Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.4.24.3 (collagenase)
18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A metalloproteinase inhibitor present in human rheumatoid synovial fluid was purified by a combination of heparin-Sepharose chromatography, concanavalin A-Sepharose chromatography, ion-exchange chromatography and gel filtration. The Mr of the purified inhibitor was 28000 by SDS/polyacrylamide-gel electrophoresis and 30000 by gel filtration. The inhibitor blocked the activity of the metalloproteinases collagenase, gelatinase and proteoglycanase, but not thermolysin or bacterial collagenase. The serine proteinase trypsin was not inhibited. The inhibitory activity was lost after treatment with trypsin (0.5 micrograms/ml) at 37 degrees C for 30 min, 4-aminophenylmercuric acetate (1 mM) at 37 degrees C for 3 h, after incubation for 30 min at 90 degrees C and by reduction and alkylation. These properties suggest that the inhibitor closely resembles the tissue inhibitor of metalloproteinases ('TIMP') recently purified from connective-tissue culture medium.
...
PMID:Purification of a metalloproteinase inhibitor from human rheumatoid synovial fluid. 300 Mar 52

Relaxin (Rlx) classically causes uterine quiescence during pregnancy and cervical dilatation prior to parturition. Its actions involve major changes in the components of the extracellular matrix of these tissues. The activities of three enzymes, collagenase, proteoglycanase and beta-glucuronidase, major determinants of the integrity of the extracellular matrix have been measured in the rat uterus and cervix in different reproductive states. The results show that there are marked differences in the changes of these enzymes occurring in the uterus and cervix during the course of pregnancy and the puerperium. It was not possible to directly relate these changes to a single hormonal event over this period of major endocrine fluctuations. Two models have therefore been used in an attempt to delineate the effects of oestrogen and Rlx on the tissue enzyme levels or their secretion into culture medium. In the first model cyclic animals were treated with oestrogen alone or oestrogen followed by Rlx and tissue enzyme levels measured. The addition of Rlx treatment reversed an inhibiting effect of oestrogen alone on both uterine and cervical collagenase and proteoglycanase activities, at the same time as completely obliterating the stimulating effect of oestrogen on uterine and cervical beta-glucuronidase activity. A second model used in vivo oestrogen priming of cyclic rats followed by in vitro Rlx treatment and measurement of the enzymes secreted into the culture medium over 7 days. The results showed as in the first model that Rlx treatment could in particular overcome the inhibiting effect of oestrogen on uterine proteoglycanase secretion without affecting beta-glucuronidase levels. In contrast, the effect of Rlx on the cervix was to decrease collagenase and proteoglycanase secretion whilst not affecting the beta-glucuronidase levels.
...
PMID:The effect of oestrogen and relaxin on uterine and cervical enzymes: collagenase, proteoglycanase and beta-glycuronidase. 300 78

We report the primary structure and cDNA cloning of human fibroblast collagenase inhibitor, a glycoprotein that appears to play a central role in modulating the activity of a number of metalloendoproteases of connective tissue origin including collagenase, gelatinase, and proteoglycanase. Secreted human fibroblast collagenase inhibitor was purified and subjected to automated Edman degradation. The secreted protein consists of 184 amino acid residues; it contains two sites of N-linked oligosaccharide linkage and six disulfide bonds. Synthetic oligonucleotide probes based on selected amino acid sequences of the inhibitor were used to screen a lambda gt10 cDNA library from a human fibroblast line. Two overlapping cDNA clones were characterized to determine the complete coding and noncoding sequences of the specific mRNA. The amino acid sequence deduced from the nucleotide sequence agrees with that determined by protein sequencing. One clone appears to contain the complete 5' end and, in addition, the cDNA sequence predicts a 23-amino acid leader peptide. The other clone represents the 3' end of the mature message and includes a short poly(A)+ tract. This 3' sequence is remarkably similar to a reported cDNA encoding part of the protein derived from mouse fibroblast poly(A)+ RNA. However, this inhibitor has no substantial homology with previously sequenced protease inhibitors.
...
PMID:Primary structure and cDNA cloning of human fibroblast collagenase inhibitor. 301 Mar 9

An antiserum to rabbit bone stromelysin (proteoglycanase) was raised in sheep and characterized as specific, recognizing the enzyme from both different tissue sources and different species. This antiserum and a specific antiserum to rabbit bone collagenase were used in the study of metalloproteinase production by rabbit articular chondrocytes stimulated with either interleukin 1 or mononuclear cell-conditioned medium. It was shown by electroimmunoblotting that the apparently co-ordinate (mole:mole) induction of collagenase and stromelysin activity with time correlated in either case with an increase in enzyme protein. The stimulated production of both enzymes could be modified in parallel by a variety of compounds. Immunohistochemical studies confirmed that although most cells were producing both metalloproteinases simultaneously, some chondrocytes produced detectable levels of only one. The data are discussed in relation to the mechanisms of breakdown in connective tissues.
...
PMID:Characterization of a specific antiserum to rabbit stromelysin and demonstration of the synthesis of collagenase and stromelysin by stimulated rabbit articular chondrocytes. 302 9

Development of a single follicle during the menstrual cycle is under control of hormones stimulating follicular maturation, ovulation and luteogenesis. Several factors intervene locally to prevent other follicles from developing at the same time as dominant follicle. These other follicles remain quiescent or evaluate to atresia. Atresia results from the action of several endocrine, paracrine and autocrine mechanisms which synergistically inhibit aromatase activity. The subsequent lack of estrogens reduces granulosa cell multiplication. The oocyte will not become fertilizable before the preovulatory peak of LH, after the resumption of meiosis and after reaching metaphase of the second meiotic division. Several factors are involved in the inhibition of spontaneous resumption of meiosis: cyclic nucleotides, sex steroids, somatostatin and oocyte maturation inhibitor(s) (OMI). Ovulation is related to breakdown of connective tissue synthesized by granulosa cells under the influence of FSH. Connective tissue lysis is dependent on proteolytic enzymes which are released and activated by FSH, LH and relaxin. A paracrine control could be involved in ovulation: LH induces the production of prostaglandin and relaxin by theca cells which, in turn, stimulate collagenase and proteoglycanase secretion by granulosa cells.
...
PMID:Endocrine, paracrine and autocrine control of follicular development. 329 54

In this study, we measured the levels of neutral metallo- and serine proteases in human osteoarthritic synovium. These enzymes degrade both collagen and proteoglycan macromolecules. They were analyzed by tissue culture methodology and direct extraction. We have demonstrated that in human osteoarthritic synovium, there is a correlation between neutral enzyme activity and the severity of synovial inflammation. Tissue culture studies have shown that the human osteoarthritic synovial membrane produces metalloproteases, such as collagenase, proteoglycanase and gelatinase. These enzymes were further characterized by their molecular weight. Extracts of osteoarthritic synovial tissues showed the presence of serine proteases, with apparent Mr of 25,000.
...
PMID:Neutral proteases in human osteoarthritic synovium: quantification and characterization. 330 37

Development of a single follicle during the menstrual cycle is under control of hormones stimulating follicular maturation, ovulation and luteogenesis. Several factors intervene locally to avoid other follicles developing at the same time as the dominant follicle. These other follicles remain quiescent or go on to atresia. Atresia results from the action of several endocrine, paracrine and autocrine mechanisms which synergistically inhibit aromatase activity. The subsequent lack of oestrogens reduces granulosa cell multiplication. The oocyte will not become fertilizable before the preovulatory peak of LH, after the resumption of meiosis and after reaching the metaphase of the second meiotic division. Several factors are involved in this inhibition of spontaneous resumption of meiosis: cyclic nucleotides, sex steroids, somatostatin, oocyte maturation inhibitor(s) (OMI). Ovulation is related to breakdown of connective tissue synthesized by granulosa cells under the influence of FSH. Connective tissue lysis is dependent on proteolytic enzymes which are released and activated by FSH, LH and relaxin. A paracrine control could be involved in ovulation: LH induces the production of prostaglandin and relaxin by theca cells which, in turn, stimulate collagenase and proteoglycanase secretion by granulosa cells.
...
PMID:[Endocrine, paracrine and autocrine mechanisms involved in follicular development]. 333 Jul 30

Interleukin-1 (IL-1) is the name given to a family of related proteins showing a variety of activities. It was originally shown to be produced by monocytes and macrophages but is now known to be produced by numerous cell types, including synovial cells. From the point of view of arthritis, its most interesting activities are those on connective tissue cells in vitro. These include stimulation of production of prostaglandins, plasminogen activator and metalloproteinases such as collagenase and proteoglycanase. IL-1 is also mitogenic for synoviocytes and bone cells, and can alter rates of production of extracellular matrix constituents. The presence of IL-1 in synovial fluids from rheumatoid and osteoarthritic joints and its actions on connective tissues in vitro suggest that IL-1 may play an important role in the pathogenesis of arthritis. There are several potential cellular sources of IL-1 in the inflamed rheumatoid joint and interactions between these cells, T lymphocytes and plasma cells may continually induce IL-1 so contributing to the chronicity of the disease. The mechanism of action of IL-1 on connective tissue cells is at present uncertain though preliminary studies suggest that IL-1 may induce cellular responses by stimulating phosphoinositide turnover and possibly protein kinase C activity.
...
PMID:The effect of interleukin-1 on connective tissue metabolism and its relevance to arthritis. 352 46

Supernatants from the P388D1 murine macrophage cell line as well as commercially prepared human interleukin-1 (IL-1) stimulated primary rabbit articular chondrocytes to produce collagen- and proteoglycan-degrading proteases. The P388D1-derived factor had a molecular weight of 16,000-20,000 and a pI of 4.5-5.0, and was sensitive to phenylglyoxal treatment. Human IL-1 and the P388D1 supernatants enhanced glycosaminoglycan (GAG) release from bovine nasal cartilage explants. The proteoglycan- and collagen-degrading proteases required Ca2+ for activity. Latent proteoglycanase and collagenase had molecular weights of 44,000-56,500 and 34,000-44,000, respectively. The activated proteases had molecular weights of 30,000-40,000 and 22,000-36,000, respectively. Heparin-Sepharose affinity chromatography yielded two latent proteoglycanase-degrading protease activities and a collagen-degrading peak. The two proteoglycanase peaks also degraded fibronectin, laminin, gelatin, and azocoll but not type I collagen. The collagenase peak also degraded proteoglycan, gelatin, fibronectin, laminin, and azocoll. The activity of the proteoglycan- and collagen-degrading peaks was inhibited by phenanthroline and alpha 2-macroglobulin but not by phenylmethylsulfonylfluoride (PMSF), tosyllysylchloromethylketone (TLCK), pepstatin, or alpha 1-antitrypsin. The control of factors which augment protease production may offer a novel therapeutic approach to arthritis.
...
PMID:Interleukin-1 stimulates the secretion of proteoglycan- and collagen-degrading proteases by rabbit articular chondrocytes. 353 22

Relaxin (Rlx) is shown in vitro to increase the release of plasminogen activator (PA) activity from granulosa cells obtained from 28-day-old rats after priming 48 h before with PMSG. Priming with PMSG was essential for the subsequent marked increase in PA by the addition of Rlx to these cells in vitro. Under the same conditions Rlx also increased the release of both total collagenase and total proteoglycanase activities but not of beta-glucuronidase activity. The total collagenase and proteoglycanase activities of control cells are made up of essentially equal amounts of their respective active and latent enzymes. Rlx stimulation increases the amounts of the respective active enzymes while the latent collagenase and proteoglycanase activities are unchanged or decreased, respectively. The enzyme beta-glucuronidase was not stimulated by Rlx and appears not to be involved in follicular proteoglycan degradation. Granulosa cells harvested from preantral follicles responded most to FSH by PA production whereas cells from antral follicles responded more to LH, reflecting the known changes in concentration of FSH and LH receptors on these cells. The release of PA is maximal by all four hormones studied (FSH, LH, prostaglandin E1, and Rlx) on granulosa cells harvested from rats 48 h after PMSG treatment and this suggests that the follicles at this time are a mixture of both preantral and antral stages. The PA response to FSH is lost by 60 h after PMSG at the same time that the response to prostaglandin E1 is maintained at the same level, whereas that to Rlx and LH, although still significantly higher than controls, were decreased. By 70 h after PMSG, postovulatory, the responses to all hormones studied were lost. Thus, the involvement of PA in ovarian connective tissue alterations appears to be greatest in the period of follicular antrum formation rather than just before ovulation. Rlx is one of a number of hormones involved in the sequence of events culminating in follicle connective tissue remodeling as shown by its action on the release of three intrafollicular enzymes.
...
PMID:Relaxin increases the release of plasminogen activator, collagenase, and proteoglycanase from rat granulosa cells in vitro. 608 81


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---