title: Endoplasmic reticulum stress in chondrodysplasias caused by mutations in collagen types II and X.
abstract: The endoplasmic reticulum is primarily recognized as the site of synthesis and folding of secreted, membrane-bound, and some organelle-targeted proteins. An imbalance between the load of unfolded proteins and the processing capacity in endoplasmic reticulum leads to the accumulation of unfolded or misfolded proteins and endoplasmic reticulum stress, which is a hallmark of a number of storage diseases, including neurodegenerative diseases, a number of metabolic diseases, and cancer. Moreover, its contribution as a novel mechanistic paradigm in genetic skeletal diseases associated with abnormalities of the growth plates and dwarfism is considered. In this review, I discuss the mechanistic significance of endoplasmic reticulum stress, abnormal folding, and intracellular retention of mutant collagen types II and X in certain variants of skeletal chondrodysplasia.
authors: Microbiology Department, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387, Krakow, Poland. katarzyna.gawron@uj.edu.pl.
authors: Katarzyna
authors: K
authors: Gawron
mesh_terms: D000818:Animals; D002356:Cartilage / Q000378:metabolism / Q000473:pathology; D024043:Collagen Type II / Q000235:genetics*; D024121:Collagen Type X / Q000235:genetics*; D059865:Endoplasmic Reticulum Stress; D006801:Humans; D010009:Osteochondrodysplasias / Q000378:metabolism / Q000473:pathology*; D015398:Signal Transduction; D056811:Unfolded Protein Response
chemical_list: D024043:Collagen Type II; D024121:Collagen Type X
keywords: Chondrodysplasia; Collagen; Endoplasmic reticulum stress; Mechanism; Mutation; Unfolded protein response