A matrix protein of Mr 55,000 that accumulates in human articular cartilage with age.
Adult human articular cartilage contains a protein of Mr 55,000 which is deficient in newborn cartilage. In the adult the molecule represents one of the most abundant non-collagenous, non-proteoglycan molecules in 4 M guanidinium chloride extracts of the tissue. The molecular size of the protein on SDS-PAGE remains constant under reducing and non-reducing conditions, suggesting that it does not exist as a disulphide-bonded multimer, nor do intramolecular disulphide bonds greatly influence its conformation. The protein has the ability to interact with some immunoglobulin preparations making its detection possible by Western blotting with some non-specific antisera. Labeling with [3H]leucine in organ culture indicates that protein of this size is being made by the chondrocytes. However, during purification the newly synthesized molecules do not behave as the resident protein on ion-exchange chromatography, suggesting that the protein may accumulate with age rather than being a major synthetic product of the adult chondrocytes. Amino terminal protein sequence analysis indicates that the N-terminus of the protein is blocked. Sequences derived from peptides generated with cyanogen bromide do not show homology with previously characterized proteins. Molecules of a similar size and composition have been described in bovine cartilage.
Melching
L I
LI
Genetics Unit, Shriners Hospital, Montreal, Quebec, Canada.
Roughley
P J
PJ
D000328:Adult; D000368:Aged; D000375:Aging; D000596:Amino Acids / Q000032:analysis; D002358:Cartilage, Articular / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D005109:Extracellular Matrix / Q000737:chemistry*; D006801:Humans; D007231:Infant, Newborn; D008875:Middle Aged; D008970:Molecular Weight; D011506:Proteins / Q000302:isolation & purification
D000596:Amino Acids; D011506:Proteins