Synthesis of aggrecan core proteins by human cartilage and chondrocytes in vitro. 1995

C J Malemud, and V M Goldberg
Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106-4946, USA.

Proteoglycans synthesized by human cartilage were studied in explants and in chondrocyte cultures. The D1 fraction proteoglycans radiolabelled with 35SO4 were analyzed by 3-16% sodium dodecyl sulfate polyacrylamide gel electrophoresis or on 3-5% acrylamide gels. After 24 h in culture, osteoarthritic and age matched nonarthritic cartilage synthesized one aggrecan core protein (LI) whose apparent size after chondroitinase ABC/keratanase digestion was approximately 520 kDa. Three proteoglycan core proteins were found in the D1 fraction of the medium compartment of nonarthritic chondrocytes, whose apparent sizes were approximately 520 kDa (LI), approximately 390 kDa (LII), and approximately 480 kDa (LIII). The LII and LIII core proteins were routinely absent from osteoarthritic chondrocytes. Chondrocytes from a 28-year-old patient with osteoarthritis secondary to congenital hip dysplasia synthesized principally the LI proteoglycan core protein.

UI MeSH Term Description Entries
D008875 Middle Aged An adult aged 45 - 64 years. Middle Age
D010003 Osteoarthritis A progressive, degenerative joint disease, the most common form of arthritis, especially in older persons. The disease is thought to result not from the aging process but from biochemical changes and biomechanical stresses affecting articular cartilage. In the foreign literature it is often called osteoarthrosis deformans. Arthritis, Degenerative,Osteoarthrosis,Osteoarthrosis Deformans,Arthroses,Arthrosis,Arthritides, Degenerative,Degenerative Arthritides,Degenerative Arthritis,Osteoarthritides,Osteoarthroses
D011508 Chondroitin Sulfate Proteoglycans Proteoglycans consisting of proteins linked to one or more CHONDROITIN SULFATE-containing oligosaccharide chains. Proteochondroitin Sulfates,Chondroitin Sulfate Proteoglycan,Proteochondroitin Sulfate,Proteoglycan, Chondroitin Sulfate,Proteoglycans, Chondroitin Sulfate,Sulfate Proteoglycan, Chondroitin,Sulfate Proteoglycans, Chondroitin
D011509 Proteoglycans Glycoproteins which have a very high polysaccharide content. Proteoglycan,Proteoglycan Type H
D002358 Cartilage, Articular A protective layer of firm, flexible cartilage over the articulating ends of bones. It provides a smooth surface for joint movement, protecting the ends of long bones from wear at points of contact. Articular Cartilage,Articular Cartilages,Cartilages, Articular
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000328 Adult A person having attained full growth or maturity. Adults are of 19 through 44 years of age. For a person between 19 and 24 years of age, YOUNG ADULT is available. Adults
D000368 Aged A person 65 years of age or older. For a person older than 79 years, AGED, 80 AND OVER is available. Elderly
D016326 Extracellular Matrix Proteins Macromolecular organic compounds that contain carbon, hydrogen, oxygen, nitrogen, and usually, sulfur. These macromolecules (proteins) form an intricate meshwork in which cells are embedded to construct tissues. Variations in the relative types of macromolecules and their organization determine the type of extracellular matrix, each adapted to the functional requirements of the tissue. The two main classes of macromolecules that form the extracellular matrix are: glycosaminoglycans, usually linked to proteins (proteoglycans), and fibrous proteins (e.g., COLLAGEN; ELASTIN; FIBRONECTINS; and LAMININ). Extracellular Matrix Protein,Matrix Protein, Extracellular,Matrix Proteins, Extracellular,Protein, Extracellular Matrix,Proteins, Extracellular Matrix

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