Expression and structure of cartilage proteins.
Cartilage has unique physical characteristics attributable to the presence of an unusually high content of proteoglycan embedded in the network of collagen fibrils. Advances in understanding the structure of these components and how their synthesis is regulated have been greatly assisted by the application of molecular biology. For example, an immortalized rat chondrocyte cell line was obtained by infection with a recombinant retrovirus encoding the myc gene product. Several positive and negative DNA regulatory elements of the collagen II gene have been identified that appear to be important in the regulation of this gene in chondrocytes. The complete primary structure of the cartilage proteoglycan (aggrecan) core protein deduced from cDNA sequence displays a complex multidomain structure including numerous repeats of Ser-Gly sequences and sequence homologies with link protein and animal lectins. Such studies advance our understanding of normal morphogenetic events and lay the groundwork for determining the basis of molecular and genetic defects.
Yamada
Y
Y
Laboratory of Developmental Biology and Anomalies, National Institute of Dental Research, NIH, Bethesda, MD 20892.
Horton
W
W
Miyashita
T
T
Savagner
P
P
Hassell
J
J
Doege
K
K
D000818:Animals; D002356:Cartilage / Q000378:metabolism*; D002478:Cells, Cultured; D002874:Chromosome Mapping; D003094:Collagen / Q000096:biosynthesis / Q000235:genetics; D005786:Gene Expression Regulation / Q000502:physiology*; D005809:Genes, Regulator / Q000502:physiology; D066298:In Vitro Techniques; D011401:Promoter Regions, Genetic / Q000502:physiology; D011509:Proteoglycans / Q000096:biosynthesis* / Q000648:ultrastructure; D051381:Rats; D014212:Tretinoin / Q000494:pharmacology
D011509:Proteoglycans; D014212:Tretinoin; D003094:Collagen