𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Contents and distributions of the proteoglycans decorin and biglycan in normal and osteoarthritic human articular cartilage

✍ Scribed by A. Robin Poole; Lawrence C. Rosenberg; Agnes Reiner; Mirela Ionescu; Earl Bogoch; Peter J. Roughley


Publisher
Elsevier Science
Year
1996
Tongue
English
Weight
808 KB
Volume
14
Category
Article
ISSN
0736-0266

No coin nor oath required. For personal study only.

✦ Synopsis


Abstract

The study was designed to determine the contents and distributions of the proteoglycans decorin and biglycan in adult human femoral condylar cartilage and whether these may change in osteoarthritis. New radioimmunoassays were established using peptides representing the amino‐terminal 21 amino acid sequence of each proteoglycan (to which a tyrosine was added for radioiodination) and antibodies in a rabbit antiserum raised to both these molecules. Cartilage was extracted with 4 M guanidine HCl to determine total content, and extracts were analyzed by chromatography to determine molecular sizes. Frozen sections were cut parallel to the articular surface and were extracted to determine distribution within the tissue. Gel chromatography on Sepharose CL‐2B under dissociative conditions revealed molecules with a partition coefficient of 0.7–0.75 in both normal and osteoarthritic cartilage. In normal adult cartilage, the mean contents of the core proteins of biglycan and decorin were calculated to be approximately 0.34 and 0.48 mg per gram wet weight, respectively. These represented molar contents similar to that of aggrecan. In osteoarthritic cartilage, there were no overall significant changes in the content and distribution of these molecules. There was, however, considerable individual variation in both distribution and content. Analyses indicated that there was a trend in osteoarthritic cartilage toward a loss of biglycan and decorin from the more superficial layers of intact cartilage, where both these molecules are normally more concentrated. This was accompanied by maintenance of proteoglycan content deeper in the cartilage, regardless of the degree of degeneration.


πŸ“œ SIMILAR VOLUMES


Neutral proteases capable of proteoglyca
✍ Dr Johanne Martel-Pelletier; Jean-Pierre Pelletier; Jean-Marie Cloutier; David S πŸ“‚ Article πŸ“… 1984 πŸ› John Wiley and Sons 🌐 English βš– 767 KB

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

Organization of ground substance proteog
✍ Kenneth D. Brandt; Marshall Palmoski πŸ“‚ Article πŸ“… 1976 πŸ› John Wiley and Sons 🌐 English βš– 595 KB

## 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 h

Metabolism of a cartilage matrix glycopr
✍ Rose S. Fife; Marshall J. Palmoski; Kenneth D. Brandt πŸ“‚ Article πŸ“… 1986 πŸ› John Wiley and Sons 🌐 English βš– 668 KB

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