Organization of ground substance proteoglycans in normal and osteoarthritic knee cartilage
β Scribed by Kenneth D. Brandt; Marshall Palmoski
- Publisher
- John Wiley and Sons
- Year
- 1976
- Tongue
- English
- Weight
- 595 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0004-3591
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
A study of the organization of proteoglycans in articular cartilage indicates that nonaggregated proteoglycans existed in larger numbers in osteoarthritic than in normal cartilage and that proteoglycan aggregates in arthritic cartilage were smaller than normal. After dissociation from hyaluronic acid and tissue glycoproteins, no difference in hydrodynamic size of disaggregated proteoglycans was noted, but chondroitin sulfate chains of those from diseased cartilage were shorter than normal. The data suggest that there is a defect in proteoglycan aggregation in osteoarthritic cartilage which could be of pathogenetic significance.
π SIMILAR VOLUMES
Proteases have been postulated to account for the progressive disappearance of matrix proteoglycans in osteoarthritic (OA) cartilage. The digestion of endogenous proteoglycans by neutral proteases in human OA cartilage homogenates has been measured and compared with that of normal age-matched contro
We have recently described a 550,000-dalton nomollagenous cartilage matrix glycoprotein (CMGP), with subunits of 130,000, which is present in hyaline cartilage and fibrocartilage. Biosynthetic studies indicated that CMGP was synthesized by short-term organ cultures of normal canine articular cartila