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

Two murine colon adenocarcinoma cell lines were established from primary cultures. The MCA-38 cell line was begun by treatment of the primary culture with trypsin to remove the fibroblastoid elements. The MCA-36 epithelial cells were sensitive to trypsin; therefore, the growth medium of MCA-36 primary cultures was augmented with collagenase to release the tumor-cell elements from the fibroblast network. These tumor elements were dissociated with trypsin and placed in tissue culture. Each cell line was cultured for at least 10 passages in vitro and gave rise to tumors when reimplanted in vivo.
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PMID:Murine colon adenocarcinomas: methods for selective culture in vitro. 125 4

Despite adequate locoregional control, colorectal metastasis to the liver remains a significant cause of death. Resection of hepatic metastasis improves five-year survival 18% to 34%. A study of the impact of 40% partial hepatectomy on cytokine production in the liver was undertaken. Nonparenchymal liver cells (NPCs) were prepared by collagenase perfusion and metrizamide gradient from partially hepatectomized and laparotomized control C57BL/6Ros mice. Nonparenchymal cell from partially hepatectomized mice compared with laparotomized mice showed a twofold to threefold increase in interferon (IFN) activity. Both interferon alpha/beta and supernatants from cultured NPCs of partially hepatectomized mice suppressed the proliferation of liver-derived MCA-38 colon adenocarcinoma cells in vitro. This tumor has been shown to metastasize to the liver of C57BL/6Ros mice. The production of various cytokines by NPCs induced by partial hepatectomy may provide a possible antimetastatic mechanism.
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PMID:Partial hepatectomy augments the liver's antitumor response. 246 82

Two children with Alport's syndrome are described, who developed anti-glomerular basement membrane (GMB) antibody-mediated nephritis after renal transplantation. The reactivity of antibodies in their serum with collagenase-solubilized normal GBM was examined by SDS-PAGE with one- and two-dimensional immunoblotting. The specificity was compared with that of antibodies present in serum from a patient with Goodpasture's syndrome, and a mouse monoclonal antibody (MCA-P1), directed against the Goodpasture antigen. All reacted in a similar way with collagenase-solubilized GBM. Since abnormalities in the composition of the GBM are present in Alport's syndrome, it is proposed that differing antigen composition of GBM in the host compared with the donor kidney, together with transplant rejection, may have provoked the development of post-transplant anti-GBM antibodies.
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PMID:The development of anti-glomerular basement membrane nephritis in two children with Alport's syndrome after renal transplantation: characterization of the antibody target. 264 9

Hereditary nephritis (HN) is associated with antigenically abnormal glomerular basement membrane (GBM) manifest by reduced or absent binding of MCA-P1, a mouse monoclonal antibody which recognizes Goodpasture antigen. In the present studies, immunoblotting has been used to analyze antigenic and biochemical composition of renal tissue from patients with HN in whom binding of MCA-P1 could not be demonstrated by indirect immunofluorescence (IIF). Pooled normal collagenase-solubilized GBM (CS-GBM) and CS-GBM from three patients with either end-stage renal failure (ESK1-3) or HN (HNK1-3), were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis gel and, after transfer by Western blotting to nitrocellulose, reacted with sera from six patients with anti-GBM disease (GPS1-6) or anti-GBM antibody containing sera from three transplanted HN patients (HNS1-3), different from those patients with HN contributing HNK1-3. We found that GPS1-6 and HNS1-2 recognized the same six major bands in CS-GBM and ESK1-3 (between 54 and 24 kilodalton (kd) but only three bands (48, 42 and 24 kd) in HNK1-3. HNS3 only bound strongly to bands of 54 and 26 kd in CS-GBM or ESK1-3 and not all to HNK1-3. Immunoblotting studies of HNK1-3 have shown a partial rather than absolute loss of Goodpasture antigenicity (54, 28 and 26 kd bands). Studies with HNS1-3 suggest heterogeneity of antibody responses to allografted kidneys between patients with HN; HNS-3 showed restricted antibody specificity with recognition in CS-GBM of some bands antigenically absent from HN kidney. The abnormality in HN kidneys appears closely related to, but distinct from, the Goodpasture determinant and the inherited defect in HN may involve an essential modifying enzyme.
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PMID:Hereditary nephritis: immunoblotting studies of the glomerular basement membrane. 265 72

We found the presence of collagenase-like (CL) peptidase in synovial fluid by a highly sensitive fluorescence assay using (succinyl-Gly-Pro-Leu-Gly-Pro)-4-methyl-coumaryl-7-amide (Suc-GPLGP-MCA) as a substrate. Suc-GPLGP-MCA is hydrolyzed at the Leu-Gly bond by CL-peptidase. The CL-peptidase activity in synovial fluid was significantly higher in patients with rheumatoid arthritis (RA) than in patients with osteoarthritis (OA) and in arthropathy-free controls. No significant difference in CL-peptidase activity in synovial fluid was found between patients with OA and arthropathy-free controls.
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PMID:Collagenase-like (CL) peptidase activity in synovial fluid from patients with rheumatoid arthritis. 283 60

A monoclonal antibody (MCA IV-1) has been developed to a determinant of the high molecular weight fractions of human placental collagen, present also in bovine lens capsule and glomerular basement membrane type IV collagens. This unique determinant is pepsin and collagenase resistant and is apparently distinct from the alpha 1(IV) and alpha 2(IV) helical peptides. As part of the high molecular weight molecules, the determinant is located in a region additively deformable by reduction and sodium dodecyl sulfate denaturation. However, when a 20-kilodalton, largely collageneous, fragment containing this determinant is separated from the larger fraction by 37 degrees C collagenase treatment, the determinant is insensitive to reduction or sodium dodecyl sulfate denaturation. Immunohistologic analysis and comparison with a polyclonal antibody to type IV collagen shows a marked selectivity of localization in the glomerular basement membrane. MCA IV-1 reacts in the inner aspect of the glomerular basement membrane but primarily in the mesangium, where it selectively expands in diabetic nephropathy. Tissue selectivity is also evident in lens and corneal basement membrane.
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PMID:Monoclonal antibody to type IV collagen with selective basement membrane localization. 636 14

Two cell isolation procedures, i.e. a scraping/collagenase-treatment and a new vibration procedure in EDTA containing medium, were used to isolate intestinal epithelial cells. In both cell populations the metabolism of 7-ethoxycoumarin and 7-hydroxycoumarin was studied. Moreover, the time course and extent of induction of both steps in the biotransformation were investigated after oral 3-methylcholanthrene pretreatment of the rats. Twenty four hours after 3-methylcholanthrene pretreatment (20 mg kg-1) monooxygenase activity was induced about 6-fold and 2.5-fold when studied with cells of the vibratory and enzymic procedures, respectively. Control 7-ethoxycoumarin deethylase activity and 7-hydroxycoumarin glucuronidation were about the same when comparing both methods for cell-isolation. The formation of glucuronides in cells (both methods) is significantly lowered by 3-MC pretreatment, while sulphation remains unaffected. Results indicate that using enzymic treatment of mucosal scrapings, cell-populations are obtained containing relatively more differentiated (tip) cells. A number of advantages of the new (vibration) method are: better recovery, viability and reproducibility.
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PMID:Comparison of two cell isolation procedures to study in vitro intestinal wall biotransformation in control and 3-methyl-cholanthrene pretreated rats. 667 22

The proteolytic potential of cellular fibronectin fragments issued from a basement membrane hydrolysate was investigated. Three different gelatinase activities (47, 43 and 37 kDa), located by gelatin zymography, were isolated using successively heparin-agarose, gelatin-agarose and immunopurification with polyclonal antibodies directed against bovine plasma fibronectin. These fragments were also characterized using a monoclonal antibody directed against the extra-domain EDA of cellular fibronectin as a probe. A collagenase activity, reliably indicated by the gelatin zymography pattern, was also found using MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2, the intramolecularly quenched fluorogenic substrate of collagenases. From these results, cellular fibronectin was found to be able to exhibit a proteolytic function after limited proteolysis. This MMP-like function could be associated with tissue remodeling in both normal and pathological states, such as metastasis, angiogenesis and tissue repair.
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PMID:Immunopurification and characterization of a collagenase/gelatinase domain issued from basement membrane fibronectin. 870 29

Protease activities with specificity toward synthetic substrates, Suc-Gly-Pro-Leu-Gly-Pro-MCA for prolyl endopeptidase or collagenase-like peptidase, and Suc-Ala-Ala-Pro-Phe-MCA for chymotrypsin were identified in the detergent-soluble fraction of herring spermatozoa. The enzyme activities increased in the presence of herring sperm-activating protein (HSAP). Among them a prolyl endopeptidase [EC. 3. 4. 21. 26] was purified to near homogeneity from herring testis. The molecular mass of the enzyme was 79 kDa and the properties of the enzyme were quite similar to prolyl endopeptidase from other tissues or cells. Both the enzyme activation and the sperm motility activation by HSAP were inhibited by benzyloxycarbonyl-L-thioproline-thioprolinal, a specific inhibitor for prolyl endopeptidase. Furthermore, the motility activation by HSAP was inhibited by substrates of the prolyl endopeptidase. Western blotting with mouse anti-prolyl endopeptidase serum revealed the presence of 79 kDa prolyl endopeptidase in the tail fraction of herring sperm. These results suggest that prolyl endopeptidase exists on the surface of the sperm tail and interacts with the HSAP.
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PMID:Purification and characterization of prolyl endopeptidase from the Pacific herring, Clupea pallasi, and its role in the activation of sperm motility. 1022 18

Metalloproteases are metalloenzymes secreted in the extracellular fluid and involved in inflammatory pathologies or events, such as extracellular degradation. A Zn(2+) metal, present in the active site, is involved in the catalytic mechanism, and it is generally coordinated with histidyl and/or cysteinyl residues of the protein moiety. In this study we have investigated the effect of both pH (between pH 4.8 and 9.0) and temperature (between 15 degrees C and 37 degrees C) on the enzymatic functional properties of the neutrophil interstitial collagenase (MMP-8), gelatinases A (MMP-2) and B (MMP-9), using the same synthetic substrate, namely MCA-Pro-Leu-Gly approximately Leu-DPA-Ala-Arg-NH(2). A global analysis of the observed proton-linked behavior for k(cat)/K(m), k(cat), and K(m) indicates that in order to have a fully consistent description of the enzymatic action of these metalloproteases we have to imply at least three protonating groups, with differing features for the three enzymes investigated, which are involved in the modulation of substrate interaction and catalysis by the enzyme. This is the first investigation of this type on recombinant collagenases and gelatinases of human origin. The functional behavior, although qualitatively similar, displays significant differences with respect to what was previously observed for stromelysin and porcine collagenase and gelatinase (Stack, M. S., and R. D. Gray. 1990. Arch. Biochem. Biophys. 281:257-263; Harrison, R. K., B. Chang, L. Niedzwiecki, and R. L. Stein. 1992. Biochemistry. 31:10757-10762). The functional characterization of these enzymes can have some relevant physiological significance, since it may be related to the marked changes in the environmental pH that collagenase and gelatinases may experience in vivo, moving from the intracellular environment to the extracellular matrix.
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PMID:pH- and temperature-dependence of functional modulation in metalloproteinases. A comparison between neutrophil collagenase and gelatinases A and B. 1102 17


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