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Article

Multiple functions of the first EGF domain in matrilin-3: Secretion and endoplasmic reticulum stress.

International journal of molecular medicine - 1 Dec 2015

Wang Yi-Chun, Liu Jing-Shi, Chen Jun-Yi, Wu Sheng-Qi, Wang Gui-Rong, Nie Jing, Zhang Shu-Kun, Guo Qu-Lian, Luo Jun-Ming

Abstract excerpt

Mutations in matrilin-3 are associated with common skeletal diseases, such as hand osteoarthritis (HOA), as well as rare chondrodysplasias, such as multiple epiphyseal dysplasia (MED) and spondyloepimetaphyseal dysplasia (SEMD). In the present study, we constructed the mutations R116W [at the von Willebrand factor, type A (vWFA) domain], T298M [at the first epidermal growth factor (EGF) domain] and C299S (at the...

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Identifiers

PMID: 26499313
DOI: 10.3892/ijmm.2015.2377

Genes

EGF

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Click a neighbor to travelStep 1 · 12 closest

Multiple functions of the first EGF domain in matrilin-3: Secretion and endoplasmic reticulum stress.PMID 26499313Read ↗

Matrilin-3 mutations that cause chondrodysplasias interfere with protein trafficking while a mutation associated with hand osteoarthritis does not.Semantic proximity Read ↗

Armet/Manf and Creld2 are components of a specialized ER stress response provoked by inappropriate formation of disulphide bonds: implications for genetic skeletal diseasesSemantic proximity Read ↗

Multiple epiphyseal dysplasia mutations in MATN3 cause misfolding of the A-domain and prevent secretion of mutant matrilin-3.Semantic proximity Read ↗

Mechanisms and models of endoplasmic reticulum stress in chondrodysplasia.Semantic proximity Read ↗

Decreased chondrocyte proliferation and dysregulated apoptosis in the cartilage growth plate are key features of a murine model of epiphyseal dysplasia caused by a matn3 mutation.Semantic proximity Read ↗

A matrilin-3 mutation associated with osteoarthritis does not affect collagen affinity but promotes the formation of wider cartilage collagen fibrils.Semantic proximity Read ↗

Loss of matrilin 1 does not exacerbate the skeletal phenotype in a mouse model of multiple epiphyseal dysplasia caused by a Matn3 V194D mutation.Semantic proximity Read ↗

Human pluripotent stem cell model of multiple epiphyseal dysplasia with <i>MATN3</i> mutation identifies altered Matrix organisation and upregulation of the cholesterol biosynthesis pathwaySemantic proximity Read ↗

Human pluripotent stem cell model of multiple epiphyseal dysplasia with MATN3 mutation identifies altered matrix organisation and upregulation of the cholesterol biosynthesis pathway.Semantic proximity Read ↗

Human iPSC-derived hypertrophic chondrocytes reveal a mutation-specific unfolded protein response in chondrodysplasiasSemantic proximity Read ↗

An unfolded protein response is the initial cellular response to the expression of mutant matrilin-3 in a mouse model of multiple epiphyseal dysplasia.Semantic proximity Read ↗

Novel mutations in exon 2 of MATN3 affect residues within the alpha-helices of the A-domain and can result in the intracellular retention of mutant matrilin-3.Semantic proximity Read ↗

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