Proteoglycans degradation

Sapolsky, A. I., Howell, D. S., Woessner, J. F. Jr. Proteoglycan degradation by neutral protease and acid cathepsin in human articular cartilage inhibition by f>-penicillamine. 

Badger, A. M., Cook, M. N., Swift, B. A., Newman-Tarr, T. M., Gowen, M., Lark, M., (1999). Inhibition of interleukin-1-induced proteoglycan degradation and nitric oxide production in bovine articular cartilage /chondrocyte cultures by the natural product, hymenialdisine. J. Pharmacol. Exp. Ther. 290, 587-593. 

The other lysosomal enzymes listed here, we have demonstrated in liver and kidney lysosomes (6). In conclusion The lactate production and therefore the pH depression in the inflamed synovial system of the gouty joint and also the increased activity of lysosomal proteoglycan degrading enzymes enhance the process of deposition of monosodium urate in joint cartilage. 

Brooks, B. P., Qiao, M., Howell, D. S., and Boyan, B. D., 1994, Matrix vesicles produced by osteoblast-like cells in culture become significantly enriched in proteoglycan-degrading metallopro-teinases after addition of beta-glycerophosphate and ascorbic acid, Calcif. Tissue Int. 54 399-408. 

Other recently reported activities of schisandra fruit include reduced proteoglycan degradation (antihyaluronidase activity) and antiplatelet activation (PAF antagonism). ... 

Chymopapain [9001 -90-6] derived from the latex of the papaya tree, produces improvement in lower back pain and sciatica in the majority (75%) of recipients (185—189) when injected into the lumbar intervertebral disks of patients suffering from herniated disk (the nucleus pulposus). This treatment degrades the proteoglycans of the diseased nucleus pulposus, resulting in shrinkage of the disk and reduction of pressure on the nerve roots (190). 

ADCOCKS c, COLLIN P and BUTTLE D J (2002) Catechins from green tea Camellia sinensis) inhibit bovine and human cartilage proteoglycan and type 11 collagen degradation in vitro , JNutr, 132 (3), 341-6. 

Greenwald, RA., Moy, W.W. and Lazarus, D. (1976). Degradation of cartilage proteoglycans and collagen by superoxide anions. Arthritis Rheum. 19, 799-806. 

Connective tissue is composed of apparently very different cells metabolically it is dynamic undergoing continual turnover and so to maintain health means that a balance must be achieved between biosynthesis and degradation. Cells in connective tissue are usually found embedded within a matrix composed of proteins with variable amounts of proteoglycan and genetically determined enzymatic defects in the production of the matrix may result in often serious pathologies. Metabolism in... 

The major non-collagenous components of the dentin matrix are highly-phosphorylated proteins, phosphoryns, with many phosphoserine and aspartate residues (Butler et al., 1992). Dentin contains fewer proteoglycans than predentin. The proteoglycans from predentin are degraded upon mineralization, while small proteoglycans and phosphoryns are excreted by odontoblasts and incorporated into dentin (Goldberg et al., 1987 Linde, 1989). 

The organic matrix of the highly-mineralized tubule walls (peritubular) differs from the bulk intertubular matrix. It consists of proteoglycans, which are not degraded upon mineralization (Takagi et al., 1990). 

In both types of lesion, the peritubular matrix appeared to be more resistant to proteolytic activity than the intertubular matrix, which may be due to a compositional difference between the matrices. In this respect, it is interesting to note that Takagi et al. (1990) found the calcification of dentin to be accompanied by the degradation of proteoglycans throughout the intertubular matrix, but not in the peritubular matrix. However, there is no evidence that there is less degradation of the peritubular than the intertubular matrix, when demineralized dentin specimens are exposed to the oral environment (Van Strijp et al., 1992). This discrepancy can be explained by the assumption that a wide variety of enzymes participates in the degradation of the dentin matrix in vivo. 

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