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)

Three human basement membranes, glomerular basement membrane (GBM) from renal cortex, alveolar basement membrane (ABM) from lung parenchyma and trophoblast basement membrane (TBM) from the terminal villi of placenta have been isolated by sieving and sonication techniques. Canine GBM and ABM were also prepared. There were marked differences among the membranes from human tissues. Compared to GBM, TBM had very little collagen but contained high concentrations of charged amino acids. ABM was intermediate in composition between GBM and TBM and contained desmosine and isodesmosine indicative of the presence of elastin. Canine ABM (c-ABM) did not contain desmosine or isodesmosine. In the canine system an antigen was detected in ABM which was not present in GBM. The membrane preparations were analyzed for fibronectin content using a specific antiserum to fibronectin. This glycoprotein could not be detected in GBM whereas it was present in ABM in amounts up to 0.8% and in TBM in amounts as high as 7.2%. All the membranes induced the formation of precipitating antibodies in rabbits. Soluble material obtained from the membranes by alkali extraction, reduction of disulfide bonds, enzymatic digestion with elastase, plasmin or collagenase provided immunologically reactive fragments. These soluble fragments gave reactions of identity among the three basement membranes in immunodiffusion reactions in gels with antisera raised to all three BMs. The finding that plasmin digests basement membranes suggests that it may play a role in connective tissue remodeling. The fact that elastase degrades basement membranes provides an endogenous system for injury which may be triggered by infections.
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PMID:Human basement membrane antigens from lung, placenta and kidney. 627 69

Using EDTA extraction and collagenase digestion, rat bone and rat skin were compared in terms of their content of hydroxyproline, hexoses, uronic aicd, sialic acid and plasma proteins. The collagen content of the organic matrix from both tissues was similar. Greater differences were observed in the sialic acid and uronic acid content of the matrix, bone containing higher amounts; smaller differences were found in the levels of hexoses, albumin, IgG and alpha 1 acid-glycoprotein, which are higher in EDTA extracts from bone. The DEAE-cellulose chromatography of the EDTA extracts and soluble collagenase digests indicated the presence of a variety of glycoproteins and a proteoglycan fraction. An acidic glycoprotein, corresponding to sialoprotein, was present in bone but not in skin extracts.
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PMID:Biochemical analyses of EDTA extracts and collagenase digests from bone and skin of Wistar rats. 628 4

The extracellular matrix, prepared by extraction of confluent cultures of human lung WI-38 fibroblasts with a dipolar tonic detergent, contains four major glycoproteins: fibronectin, GP250, GP170, and GP140. All the glycoproteins can be surface-labeled; however, only fibronectin and GP170 can be readily removed by digestion with trypsin (Carter, W. G., and Hakomori, S. (1981) J. Biol. Chem. 256, 6953-6960). Most of the noncovalently bound GP250, GP170, and GP190, an additional minor glycoprotein, can be dissociated from the matrix by extraction with 8 M urea. The remaining insoluble matrix is stabilized by extensive intermolecular disulfide bonds and contains primarily GP140 and fibronectin (Carter, W. G. (1982) J. Biol. Chem. 257, 3249-3257). Affinity-purified, monospecific antibodies were prepared against GP[140 and fibronectin and utilized for detection of GP140 and fibronectin in extracts and conditioned media of WI-38, WI-38 VA13, WI-26, WI-26 VA4, and HT-1080 cells. Additional affinity-purified, polyspecific antibodies that react with GP250, GP190 GP170, and GP140 were also utilized. Fibronectin, GP250, GP190, GP170, and GP140 were all absent from transformed cells. With the exception of GP140, the absence of these glycoproteins from the matrix of transformed cells was paralleled by their accumulation in the conditioned culture media. Incubation of conditioned culture media with collagenase indicated that GP190, GP170, and GP140, as well as other glycoproteins, were digested. Antibodies to GP140 did not react with any other cellular component indicating that it is not a processing product of other matrix glycoproteins. GP140 has characteristics unlike all reported collagen types and appears to be a new collagen-like glycoprotein. In contrast, neither Gp250 nor fibronectin were sensitive to digestion with collagenase. Antibodies that react with GP250 did not react with fibronectin and vice versa, suggesting that GP250 and fibronectin do not share antigenic determinants. The interaction of labeled fibronectin and the labeled, gelatin-binding domain of fibronectin with cells after fractionation on polyacrylamide gels indicated that GP170 is the primary procollagen receptor for fibronectin in the extracellular matrix. GP140 also bound fibronectin but to a lesser degree. Soluble GP170 and GP190 present in the conditioned medium of cultured cells also bound to insolubilized fronectin, confirming the association of GP170 and GP190 with fibronectin. The interaction of the glycoprotein components in the matrix are discussed in relation to their potential cooperative function in cell attachment and their failure to adhere to the surface of transformed cells.
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PMID:Transformation-dependent alterations is glycoproteins of extracellular matrix of human fibroblasts. Characterization of GP250 and the collagen-like GP140. 629 8

The oligomeric glycoprotein hormone, ovine lutropin was treated with anhydrous HF at 0 degrees C for 30, 60 and 180 min and at 23 degrees C for 60 and 180 min. The products, designated deglycosylated lutropin 1 (DGLH-1) to deglycosylated lutropin 5 (DGLH-5) respectively, were characterized by gel filtration, concanavalin A-Sepharose binding, disc electrophoresis, amino acid analysis, carbohydrate composition and spectral properties. The preparations were also evaluated for receptor binding activity and immunological activity and bioassayed in vitro in collagenase-dispersed rat interstitial cells. In DGLH-1, fucose and galactosamine were removed completely, and there was a 94% decrease in hexoses and 39% decrease in N-acetylglucosamine. Reaction with HF at 0 degrees C for 1 or 3h led to removal of all hexoses and additional loss of hexosamines. Reactions at 23 degrees C for either 1 or 3h were not of additional value in deglycosylation and none of the reaction conditions yielded the apohormone. All the five deglycosylated hormone preparations were not retained on immobilized-concanavalin A columns and on Sephadex G-100 they were eluted with an increased V(e)/V(0) ratio consistent with the loss of carbohydrate residues. Loss of all but the last of the N-acetylglucosamine residues decreased the abnormality of lutropin on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, but did not eliminate it. Receptor binding activities of DGLH-1 and DGLH-2 were not different from that of the native hormone, but that of DGLH-3 was slightly decreased and the products obtained at 23 degrees C (DGLH-4 and DGLH-5) had lower activity. Immunoreactivities followed a similar pattern. None of the derivatives had activity in the bioassay in vitro. All of the five derivatives inhibited the action of the native hormone in the bioassay in vitro. Their hormonal antagonistic activity was consistent with the receptor binding activity, with DGLH-5 being the least potent in this respect. The DGLH-4 and DGLH-5 preparations had undergone conformational changes as revealed by 8-anilinonaphthalene-1-sulphonate fluorescence, but this did not result in loss of quaternary structure.
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PMID:Chemical deglycosylation of ovine pituitary lutropin. A study of the reaction conditions and effects on biochemical, biophysical and biological properties of the hormone. 629 61

Parietal yolk sacs isolated from 14.5-day rat embryos and incubated in vitro with either [14C]proline, [3H]mannose or 3H-labeled amino acid mixture synthesized and secreted basement membrane collagenous and noncollagenous glycoprotein components with relative molecular weights of 350,000 (350K), 220,000 (220K), 185,000 (185K), 175,000 (175K) and 150,000 (150K). The 185K and 175K components appeared to be similar to the pro-alpha 1 (IV) and pro-alpha 2(IV) chains, respectively, which have been isolated from other sources. These components were completely susceptible to bacterial collagenase, but were only partially susceptible to alpha-chymotrypsin digestion. The 350K and 220K components appeared to be similar to subunits of laminin (or PYS A and PYS B, respectively) which have been characterized by others, while the 150K component may be similar to entactin (or PYS C). These components were completely resistant to bacterial collagenase and completely susceptible to alpha-chymotrypsin digestion. In addition, the basement membrane of the parietal yolk sac (Reichert's membrane) stained intensely with antibodies directed against either rat laminin or mouse basement membrane procollagen. The results of these experiments suggest that the 14.5-day rat embryo parietal yolk sac is a useful system for studying the structure, biosynthesis and deposition of basement membrane components.
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PMID:Partial characterization of collagenous and noncollagenous basement membrane proteins synthesized by the 14.5-day rat embryo parietal yolk sac in vitro. 629 50

We have isolated a major glycoprotein that appears to be associated with rat skeletal muscle basement membrane. We determined that the glycoprotein was part of the muscle cell surface complex when we found it to be enriched in preparations of muscle ghosts. We isolate the glycoprotein from homogenized muscle preextracted with 4 M and 8 M urea. It elutes as a major component in the presence of 8 M urea/50 mM 2-mercaptoethanol. Its apparent molecular weight on sodium dodecyl sulfate gels is 130,000. Amino acid analysis indicates that it is not a collagen but that it does contain small amounts of hydroxyproline and hydroxylysine. There may be collagenous domains in the glycoprotein molecule, for it is cleaved into three fragments by purified bacterial collagenase. Immunoperoxidase staining confirms that the 130,000-dalton protein is localized at the surface of adult skeletal muscle cells. It is probably a general basement membrane-associated glycoprotein because we found material immunologically cross-reactive with the muscle glycoprotein in basement membrane regions of kidney, liver, brain, and small intestine. We have shown the glycoprotein to be distinct from fibronectin, laminin, and types I, III, IV, and V collagens in enzyme-linked immunosorbent assays.
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PMID:A basement membrane-associated glycoprotein from skeletal muscle. 629 56

Rabbit hepatocytes were isolated by a collagenase perfusion technique, and used to study the binding and endocytosis of the glycoprotein, asialo-orosomucoid, and the neoglycoprotein, Gal39-bovine serum albumin. Both of these proteins contain exposed galactosyl residues, and were avidly bound by the lectin on the hepatic parenchymal cell surface. Steady state and kinetic experiments performed at 2 degrees C and at 37 degrees C revealed the presence of two apparent classes of binding sites totalling 4.7 X 10(5) sites/cell at 2 degrees C, and 6.3 X 10(5) sites/cell at 37 degrees C. At 37 degrees C, both classes of sites participated in internalization of bound ligand. The cells were capable of internalizing about 60 000 molecules/min per cell. The process appeared to be first-order, with a rate constant k = 0.098 min-1 and t1/2 = 7.1 +/- 0.6 min. Binding could be inhibited by galactose-containing compounds, EGTA, and by anti-(hepatic lectin) immunoglobulin G. The inhibition by antibody appeared to be reversible upon removal of antibody-containing medium.
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PMID:Binding and endocytosis of glycoproteins and neoglycoproteins by isolated rabbit hepatocytes. 631 Nov 84

The mineral and non-collagenous organic components of normal human femoral cortex were examined following powdering, demineralization with EDTA and digestion with bacterial collagenase. The protein, hexose, sialic acid and uronic acid contents of the matrix were determined. Neonatal bone had lower levels of mineral and calcium and higher levels of organic material and sialic acid than adult bone, suggesting increased glycoprotein content in neonatal bone. The soluble non-collagenous matrix of human femoral cortex was examined by gel filtration on Sephadex G100 and by ion-exchange chromatography on DEAE-cellulose. Four fractions were eluted off Sephadex-G100: a large molecular weight fraction, a shoulder on the descending portion of this, both of which contained sialic acid and two smaller molecular weight fractions. The material eluted off DEAE-cellulose was separated into 6 fractions which were similar to those found for beef and rabbit bone matrix. Human bone matrix appeared more resistant to collagenase digestion than beef bone, soluble collagen eluted later off DEAE-cellulose than beef bone; sialic acid gave 3 peaks: a major and two lesser ones. The sialic acid-containing material in the fifth fraction was probably bound to proteoglycan. Rabbit bone has 2 to 3 sialic acid peaks whereas beef bone has one, indicating species differences in cortical bone matrix.
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PMID:Chemical composition of human bone. 631 48

The organ culture of neonatal mouse calvaria produced both collagenase and collagenase inhibitor. The inhibitor was purified by a series of column chromatographies: DEAE-cellulose and CM-cellulose ion-exchange chromatography, concanavalin A-Sepharose and heparin-Sepharose affinity chromatography, and finally by Sephacryl S-200 gel filtration. The purified inhibitor migrated as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and had a molecular mass of 28,000. The inhibitor was purified 140-fold to a specific activity of 163 units/mg with a yield of 18% over the first step of the purification by DEAE-cellulose chromatography. The inhibitor stained positively for carbohydrate with periodic acid-Schiff's reagent indicating, in conjunction with its affinity to concanavalin A, that the inhibitor is a glycoprotein. In addition to mouse bone collagenase, this inhibitor also inhibited chick bone, rat bone, rabbit corneal, and human gingival collagenase, but did not inhibit bacterial collagenase.
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PMID:Mouse bone collagenase inhibitor: purification and partial characterization of the inhibitor from mouse calvaria cultures. 632 Jul 46

A collagenous glycoprotein (Mr 140000) was isolated from dissociative extracts of foetal bovine nuchal ligament and purified by a combination of ion-exchange and gel-filtration chromatography. This glycoprotein (designated MFPI) exists as a large-Mr disulphide-bonded aggregate in the absence of a reducing agent. The purified glycoprotein was shown to contain about 6% (w/w) carbohydrate, mostly as galactose, glucose and mannose. Amino acid analysis showed the presence of hydroxyproline and hydroxylysine, indicative of its collagenous nature. The collagenous nature of this glycoprotein was further investigated by enzyme digestion. Pepsin digestion produced three major fragments, which were identical with peptides of type VI collagen. Bacterial-collagenase digestion of the unreduced glycoprotein also produced several discrete peptides. However, reduction of the glycoprotein before bacterial-collagenase digestion resulted in the degradation of these discrete peptides. Glycoprotein MFPI extracted in dissociative conditions appears to be a larger-Mr form of type VI collagen, believed to originate from microfibrillar components in the intact tissue.
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PMID:A collagenous glycoprotein found in dissociative extracts of foetal bovine nuchal ligament. Evidence for a relationship with type VI collagen. 633 16


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