Studies on the interaction of newly secreted proteoglycan subunits with hyaluronate in human articular cartilage.
Newly secreted proteoglycans from adult human cartilage do not interact well with hyaluronate, but attain this ability with time in the extracellular matrix. The conversion process occurs in all types of cartilagenous matrix, as newborn cartilage cultures, chondrosarcoma cultures and adult chondrocyte cultures each secreted proteoglycan subunits which exhibited the delayed aggregation phenomenon. However, the rate of conversion is probably dependent upon the structure of the surrounding matrix and the cell type. In vitro, link protein appears to enhance an initial change in the hyaluronate-binding region of the newly secreted proteoglycan subunits to allows stronger interaction with hyaluronate. In a second step, which is pH- and temperature-dependent, the change becomes irreversible. Thus, in addition to its role in stabilizing the interaction of mature proteoglycan subunits with hyaluronate, link protein may also aid in promoting the conversion of the newly synthesized proteoglycan subunit to a form that is capable of strong interaction with hyaluronate.
Melching
L I
LI
Joint Diseases Laboratory, Shriners Hospital for Crippled Children, Montreal, Quebec, Canada.
Roughley
P J
PJ
D000328:Adult; D002358:Cartilage, Articular / Q000187:drug effects / Q000378:metabolism*; D002813:Chondrosarcoma / Q000378:metabolism; D046508:Culture Techniques; D005109:Extracellular Matrix / Q000378:metabolism*; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007231:Infant, Newborn; D007700:Kinetics; D011509:Proteoglycans / Q000378:metabolism*
D011509:Proteoglycans; D006820:Hyaluronic Acid