More... »

PAGES

13928

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep13928

DOI

http://dx.doi.org/10.1038/srep13928

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028492644

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26355076


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