Proteolytic cleavage of the disease-related lysosomal membrane glycoprotein CLN7

Article ID	Journal	Published Year	Pages	File Type
8261430	Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease	2012	12 Pages	PDF

Abstract

âº The lysosomal membrane glycoprotein CLN7 is proteolytically cleaved in lysosomes. âº Proteolytic cleavage can be mediated by cathepsin L and occurs in luminal loop L9. âº CLN7 cleavage occurs gradually and cleavage products are relatively stable. âº Disease-associated mutations in CLN7 result in increased proteolytic cleavage.

Keywords

MEF lysosomal acid phosphatase PNGase F Peptide:N-Glycosidase F CTSL CtsB NCL BFA MFS CHX LAP IC50 DMEM GFP TLR9 HEK293 neuronal ceroid lipofuscinosis Lysosomal storage disorder Endo H endoglycosidase H brefeldin A Major facilitator superfamily Neurodegeneration Proteolytic cleavage Dulbecco's minimal essential medium transmembrane domain cycloheximide endoplasmic reticulum mouse embryonic fibroblast half maximal inhibitory concentration green fluorescent protein Cathepsin B Cathepsin L human embryonic kidney 293 Toll-like receptor 9