Presence of link protein in cartilage from cmd/cmd (cartilage matrix deficiency) mice.
Immunohistochemical and biochemical evidence that the cartilage from cmd/cmd mice, who have an autosomal recessive lethal mutation causing cartilage matrix deficiency, synthesizes link protein nearly at a normal level is provided. Since cartilage-characteristic proteoglycan is not synthesized in this mutant mouse (K. Kimata, H-J. Barrach, K. S. Brown, and J. P. Pennypacker (1981) J. Biol. Chem. 256, 6961-6968), link proteins are apparently not in conventional proteoglycan aggregate. However, the link proteins are functional and able to interact with exogenous cartilage-characteristic proteoglycan monomer and hyaluronic acid to form aggregates.
D000818:Animals; D002356:Cartilage / Q000032:analysis*; D003240:Connective Tissue Diseases / Q000235:genetics / Q000503:physiopathology*; D004622:Embryo, Mammalian; D016326:Extracellular Matrix Proteins; D005260:Female; D005455:Fluorescent Antibody Technique; D051379:Mice; D008817:Mice, Mutant Strains; D011247:Pregnancy; D014176:Protein Biosynthesis; D011506:Proteins / Q000302:isolation & purification*; D011509:Proteoglycans / Q000302:isolation & purification*; D000099249:Proteoglycan Link Protein
D016326:Extracellular Matrix Proteins; D011506:Proteins; D011509:Proteoglycans; D000099249:Proteoglycan Link Protein