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

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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)

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

Samoyed hereditary glomerulopathy (SHG) in dogs serves as a model for human X-linked hereditary nephritis (HN). We previously showed that glomerular capillaries of affected males did not stain by immunofluorescence (IF) using serum from a patient with Goodpasture's syndrome. Our goal in the present study was to determine whether the NC1 domain of the collagen type IV molecule, which contains Goodpasture antigen (GPA), could be demonstrated in these dogs, and to assess its immunological reactivity. By SDS-PAGE, NC1 in collagenase digests of glomerular basement membranes (GBM) of unaffected and carrier female dogs in the family with SHG showed 24 kilodalton (kD), 26 kD and 28 kD monomer, and 46 kD and 47 kD dimer components, but the 24 kD monomer was diminished in the affected males. By IF, a rabbit antibody to NCl stained glomerular capillaries of unaffected, affected male, and carrier female dogs. In contrast, a human anti-GBM plasmapheresis fluid (PPF) stained glomerular capillaries of only the unaffected and carrier female dogs. By RIA, both antibodies reacted strongly with NCl in collagenase digests of GBM of the unaffected and carrier female dogs, but showed reduced reactivity with NCl of affected males. By Western blotting, both antibodies bound to dimers and 24 kD and 26 kD monomers of the NCl domain in collagenase digests of GBM of unaffected and carrier female dogs. However, in affected males, the rabbit anti-NCl antibody did not bind to the 24 kD monomer, while the human anti-GBM PPF showed weak binding to the 24 kD and 26 kD monomers.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Abnormalities in the NC1 domain of collagen type IV in GBM in canine hereditary nephritis. 265 61

Synthetic activity of collagen types was examined in cultured arterial smooth muscle cells during modulation from synthetic to contractile phenotype by treatment with dimethyl sulfoxide (DMSO). Smooth muscle cells of rabbit thoracic aorta cultured with a 1% supplement of DMSO for 8 days (DMSO group) predominantly exhibited cellular features of the contractile type with abundant microfilaments and a distinct basement membrane. Cultured cells in the DMSO group or in controls during stationary or subconfluent phase were labeled with [3H]proline for 24 h, and the samples including the cell layer and medium were analyzed. The incorporation of proline into bacterial collagenase-digestible fractions was increased slightly in the DMSO group. Type analysis of the collagenous protein by SDS-PAGE and subsequent fluorography disclosed a markedly increased ratio of type IV/I collagen and a slightly increased type V/I collagen ratio, as compared with those of controls. A decrease of type III collagen production in DMSO-treated cells probably due to their lower cell density was also recognized. From these biochemical and morphological observations, it is suggested that increased synthesis of minor collagen types, particularly type IV collagen, is closely associated with smooth muscle phenotypic expression following DMSO treatment. Similar cellular events may occur in smooth muscle cells migrating into the intima during the process of arteriosclerosis in vivo.
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PMID:Altered synthesis of collagen types in cultured arterial smooth muscle cells during phenotypic modulation by dimethyl sulfoxide. 265 78

Anti-glomerular basement membrane (GBM) nephritis is associated with production of antibodies to the Goodpasture antigen (GPA) component of the NC1 domain of collagen type IV. We studied a patient with anti-GBM nephritis with regard to 1) reactivity of the anti-GBM antibodies in his serum, plasmapheresis fluid (PPF), and an eluate prepared from GBM of his nephrectomy specimen, and 2) electrophoretic and immunologic properties of the NC1 domain extracted by collagenase digestion from GBM of his nephrectomy specimen. Antibodies to different NC1 determinants in serum, PPF and eluate were detected by immunofluorescence of glomerular capillaries of normal kidney. In addition, the antibody in PPF, but not in the eluate, reacted strongly in a plate-binding radioimmunoassay with NC1 domain extracted from normal human GBM, and bound by Western blotting to both dimer (46 kD and 49 kD) and monomer (24 kD, 26 kD and 28 kD) components of the NC1 domain. Analysis of the NC1 domain in the patient's GBM by SDS-PAGE showed a number of abnormalities, including an absence of monomer bands. Moreover, there was diminished reactivity of the patient's NC1 domain by the radioimmunoassay and Western blotting, using his PPF and a rabbit anti-NC1 antiserum. These findings indicated that there were different types of antibodies to NC1 domain in PPF and eluate, associated with an abnormal NC1 domain in GBM. These results have allowed us to speculate on the pathogenesis of anti-GBM nephritis in this patient.
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PMID:Characterization of the NC1 domain of collagen type IV in glomerular basement membranes (GBM) and of antibodies to GBM in a patient with anti-GBM nephritis. 270 12

A procedure for extraction and quantification of fibronectin in human aortic tissue is described in this paper. Dried, defatted samples of human aortic tissue were subjected to sequential extraction with (i) 0.89% NaCl, 10 mmol/l Tris/HCl, pH 7.4, (ii) 5 mg/ml heparin, 2 mol/l urea and (iii) collagenase digestion. More than 75% of hexosamine-containing molecules were solubilized by this procedure. Immunoblotting of extracted proteins separated by SDS-PAGE showed that extracted fibronectin had a mobility in the same range as that of plasma fibronectin. Fibronectin ELISA performed on these extracts gave dilution curves parallel to the standard curve, the sensitivity was 2.7 micrograms/l. Recoveries of a fibronectin standard added to the NaCl, heparin/urea and collagenase solutions during extraction were 97%, 90% and 84% respectively. Normal aortic tissue from 31 patients was subjected to the sequential extraction scheme and fibronectin quantification in the various extracts demonstrated that 4.52 +/- 1.79 micrograms was dissolved in the NaCl extracts, 5.41 +/- 2.28 in the heparin/urea extract and 1.08 +/- 0.43 in the collagenase digest, respectively. (Values are expressed as micrograms fibronectin/10 mg dry, defatted tissue (mean +/- SD]. Our results indicate that the ELISA method can be applied for the measurement of fibronectin in extracts of human aortic tissue. This might be useful in the study of diseases where alterations in arterial fibronectin content may be expected.
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PMID:Quantification of fibronectin in extracts of human aortae by an ELISA. 274 Aug 16

Collagen accumulation is a major feature of pulmonary fibrosis and other fibrotic lesions. We have studied the synthesis of collagens in fibroblasts cultured from normal and fibrotic human lung specimens and evaluated how it is affected by transforming growth factor-beta (TGF-beta). Fibroblasts were obtained from normal and fibrotic adult human lungs (n = 11; normal = 6, idiopathic pulmonary fibrosis = 5). They were exposed to TGF-beta and pulse-labeled with [3H]proline and [3H]glycine. Collagen production was measured as bacterial collagenase-susceptible radioactivity, and collagen mRNA levels were determined by a solution hybridization assay using labeled procollagen alpha 1[I] cDNA clone HF677 as probe. Synthesis of collagen types I, III, and V were assessed after separating them by DEAE-cellulose chromatography and SDS-polyacrylamide gel electrophoresis. The results showed that both normal and fibrotic lung fibroblasts synthesized similar amounts of collagen. Type I was the major collagen species synthesized by both normal and fibrotic cell types, and the relative proportion of type I, III, and V collagens was similar in both cell types. TGF-beta caused a two to fourfold increase in stimulation of collagen production and collagen mRNA levels, and no differences were detected in the response of normal and fibrotic lung fibroblasts. All collagen types were stimulated by the TGF-beta. TGF-beta did not increase fibroblast proliferation and the majority of normal and fibrotic lung cells exposed to TGF-beta remained in G1 phase of the cell cycle. We conclude that fibroblasts of normal and fibrotic human synthesize similar amounts of collagens.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Collagen synthesis by normal and fibrotic human lung fibroblasts and the effect of transforming growth factor-beta. 275 Nov 76

Drugs in the tetracycline family can inhibit mammalian tissue collagenase both in vitro and in vivo by a mechanism that is independent of antibiotic action. The epiphyseal cartilages of rachitic rats contain extremely high levels of collagenase (CGase), and we have used this model to study further the phenomenon of tetracycline inhibition of tissue CGase. Rickets was induced in rats by phosphate/vitamin D deficiency and parameters of gross bone morphology, bone chemistry, and serum chemistry were evaluated in both rachitic and nonrachitic animals with and without treatment with oral tetracyclines (TETs). Minocycline (or doxycycline) partially suppressed the appearance of many of the expected changes in the rachitic animals, including gross bone hardness, growth plate widening, long bone length, suppression of weight gain, and decreased bone ash content. The effects were dose dependent and were associated with marked suppression of the enhanced CGase activity. Examination of collagen breakdown products by SDS-PAGE documented that the rachitic enzyme behaved like other mammalian collagenases including in vitro inhibition with minocycline 10-20 micrograms/ml and with a nonantibiotic tetracycline. No evidence of TET osseous toxicity was noted, and, in fact, administration of TET to nonrachitic animals had a mildly favorable effect on growth and development. TET suppression of CGase can be demonstrated in a well defined model system and this form of pharmacologic enzyme inhibition can be a useful probe for delineating the role of the enzyme in connective tissue pathology.
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PMID:Inhibition of epiphyseal cartilage collagenase by tetracyclines in low phosphate rickets in rats. 284 40

Cathepsins B and L were purified from human kidney. SDS/polyacrylamide-gel electrophoresis demonstrated that cathepsins B and L, Mr 27000-30000, consist of disulphide-linked dimers, subunit Mr values 22000-25000 and 5000-7000. The pH optimum for the hydrolysis of methylcoumarylamide (-NHMec) substrates (see below) is approx. 6.0 for each enzyme. Km and kcat. are 252 microM and 364s-1 and 2.2 microM and 25.8 s-1 for the hydrolysis of Z-Phe-Arg-NHMec (where Z- represents benzyloxycarbonyl-) by cathepsins B and L respectively, and 184 microM and 158 s-1 for the hydrolysis of Z-Arg-Arg-NHMec by cathepsin B. A 10 min preincubation of cathepsin B (40 degrees C) or cathepsin L (30 degrees C) with E-64 (2.5 microM) results in complete inhibition. Under identical conditions Z-Phe-Phe-CHN2 (0.56 microM) completely inhibits cathepsin L but has little effect on cathepsin B. Incubation of glomerular basement membrane (GBM) with purified human kidney cathepsin L resulted in dose-dependent (10-40 nM) GBM degradation. In contrast, little degradation of GBM (less than 4.0%) was observed with cathepsin B. The pH optimum for GBM degradation by cathepsin L was 3.5. Cathepsin L was significantly more active in degrading GBM than was pancreatic elastase, trypsin or bacterial collagenase. These data suggest that cathepsin L may participate in the lysosomal degradation of GBM associated with normal GBM turnover in vivo.
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PMID:Human kidney cathepsins B and L. Characterization and potential role in degradation of glomerular basement membrane. 284 49

Adult Onchocerca volvulus recovered for excised nodules by dissection or treatment with collagenase have been used as a source of RNA for in vitro translation experiments. RNA was purified using either the hot phenol/SDS procedure or the guanidine isothiocyanate protocol. Immunoprecipitation experiments performed on in vitro products demonstrate a marked heterogeneity in responses by individed human infection sera. Further immunoprecipitation experiments demonstrate cross reactivity between O. volvulus and other filarial nematodes.
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PMID:Isolation and in vitro translation of Onchocerca volvulus mRNA. 285 97

To clarify interactions between carcinoma and mesenchymal cells, we examined the extracellular matrix-substance remaining on culture dishes after confluent growths of gastric carcinoma cells were removed with EDTA. The matrix synthesized by poorly differentiated adenocarcinoma cells (cell lines KATO-III and MKN-45) cultivated in serum-free medium has a fibroblast (cell line WI38)-attachment activity, which is not detected in the matrix synthesized by a well differentiated adenocarcinoma (cell line MKN-28). This activity was not observed in KATO-III-matrix extracted with 6 M urea, but could be detected in a 1% SDS extract from the remaining matrix on the culture dishes after 6 M urea extraction. The activity was abolished by treatment with pronase (16 micrograms/ml), trypsin (0.005%) or alkali, but was unaffected by collagenase (80 micrograms/ml, 4 h) or chondroitinase ABC (1 U ml, 1 h). It is conceivable that the fibroblast-attachment activity of the matrix produced by poorly differentiated adenocarcinoma cells is related to the proliferation of interstitial connective tissue in vivo.
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PMID:Extracellular matrix of cultivated, poorly differentiated human gastric adenocarcinoma cells promotes attachment and spreading of mesenchymal cells. 290 Nov 69


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