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- W3135779737 abstract "The loss of proteoglycans, macromolecular aggregates present in articular cartilage, is one of the earliest manifestations in the pathogenesis of osteoarthritis. Differences have been observed in the physical and chemical properties of these molecules from arthritic, when compared with normal tissues, which proved useful to understand the regulatory mechanisms better. Many physiological systems, including the multicomponent pyruvate and α-ketoglutarate dehydrogenase complexes, are modulated by phosphorylation and dephosphorylation. The data described the phosphorylation of the core molecule of proteoglycan in articular cartilage by 32 P-inorganic phosphate or α– 32 P–ATP in an in vitro incubation system. Specimens of human knee articular cartilage obtained at the time of surgery or autopsy were incubated. All cartilage specimens tested were found to contain an enzyme system capable of utilizing α- 32 ϕ-ATP or 32 P i to synthesize 32 P-proteoglycans, which were released into the incubation medium and incorporated into the tissue matrix. Phosphorylated proteoglycan subunits ( 32 P–PG) were isolated from the A1–D1 fraction subsequent to centrifugation under dissociative conditions. Treatment of these subunits with chondroitinase ABC and chondroitin 4- and 6-sulfatases, followed by recentrifugation on a dissociative gradient, resulted in the redistribution of the 32 P-labeled material to the A1–D4 fraction. It indicated that the protein core molecule must contain the sites of phosphorylation." @default.
- W3135779737 created "2021-03-15" @default.
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- W3135779737 date "1979-01-01" @default.
- W3135779737 modified "2023-09-26" @default.
- W3135779737 title "Phosphorylation of Proteoglycans in Human Articular Cartilage" @default.
- W3135779737 cites W1999652145 @default.
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- W3135779737 doi "https://doi.org/10.1016/b978-0-12-301302-6.50041-5" @default.
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