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)

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

Chick embryo epiphyseal cartilage has been shown to contain three different proteoglycan species (PG-H, PG-Lb, and PG-Lt). This report is concerned with the purification and characterization of the third proteoglycan, PG-Lt. The proteoglycan can be separated from the other two by virtue of its low buoyant density in a CsCl density gradient and further purified by consecutive ion exchange and gel chromatography. The final preparation is composed of PG-Lt monomer and PG-Lt oligomer. The amino acid composition of PG-Lt is quite different from that of PG-H and PG-Lb and rather resembles that of collagens with respect to high content of glycine and high degrees of hydroxylation of proline and lysine. PG-Lt monomer is composed of disulfide-bonded subunits of Mr congruent to 120,000 and 190,000 as demonstrated by its gel electrophoretic behavior after reduction with 2-mercaptoethanol. The latter, but not the former, contains dermatan sulfate chains with glucuronic acid/iduronic acid residues and yields a protein-enriched core molecule of Mr congruent to 100,000 after digestion with chondroitinase ABC. Both of the protein subunits are completely digestible with bacterial collagenase. Immunofluorescence microscopic examination of cartilage tissues, using an antibody against PG-Lt, shows that this proteoglycan exists in both the cartilage matrix and perichondrial noncartilagenous region. When chondrocytes are plated onto tissue culture dishes, the antibody stains strands found on the cell surfaces and in the intercellular space of substrate-attached cell layers, suggesting that PG-Lt mediates cell-to-cell and cell-to-substrate contacts.
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PMID:Isolation and characterization of a third proteoglycan (PG-Lt) from chick embryo cartilage which contains disulfide-bonded collagenous polypeptide. 687 91

Attempts were made to isolate adherent phagocytic cells (macrophages) from mouse Peyer's patch cell suspensions. Cell suspensions prepared by teasing apart the Peyer's patches contained no adherent phagocytic cells. However, if Peyer's patch fragments were treated with collagenase to disrupt the tissue matrix, cells prepared in this way contained a subpopulation of adherent phagocytic cells. These cells comprised only 0.1-0.2% of the total nucleated cell population of the Peyer's patch. Similar cells could also be isolated from the Peyer's patches of germ-free mice, but as judged by their ability to ingest opsonized erythrocytes, these cells were less activated than cells from the Peyer's patches of normal mice. Adherent cells from the Peyer's patches of normal mice could present antigen (ovalbumin) to T cells, and Peyer's patches cell suspensions containing adherent cells could be stimulated in vitro to produce an anti-sheep red blood cell plaque-forming cell response in the absence of 2-mercaptoethanol. These studies show that although the frequency of phagocytic adherent cells is extremely low in Peyer's patches, these cells have functions consistent with that of adherent cells in other lymphoid tissues.
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PMID:Isolation and functional characteristics of adherent phagocytic cells from mouse Peyer's patches. 706 73

Somatic extracts of Nippostrongylus brasiliensis contain protease inhibitor(s) capable of inhibiting the activity of trypsin and chymotrypsin A and B. This inhibitor was partially purified by affinity chromatography. Its molecular weight is in the range of 9500-10 000. The inhibition of both trypsin and chymotrypsin depends on the same or closely adjacent active sites of the inhibitor molecule. The inhibitor is unaffected by heating, pH changes or urea, but is sensitive to 2-mercaptoethanol The formation of the enzyme-inhibitor complex is time-dependent. The complex does not dissociate with KC1. The inhibitor has no effect on the activity of elastase, subtilisin, pepsin, rennin, papain and collagenase.
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PMID:A protease inhibitor of Nippostrongylus brasiliensis. 725 48

Liver and peritoneal macrophages under similar test conditions behaved in an identical manner with regard to accessory cell effects in the lymphocyte response to concanavalin A. When present in low concentrations (less than or equal to 3.3%) they stimulate lymphocytes, and when present in high concentrations (greater than or equal to 10%) they inhibit lymphocyte proliferation. These two effects are, however, mediated through totally different mechanisms. Stimulation was an early effect, required viable cells, was not affected by enzymatic treatment of macrophages, and was similar to the effect of 2-mercaptoethanol, allogeneic macrophages, and even non-macrophages. Inhibition occurred at a larger stage of lymphocyte transformation, was sensitive to collagenase and pronase treatment of macrophages, was more specifically due to macrophages, was reduced with allogeneic macrophages, and persisted after freeze-thawing of macrophages. Removal of Fc receptors or related segments of the surface of macrophages greatly reduced their inhibitory capacity, whereas removal of foreign surface receptors apparently had no consequence.
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PMID:The accessory cell effects of liver macrophages in concanavalin A stimulation of rat spleen lymphocytes. 738 53

Myocardial cells were isolated after treatment with collagenase (0.05%) and hyaluronidase (0.1%) by discontinuous-gradient centrifugation on 3% Ficoll. Nuclei derived from these myocardial cells were then fractionated on a discontinuous sucrose density gradient with the following steps: (I) 2.0M/2.3M, (II) 2.3M/2.4M, (III) 2.4M/2.5M, (IV) 2.5M/2.6M, and (V) 2.6M/2.85M. The myocardial nuclei were sedimented in the interfaces of gradient fractions (II) and (III). Nuclei from whole ventricles that had been treated with the enzymes before isolation sedimented into five major subsets of nuclei. These findings suggest that nuclei sedimented in the isopycnic gradient at fractions (II) and (III) are most probably derived from myocardial cells. However, this procedure is laborious and lengthy, and the recovery of myocardial-cell nuclei is low. An alternative method was developed to isolate an enriched fraction of myocardial-cell nuclei from whole ventricular tissue without exposing the tissues to enzyme digestion. These ventricular nuclei could be fractionated into five nuclear subsets by using the same discontinuous sucrose density gradient as that described above. The content of DNA, RNA and protein per nucleus for each band was determined. Although the DNA content per nucleus was constant (10pg), that of RNA varied from 1.5 to 4.5pg and that of protein from 16 to 24pg. Nuclei from each band were examined by light-microscopy: large nuclei occurred in the ligher regions whereas smaller nuclei were found in the denser regions of the gradient. From the size distribution pattern of myocardial-cell nuclei compared with that of total ventricular nuclei, it was found that nuclear subsets (II), (III), and (IV) were similar to myocardial nuclei. Electrophoretic analyses of the proteins solubilized in sodium dodecyl sulphate/phenol or Tris/EDTA/2-mercaptoethanol/phenol obtained from each nuclear subset indicate that these fractions are similar, with limited qualitative differences. These findings indicate that isolation of an enriched fraction of myocardial-cell nuclei could be achieved by discontinuous-sucrose-density-gradient centrifugation.
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PMID:Fractionation of rat ventricular nuclei. 739 68

Ca2+ dependent conformational change of collagenase resistant fragment (CRF) of human surfactant protein A (SP-A) was studied by measurements of the far UV circular dichroism spectrum. The spectrum was altered by Ca2+ and DTT. The beta-sheet content was decreased by the addition of Ca2+ from 28.1 to 26.6%. On the other hand, the beta-sheet content was increased in the presence of dithiothreitol from 28.1 to 36.0%, and decreased by the addition of Ca2+ from 36.0 to 30.5%. The total Ca2+ concentration required for half maximal change of the ellipticity at 220 nm was estimated to be 30 microM both in the presence and absence of dithiothreitol. One of the functions of SP-A, enhancement of phospholipid uptake by alveolar type II cells, was abolished by the addition of 2-mercaptoethanol. These results strongly indicate a relationship between the conformation of CRF and SP-A functions.
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PMID:Calcium and dithiothreitol dependent conformational changes in beta-sheet structure of collagenase resistant fragment of human surfactant protein A. 836 13

To determine whether morphologic changes are accompanied by variations in the biochemical and antigenic properties of the cuticle of Onchocerca volvulus during development, we isolated and compared the 2-mercaptoethanol soluble cuticular proteins and the insoluble cuticlin from the predominant life-cycle stages occurring in man. SDS-PAGE analysis, before and after digestion with collagenase from Achromobacter iophagus, revealed that the polypeptide composition of the 2-mercaptoethanol-solubilised extracts from adult males and nodular microfilariae are quite distinct and that these extracts contained predominantly collagen-like proteins. Demonstrated by immunoblotting with a hyper immune patient serum pool (n = 107), five strongly reactive antigens with apparent molecular weights of 126, 68, 43, 37 and 33 kDa were detected in the extracts from adult males, while at least eight prominent and several weakly reactive components were detected in the extracts from nodular microfilariae. The overall amino acid composition of the cuticular extracts from the various stages demonstrates that: (a) the cuticle of the adult male stage is rich in glycine, pyrrolidone amino acids, and acidic amino acids or their amides, (b) eggshells are particularly poor in proline but rich in serine residues (14.5%), (c) nodular microfilariae cuticular extracts are poor in proline but rich in valine (9.0%) and lysine (7.3%) and (d) hydroxyproline and hydroxylysine are present in the cuticle of adults but absent in the juvenile life-cycle stages (nodular microfilariae and eggs). This study firstly, indicates that the composition of the cuticle of O. volvulus may thus, be quite distinct from one parasite stage to another and secondly, that the maturation of the parasite in the human host may be accompanied by the extensive hydroxylation of prolyl residues and to a lesser extent of lysyl residues in the predominantly collagen-like cuticular proteins.
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PMID:Evidence for increased hydroxylation of pyrrolidone amino acid residues in the cuticle of mature Onchocerca volvulus. 919 61

Our previous studies have shown that the degree of damage to a liposome corresponds to the variability of the animal species from which the serum comes, and that a complement activating factor (CAF) plays an important role in inducing the activation of the complement system, ultimately leading to the lysis of the liposomes. In this study, our attention focused on the characterization of the bovine serum factor (bCAF) that is involved in complement-mediated immune lysis of the liposome. The active fraction containing CAF partially purified with PEG and ammonium sulfate results in marked activation of the complement system via the alternative pathway when interacted with CAF-depleted serum, whereas the active fraction or CAF-depleted serum alone does not activate the complement. The interaction between lipopolysaccharide (LPS), heparin, zymosan or their mixture in place of CAF and CAF-depleted serum does not result in any significant activation of the complement system. Results from pretreatment with rabbit anti-bovine IgM IgG and rabbit anti-bovine IgG IgG indicate that activation of the complement system is not attributable to the antibody which is generally involved in activation of complement via the classical pathway. The results have further been proven by pretreatment with Concanavalin A (Con A) sepharose and protein G sepharose ruling out the possibility of antibody-mediated activation of complement. Our studies on collagenase and trypsin digestion demonstrate that the relative activity of CAF does not diminish with increase in collagenase concentration, and decreases with increase in trypsin concentration, strongly indicating that CAF does not have a collagen-like domain in its structure. The relative activity of CAF is dramatically inhibited after reduction with 2-mercaptoethanol (2-ME), clearly demonstrating that CAF is sensitive to reduction with 2-ME and confirming a sulhydryl-dependent protein. The optimal activity of CAF is observed in the range of 35-45 degrees C and its half-life at 37 degrees C is about 105 h. Furthermore, the relative activity of CAF increases and gradually approaches a plateau level with the increase of Mg2+ concentration. Obviously, complement activation induced by CAF depends on adequate Mg2+ concentration, confirming that this dependence is characteristic of the alternative pathway.
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PMID:Characterization of bovine serum factor triggering the lysis of liposomes via complement activation. 958 79

We determined the surface-associated proteolytic activity in three Entamoeba histolytica Schaudinn, 1903 strains (monoxenic HM1, axenic HM1, and HK9) of known virulence and its relationship with collagenase activity. Both activities were also determined in axenic HM1 amoebae trophozoites which were sensitive and resistant to complement-mediated lysis. Surface proteolytic activity was determined in glutaraldehyde-fixed E. histolytica trophozoites, which degraded the insoluble substrate, hide powder azure, and cleaved the human immunoglobulin G heavy chain in a time-dependent fashion, at neutral pH, in presence of 2-mercaptoethanol as cysteine protease activator. Surface proteolytic activity was strain dependent: monoxenic HM1 > axenic HM1 > axenic HK9. This activity correlated with collagenolytic activity (p < 0.05). Acquisition of resistance to complement-mediated lysis by axenic HM1 strain did not modify either surface proteases or collagenase expression. Our results suggest that this surface proteolytic activity could be used as an in vitro virulence marker for E. histolytica.
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PMID:Entamoeba histolytica: surface proteolytic activity and its relationship with in vitro virulence. 1055 49


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