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)

The process of collagenolysis and the source of collagenase liberated from different cell types in the colonic mucosa has been investigated by the lysis of collagen gels in vitro. The reconstituted collagen gel strongly reacted to periodic acid Schiff (PAS) when stained with combined alcian blue-PAS, indicating the presence of glycoprotein with neutral sugars in the collagen gel. Colonic explants of rabbits produced visible collagenolysis. An area of alcian blue stained gel was seen replacing the usual PAS staining around the area of the lysis. Several histochemical methods revealed that the columnar cells had multiplied with high enzymatic activity and penetrated the collagen gel where collagenolysis took place. The action of several proteolytic enzymes on collagen gel showed that ficin caused lytic activity, even though collagen is resistant to most proteolytic enzymes. Papain, pepsin and trypsin altered composition of collagen gel from neutral mucopolysaccharide to acid mucopolysaccharide. Collagenase and pronase at low concentration were found to cause extensive collagenolysis. The synthesis and breakdown of collagen is a desirable balanced process in the remodelling of connective tissue. This dynamic equilibrium may be achieved through the subtle interplay of cells liberating and inhibiting collagenase.
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PMID:An investigation into the mechanism of collagenolytic activity in colonic mucosa by a tissue culture method. 329 25

A polyclonal antiserum was prepared in rabbits against the structural glycoprotein (SGP) complex previously isolated from a bacterial collagenase digest of bovine corneal stroma (R. Alper, Curr. Eye Res. 2:479, 1983). Direct and indirect enzyme-linked immunosorbent assays indicated that the antiserum was specific for the SGP-complex and did not react with Types I, III and IV collagen, fibronectin, laminin or actin. Immunoblot experiments indicated that the antiserum reacted with all of the components of the SGP-complex as well as with the cell matrix laid down by bovine keratocytes in culture. An attempt was made to isolate individual antibodies from the antiserum by selective elution from immunoblots of the components of the SGP-complex separated by SDS-PAGE. It was found that regardless of the protein band from which the antibody was eluted, every antibody isolated reacted with every protein component of the SGP-complex suggesting that the SGP-complex may have been derived from a single precursor protein and that the observed heterogeneity of the SGP-complex may have been the result of proteolytic breakdown of the protein held together by disulfide bonds. When the anti-SGP antiserum was used to immunoprecipitate 14C-proline labeled proteins from the media of bovine keratocytes in culture, the major protein observed had a Mr of about 140,000 daltons, similar to that of GP-140 also known as CL-glycoprotein. These proteins have been shown to represent the tissue form of Type VI collagen. To test the hypothesis that the SGP-complex may be related to the GP-140 (CL-glycoprotein), ELISA and immunoblotting studies were performed comparing the properties of the anti-SGP serum with those of a polyclonal antibody specific for Type VI collagen. The SGP-complex reacted positively by ELISA with the anti-human Type VI collagen antiserum and, conversely, human Type VI collagen gave a positive ELISA reaction with an antiserum against the SGP-complex. The anti-human Type VI collagen antiserum reacted with most of the major components of the SGP-complex on immunoblots of SDS-PAGE gels. These data indicate that the SGP-complex is related to and probably is derived from the tissue form of Type VI collagen.
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PMID:The bovine corneal SGP-complex is related to the tissue form of type VI collagen. 335 3

The human tissue inhibitor of metalloproteinases (TIMP) is a glycoprotein with a molecular weight of 28,000. It appears to be ubiquitous in human mesoderm tissues and has previously been shown to be identical to the collagenase inhibitor isolated from human skin fibroblasts. TIMP inhibits type I- and IV-specific collagenases and other neutral metalloendoproteinases that may be responsible for the degradation of extracellular matrix in tumor cell metastasis. In this work we have utilized recombinant human TIMP (rTIMP) obtained by expression of its cDNA gene (Carmichael et al., Proc. Natl. Acad. Sci. USA, 83:2407, 1986). The rTIMP is shown to have similar inhibition properties as natural TIMP against human skin fibroblast collagenase. In an in vitro amnion invasion assay system, rTIMP inhibited the invasion of B16-F10 murine melanoma cells through the human amniotic membrane at an identical concentration to that reported previously for natural TIMP. The mechanism by which rTIMP inhibits amniotic membrane invasion was compared to the mechanism by which the fibronectin receptor binding peptide RGDS and the aminin receptor binding peptide YIGSR inhibit amnion invasion. RGDS and YIGSR inhibited strong binding of the tumor cells to the amniotic membrane. In contrast rTIMP did not inhibit the cell adhesion step in amnion invasion, but actually increased the number of tumor cells that were tightly bound to the amnion. Thus rTIMP appears to inhibit a later step in the amnion invasion process, following B16-F10 cell adhesion. C57BL/6 mice treated with i.p. injections of rTIMP every 12 h for 6.5 days showed a significant inhibition of metastatic lung colonization by B16-F10 murine melanoma cells. While the rTIMP inhibited the number of metastatic lung tumors formed, it had no significant effect on the size of the lung tumors. Furthermore, tumors grown s.c. in mice receiving 12-h i.p. injections of rTIMP for 6.5 days, as in the in vivo colonization assay, showed no difference in size from controls. Thus the anticolonization effect of rTIMP appears not be due to an effect on tumor growth, but on the invasion step itself. The inhibition of lung colonization in C57BL/6 mice by rTIMP is one of the first examples showing an antimetastatic effect of a selective metalloproteinase inhibitor in a mammalian animal model, and supports an essential role for metalloproteinase(s) in the extravasation and invasion of tumor cells during lung colonization by blood-borne tumor cells.
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PMID:Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells. 341 7

An inhibitor of serine proteinases from human articular cartilage was purified to homogeneity by sequential ultrafiltration and ion exchange chromatography on CM-Sephadex C-50. The apparent molecular weight of the cationic glycoprotein (pI greater than 10) was determined to be 16.5 X 10(3) by SDS gel electrophoresis. The inhibitor blocked the activity of leukocyte elastase, cathepsin G and trypsin but not leukocyte collagenase. In kinetic studies for the interactions with leukocyte elastase a firm enzyme-inhibitor binding was obtained. Amino acid analyses did not reveal homologies with other serine proteinase inhibitors already purified from human tissues.
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PMID:Purification and characterization of a serine proteinase inhibitor from human articular cartilage. 349 75

Using a monoclonal anti-tubular basement membrane antibody (alpha TBM-Ab) affinity column, we isolated from collagenase-solubilized human renal tissue (HSRTA) a predominantly 48,000-mol-wt moiety (H3M-1) which is selectively recognized by antisera from two patients with alpha TBM-Ab-associated interstitial nephritis (alpha TBM disease). Whereas both antisera had alpha TBM-Ab titers of 1:64-1:128 by immunofluorescence on tissue sections, their reactivity with H3M-1 in a solid-phase radioimmunoassay was demonstrable at dilutions up to 1:10,000. While these sera displayed some reactivity with pre-column HSRTA, this was markedly less than with H3M-1. HSRTA depleted of H3M-1 by passage over the alpha TBM-Ab affinity column was almost completely depleted of reactivity. Neither pooled normal human sera nor sera from patients with a variety of renal lesions not associated with alpha TBM-Ab (including interstitial nephritis and antiglomerular basement membrane disease) were reactive with H3M-1. Both patient antisera containing alpha TBM-Ab were also highly reactive with R3M-1, the 48,000-mol-wt rabbit glycoprotein antigen of experimental alpha TBM disease. Furthermore, a competitive inhibition radioimmunoassay revealed that alpha TBM-Ab from rodents with experimental alpha TBM disease could inhibit 45-98% of the R3M-1 binding reactivity of patient antisera and 85% of the H3M-1 binding reactivity of patient antisera, thus suggesting paratypic cross-reactivity. We conclude, therefore, that tubular basement membrane target epitopes and their paratypic recognition are highly conserved among mammals.
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PMID:Isolation of the target antigen of human anti-tubular basement membrane antibody-associated interstitial nephritis. 351 74

We examined the ability of fibronectin, an extracellular glycoprotein that interacts with cell surfaces and matrix components, to bind to glomerular basement membrane and the effect of diabetes on this binding. 125I-labeled fibronectin binding to rat glomerular basement membrane (GBM) was dose dependent, related to time and amount of basement membrane, and inhibited by unlabeled fibronectin but not by unrelated proteins. Binding was reduced approximately 60% when GBM was pretreated with collagenase and approximately 24% when pretreated with chondroitinase plus heparinase. Treatment with NaCl had little effect on binding, whereas reduction with beta-mercaptoethanol removed approximately 25% of the bound 125I-fibronectin. Binding to samples prepared from rats with streptozocin-induced diabetes was significantly increased compared with that observed with control preparations at all concentrations of fibronectin and of basement membrane tested. The findings provide direct evidence that fibronectin binds to GBM and that this binding, which represents a biologic function of the protein, is enhanced in diabetes.
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PMID:Fibronectin binding to glomerular basement membrane is altered in diabetes. 356 74

Single viable muscle fibers isolated from adult rats by collagenase digestion rapidly bind dissociated spinal neurons or PC-12 cells but not a variety of other cells tested. The adhesion process is calcium-independent, temperature-sensitive, and is not blocked by pretreating cells with inhibitors of energy metabolism or actin polymerization. Adhesion is mediated by a carbohydrate-binding protein and can be inhibited by N-acetylneuraminic acid or mucin, a glycoprotein with high sialic acids content. The hapten inhibitors do not dissociate cells if added after aggregation has occurred. Experiments to block adhesion by pretreatment of cells with either neuraminidase or mucin show that the sialic acids-rich moiety is on the nerve cells, while its receptor is on the muscle fibers.
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PMID:Rapid adhesion of nerve cells to muscle fibers from adult rats is mediated by a sialic acid-binding receptor. 371 Nov 46

Hydrophobic protein of 6,000 and 14,000 daltons was isolated from mammalian pulmonary surfactant obtained from canine, human, and bovine alveolar lavage material. Low molecular weight, hydrophobic, surfactant-associated protein (SAP), herein referred to as SAP 6-14, was distinguished from SAP-35, the major glycoprotein in mammalian surfactants (the 35,000 dalton glycoprotein A or apolipoprotein A) by amino acid composition, peptide mapping, and by resistance of SAP 6-14 to digestion by endoglycosidase F, collagenase, trypsin, and other proteases. The amino acid composition of SAP 6-14 was found to be highly enriched in leucine and other hydrophobic amino acids. The characteristics of protein isolated from bovine replacement surfactant extracts utilized for the treatment of hyaline membrane disease in humans were also studied. SAP 6-14 isolated from calf lung surfactant replacement extracts (CLSE) and surfactant-TA were found to be identical to SAP 6-14 isolated from ether/ethanol extracts of various mammalian surfactants. By contrast, SAP-35, the major surfactant-associated glycoprotein of molecular weight = 35,000, and other higher molecular weight proteins were not detected in significant quantities in the CLSE or surfactant-TA replacement surfactants, either by highly sensitive silver stain analysis or by immunoblot using monospecific antisera generated against bovine SAP-35. Biophysical studies of the CLSE replacement surfactant containing only SAP 6-14 and native phospholipids demonstrated full surface activity compared to natural lung surfactant. Dynamic surface tension lowering and adsorption properties of CLSE were essentially identical to those of freshly isolated bovine whole surfactant. Thus, hydrophobic SAP 6-14 is the only protein detected in bovine lung extract surfactants with full biophysical activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Hydrophobic surfactant-associated protein in whole lung surfactant and its importance for biophysical activity in lung surfactant extracts used for replacement therapy. 375 57

We have isolated type VI collagen, a transformation-sensitive glycoprotein of the extracellular matrix, in an intact, disulfide-bonded form. The protein contains a 200 kd subunit and two different 140 kd subunits in a stoichiometric ratio. Based on the amount of hydroxyproline and hydroxylysine, the sensitivity to bacterial collagenase and the cross-reactivity with antibodies to pepsin-extracted type VI collagen, we have identified the 200 kd subunit as the alpha 3(VI) chain and the two 140 kd subunits as the alpha 1(VI) and alpha 2(VI) chains. The alpha 3(VI) chain is synthesized by cells in culture as a precursor of 260 kd, while no precursor form of the other two chains could be detected.
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PMID:Type VI collagen is composed of a 200 kd subunit and two 140 kd subunits. 379 2

Surfactant-associated glycoprotein A [molecular weight (Mr) = 34,000, isoelectric point (pI) 4.6-5.0] and its sulfhydryl dependent oligomers were purified and partially characterized from surfactant obtained from human alveolar lavage. Two major forms of the protein were identified by silver stain and immunoblot analysis of surfactant using human surfactant-associated glycoprotein A antisera: glycoprotein A2, Mr = 34,000 and glycoprotein A1, Mr = 28,000. The larger form was reduced to Mr = 28,000 by treatment with endoglycosidase F, indicating the presence of complex N-linked oligosaccharide on the molecule. Charge heterogeneity was decreased and the isoelectric point increased by treatment with neuroaminidase, supporting the presence of sialic acid. Homology between the proteins Mr = 34,000 and 28,000 was confirmed by analysis of two-dimensional tryptic and chymotryptic peptides of 125I-iodo-glycoproteins A1 and A2 which were identical. The protein was very rich in glycine and its amino acid composition was similar to that of glycoprotein A previously reported for the dog and rat. Treatment of glycoproteins A with bacterial collagenase resulted in the generation of highly glycosylated peptides Mr = 20,000-22,000, pI 4.6-5.0, which no longer formed sulfhydryl-dependent oligomers, supporting the presence of significant collagen-like region in the molecule. In the absence of reducing agents, glycoprotein A from surfactant was present as sulfhydryl-dependent dimers and larger oligomers. Higher molecular weight aggregates of glycoproteins A were also present in lavage material even after sulfhydryl reduction. Glycoproteins A were identified in surfactant from amniotic fluid, normal adult lung lavage, human cadaver lung lavage, and material obtained from lung lavage from a patient with alveolar proteinosis.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Characteristics of human surfactant-associated glycoproteins A. 383 68


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