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PubMed1989

Structural studies of two populations of keratan sulphate chains from mature bovine articular cartilage.

Two discrete peptido-keratan sulphate fragments were isolated via chondroitinase ABC and trypsin digestion of a proteoglycan aggregate fraction prepared from bovine femoral head cartilage (six year old animals). The larger fragments (K(av) = 0.07, CL-6B) contained peptides substituted with several keratan sulphate (KS) chains from the KS-rich region of the proteoglycan and the smaller fragments (K(av) = 0.5, CL-6B) contained peptides with, perhaps, only one KS chain and the stubs of post-chondroitinase-treated chondroitin sulphate chains. The two peptido-KS samples and the KS chains derived from these by alkaline borohydride reduction were characterised by 13C-NMR spectroscopy. The two populations of KS chains were also examined by chromatography (Sephadex G-75), and keratanase digestion followed by chromatography on Bio-Gel P-10. From the results it was concluded that the KS chains from the two major trypsin-derived peptido-KS fragments had similar sulphation levels, distributions of hydrodynamic sizes and susceptibilities to keratanase.

Animals↗
PubMed1997

Quantification of mRNA levels in joint capsule and articular cartilage of the murine knee joint by RT-PCR: kinetics of stromelysin and IL-1 mRNA levels during arthritis.

We developed a method to isolate well defined joint specimens from different compartments of normal and arthritic murine knee joints in which mRNA levels of stromelysin and IL-1 were semiquantified using RT-PCR. Joint capsule specimens were isolated on medial and lateral sides of the patella with a biopsy punch. Cartilage layers were isolated from patellae after a mild decalcification with EDTA. EDTA treatment had no effect on the amount and efficiency of amplification of mRNA when tested on isolated chondrocytes. After induction of experimental arthritis, stromelysin mRNA was elevated approximately 50 times in both joint capsule and cartilage. IL-1 was elevated 100 times in joint capsule but only 10 times in cartilage. Kinetic analysis of mRNA levels in cartilage during arthritis showed a prolonged elevation of stromelysin mRNA compared to IL-1. The variation in mRNA levels between joints of individual mice proved to be low, showing that sampling of the specimens and subsequent RT-PCR can be performed reliably. The current method offers a valuable approach to study gene expression in knee joints during murine experimental arthritis.

Animals↗
PubMed1990

Localization of endogenous osteocalcin in neonatal rat bone and its absence in articular cartilage: effect of warfarin treatment.

Immunocytochemistry after cryoultramicrotomy was used to localize endogenous osteocalcin in bone (calvaria, femoral diaphysis) and epiphyseal femoral cartilage from 8-day-old rats treated (or mot) for 7 days with warfarin. Ultrathin frozen sections were incubated with goat antiserum against rat osteocalcin at high dilutions (2 x 10(-4) to 2 x 10(-6). In calvaria and femur of untreated rats, endogenous osteocalcin was observed in osteoblasts (cytoplasm and nucleus) and in the collagenous matrix. Osteocalcin appeared progressively in osteoblasts and bone matrix in the mineralization front, then increased in the regions of extended calcification. Osteocalcin was also detected in osteocytes but was not as abundant as in osteoblasts. In bone samples of warfarin-treated rats, endogenous osteocalcin was only detected in bone matrix but not in osteoblasts. Furthermore, osteocalcin was only observed if antiserum was not very dilute (2 x 10(-2). In cartilage (hypertrophied and degenerative zones), osteocalcin was not observed in matrix and chondrocytes. However, it was found in the vicinity of matrix vesicles at the initial loci of calcification. Osteocalcin was never detected in the cartilage of warfarin-treated rats. Our results provide ultrastructural immunocytological evidence for the localization of endogenous osteocalcin in osteoblasts, the presence of osteocalcin in bone matrix and a direct gradient between the presence of osteocalcin and the calcification process. Osteocalcin is absent from cartilage, except possibly close to calcifying matrix vesicles. Warfarin inhibits the formation of osteocalcin.

Animals↗