Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The potential relationship of an intact membrane organization to the synthesis of chondroitin was examined before and after modification of a chick-embryo cartilage microsomal system with the non-ionic detergent Triton X-100. Incubations with labelled UDP-GlcA and UDP-GalNAc indicated that Triton X-100 had little effect on the amount of chondroitin synthesized to form one species of large proteochondroitin (Type I). However, Triton X-100 had a marked stimulatory effect on the formation of another smaller species of proteochondroitin (Type II). Presence of this detergent during chondroitin polymerization also resulted in chains that were slightly smaller. Neither of the two proteochondroitin species were collagenase-sensitive, nor did they contain dermatan-like regions. Thus in these respects they were unlike the small proteochondroitins (PG-Lb or PG-Lt) that have been found in chick-embryo cartilage. They also differed greatly in size from these small proteoglycans as well as from the large aggregatable proteochondroitin (PG-H) from the same source. Synthesis of the larger (Type I) proteochondroitin species was not affected by prior treatment of the microsomes with chondroitin ABC lyase at concentrations sufficient for elimination of synthesis of most of the smaller (Type II) proteochondroitin species. Use of chondroitin ABC lyase subsequent to synthesis of the chondroitin also resulted in preferential degradation of the smaller species. Thus there were differences in formation and limitation in access of the chondroitin ABC lyase to the two species, consistent with other differences described previously. These results indicate that there are separate loci within the microsomal membranes for synthesis of the two species.
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PMID:Formation of two species of nascent proteochondroitin in separate loci of a microsomal preparation from chick-embryo epiphyseal cartilage. 165 3

Human skin fibroblasts express, in addition to versican, a second large chondroitin sulfate/dermatan sulfate proteoglycan, which has been investigated with the aid of a specific antiserum in cultures of fetal fibroblasts. Its core protein, obtained after chondroitin ABC lyase treatment, exhibits an apparent molecular mass of about 740 kDa in the absence of a reducing agent whereas reduction produces two core proteins of 460 and 300 kDa, respectively. Both subunits carry one or very few dermatan sulfate chains of about 20 kDa which are of similar chemical composition irrespective of the type of subunits to which they are attached. Tryptic peptide maps of [35S]methionine-labeled core proteins indicated that both subunits are related neither to each other nor to versican, suggesting that the proteoglycan exists predominantly as a heterodimeric molecule. It is insensitive to collagenase and does not interact with hyaluronan. Pulse-chase experiments suggested that the core proteins are different gene products. Dimerization begins soon after core protein synthesis but requires more than 2 h for completion. Glycosaminoglycan synthesis occurs immediately prior to secretion. A small proportion of both subunits may be secreted in form of a monomeric proteoglycan. The heterodimeric proteoglycan is a major proteoglycan species of fetal fibroblasts. The secreted product represents 10-20% of [35S]methionine and about 5-10% of [35S]sulfate incorporated into secreted proteoglycans.
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PMID:A novel large dermatan sulfate proteoglycan from human fibroblasts. 207

PDGF is a powerful mitogen initially identified within platelets, but also shown to be produced by a wide variety of cell types. PDGF is encoded on two separate genes. These give rise to three polypeptides, PDGF B and two forms of PDGF A (SA and LA), resulting from alternative splicing of the PDGF A gene primary transcript. We report that in CHO cells transfected with PDGF gene constructs and producing moderate levels of PDGF homodimers, much of the PDGF LA and B produced, but little if any SA, is found in the matrix laid down beneath the cells. Immunoreactive PDGF in cells, and in matrix below expressing cells, was visualized by laser confocal microscopy. Western blotting of protein in matrix extracts, cell extracts, and secreted into the growth medium was used to demonstrate that the range of PDGF A polypeptides seen in the matrix was overlapping with those reported previously to be cell associated in cell types such as NIH3T3 and COS 7. This suggests that attachment to matrix or cell surface may be alternative fates for these polypeptides, with fate dependent on the characteristics of the producing cells. Immunoreactive PDGF A and B could be partially released by incubation of matrix material with heparin but not with other glycosaminoglycans. Digestion of matrix with chondroitin ABC lyase but not heparitinase or collagenase displaced some PDGF from its attachment sites. The results indicate attachment of PDGF to matrix proteoglycans, at least partly through the glycosaminoglycan moieties, and perhaps to additional components. The significance of matrix deposition for PDGF action is discussed.
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PMID:Accumulation of PDGF B and cell-binding forms of PDGF A in the extracellular matrix. 850 Nov 20

The gene expression of matrix metalloproteinase-1 and -3 was examined in basal cell carcinomas by in situ hybridization using digoxigenin-labelled riboprobes. Nodulo-ulcerative basal cell carcinomas demonstrated the gene expression for both metalloproteinases but superficial basal cell carcinomas did not present any transcripts for them. Transcripts for matrix metalloproteinase-1 (interstitial collagenase) were demonstrated densely in stromal cells among tumour masses, and those for matrix metalloproteinase-3 (stromelysin-1) were detected only in more advanced cases. Neither were expressed in tumour cells. The two metalloproteinases were produced by stromal cells according to the tumour invasion process, in which various growth factors, cytokines and inflammatory factors, which could regulate gene expressions of matrix metalloproteinases, were involved. It was also found that hybridization signals were enhanced by treatment with chondroitin ABC lyase, which digested abundant glycosaminoglycans in basal cell carcinoma. The procedure for the digestion is simple, and appears to be of value for in situ hybridization studies on tissues containing large amounts of glycosaminoglycans.
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PMID:Gene expression of matrix metalloproteinase-1 (interstitial collagenase) and matrix metalloproteinase-3 (stromelysin-1) in basal cell carcinoma by in situ hybridization using chondroitin ABC lyase. 918 54