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)

Polycationic labels such as cationized ferritin and colloidal iron were used to evaluate the surface negative charges over the mandibular condyles of ICR mice. The effects of neuraminidase, hyaluronidase, pronase, and collagenase on the binding of cationized ferritin and colloidal iron particles to the condylar articular surface were also studied. The results of this study clearly indicate that the surface area of the cartilaginous condyle is negatively charged and that its composition consists mainly of a collagenous material embedded within a proteinaceous matrix. With age, a substantial decrease in the density of negative charges took place along the surface area and, in particular, in the context of sialic acid residues. It is, therefore, possible that the reduction in cartilage surface charge might be associated with the onset of osteoarthritic changes commonly seen in aging humans and experimental animals.
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PMID:Cartilage surface charge. A possible determinant in aging and osteoarthritic processes. 298 74

The importance of the glycocalyx in controlling responses to proteinases was studied by enzymic removal of sialic acids from the luminal surface of arterial endothelium. In the perfused rat aorta collagenase induced cell detachment in greater numbers from the desialylated than from the untreated endothelium. Neuraminidase treatment increased by three-fold prostacyclin synthesis by the vessel wall in response to thrombin. The supernatant from activated human neutrophils, containing elastolytic activity, when perfused together with neuraminidase enhanced and prolonged sialic acid release induced by neuraminidase alone. Thus the effects of different proteinases on various endothelial cell functions are potentiated by removal of surface sialic acid residues.
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PMID:Sialic acid moieties on surface glycoproteins protect endothelial cells from proteolytic damage. 299 70

A procedure for purification of surfactant-associated glycoproteins A from canine surfactant was established utilizing preparative isoelectric focusing as a major purification step in absence of detergents. The proteins migrated as charge trains, isoelectric points 4.2-5.0. Unglycosylated forms of surfactant-associated protein A1 (26 kDa) and glycoproteins A2 and A3 (32-36 kDa) were identified by silver-staining and immunoblot analysis. These forms were demonstrated to be identical polypeptides by fingerprint analysis of 125I-labeled peptides generated by tryptic-chymotryptic digests of the iodinated proteins. Size and charge heterogeneity were related to varying amounts of N-linked complex carbohydrates, including sialic acid, which were sensitive to endoglycosidase F and neuraminidase but resistant to endoglycosidase H. A collagenase-sensitive region was demonstrated which was required for sulfhydryl-dependent oligomerization of the molecule. Collagenase treatment resulted in removal of approx. 10 kDa from the glycoprotein molecule. Collagenase-resistant fragments of 21-23 kDa migrated with carbohydrate-dependent size and charge heterogeneity and were reduced to 16 kDa by endoglycosidase F. Amino acid composition of the surfactant glycoproteins demonstrated high glycine content which was diminished after digestion with collagenase. Several glycine-rich tryptic peptides were isolated by reverse-phase chromatography. Partial sequence information shows Gly-X-Y repeat sequences containing hydroxyproline residues. The major canine surfactant-associated proteins, glycoproteins A contain complex-type N-linked carbohydrate. In addition, a separate collagen-like peptide domain is present and is required for sulfhydryl-dependent oligomerization.
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PMID:Purification of canine surfactant-associated glycoproteins A. Identification of a collagenase-resistant domain. 300 81

Immunocytochemical staining of tissues with the mouse macrophage-specific monoclonal antibody, F4/80, has shown that large numbers of stromal macrophages are present in adult and foetal haematopoietic tissues. Macrophage plasma membrane processes are seen to establish extensive associations with myeloid and erythroid cells in adult bone marrow and with developing erythroblasts in foetal liver, suggestive of local trophic interactions. To explore the nature of these interactions, methods were developed for isolation of resident bone marrow macrophages (RBMM) and foetal liver macrophages (FLM). Following collagenase digestion of bone marrow or foetal liver, clusters were obtained which were composed of one or more central macrophages surrounded by proliferating haematopoietic cells. After attachment of clusters to glass coverslips, adherent macrophages could be stripped free of haematopoietic cells by pipetting in the absence of divalent cations. The purified RBMM, but not FLM, expressed a novel haemagglutinin, which mediated binding, without ingestion, of large numbers of unopsonized sheep erythrocytes by a divalent cation-independent mechanism. In view of the possibility that this sheep erythrocyte receptor (SER) could interact with a homologous ligand on mouse bone marrow cells, its properties were examined. SER was found to be a lectin-like protein which recognized protease-resistant sialylated glycoconjugates on sheep erythrocytes. The expression of SER was restricted to certain stromal tissue macrophages and was low or absent on monocytes and macrophages obtained from serous cavities. High levels of SER could be induced on elicited peritoneal macrophages by cultivation in mouse serum and the induced receptor was found to mediate low-avidity binding of murine bone marrow cells with characteristics indistinguishable from those seen for binding of sheep erythrocytes. However, maximal binding of bone marrow cells to RBMM depended on a distinct, divalent cation-dependent adhesion system. Using erythroblasts as a ligand, FLM were selected to explore the properties and expression of this adhesion receptor, the erythroblast receptor (EbR). Similar to SER, EbR did not mediate ingestion, and was restricted in its expression to foetal and adult stromal tissue macrophages. Unlike SER, EbR activity was not affected by neuraminidase treatment of the ligand and the receptor was not induced on peritoneal macrophages cultured in mouse serum. EbR appears to be a novel cell adhesion receptor because it was unaffected by inhibitors of several previously described cell adhesion molecules, including the fibronectin receptor. Future studies will attempt to explore the f
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PMID:Novel cell surface adhesion receptors involved in interactions between stromal macrophages and haematopoietic cells. 307 37

Preterm delivery remains a preeminent problem in reproductive and pediatric care worldwide. Recent data suggest that cervicovaginal microflora and/or the inflammatory response they engender produce factors which can cause or predispose to preterm labor and rupture of membranes. Microorganisms mediating such processes may not be "recognized pathogens" and are often considered normal flora. These microorganisms may act singly, additively, or synergistically with host factors released during an induced inflammatory response. Quantitative, as well as qualitative aspects of cervicovaginal microflora may be important. Multiple cervicovaginal microorganisms produce IgA protease, neuraminidase, and mucinase which may facilitate passage of these and other agents past cervical barriers and into the lower uterine segment. Multiple microflora also produce phospholipases A2 and C, each of which can locally augment production of eicosanoids within the uterus which are important in cervical ripening and labor. Similar microflora produce various proteases, including collagenase, which can focally weaken the amniochorion and predispose to premature rupture of membranes and cervical ripening. Intrauterine microorganisms induce inflammatory reaction and may engender local release of similar proteases, phospholipases, as well as platelet-activating factor (PAF) and lymphokines which can also initiate or further potentiate labor-inducing mechanisms. Recognition of microbe-induced pathogenesis of some cases of preterm birth offers the hope of specific treatment and prophylaxis. In recent studies, administration of erythromycin and tocolytic agents was associated with an improved outcome in selected women with preterm labor. Further microbiological and clinical studies are ongoing. "Just why so many gravidas go into labor prematurely and hence give birth to infants who often are unable to cope with extrauterine conditions is one of the great unsolved problems of obstetrics."
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PMID:Prevention of preterm birth: new initiatives based on microbial-host interactions. 327 1

X-ray-induced, lymphoblastic, T-cell lymphoma/leukemias from irradiated RF mice were observed to uniformly expressed a 44-kd oncofetal antigen (OFA). The OFA polypeptide was detected by flow cytometry, affinity column SDS-PAGE analysis, and immunoblotting with monoclonal antibody (MAb) 115 prepared against syngeneic mouse fetus. X-ray and ultraviolet (UV) induced murine fibrosarcoma cell lines, used as classic models in radiation biology, were also found to express the OFA, which suggested that the 44-kd OFA was a general transformation marker of tumors. Adult mouse thymocytes and other adult tissues expressed no OFA. The 44-kd polypeptide was located at the surface membrane of the tumors examined. In contrast to other reports, lymphoblastic lymphoma cell lines expressed the OFA as a cross-protective, rather than an individually-specific, tumor-associated transplantation antigen. Pronase treatment removed OFA from the surface of living lymphoma cells, whereas collagenase, neuraminidase, and hyaluronidase did not. The OFA was rapidly reexpressed upon culture of the pronase-treated cells. Taken together, these results suggest that the 44-kd OFA polypeptide described here may provide a useful cell surface marker for future radiation carcinogenesis studies. MAb 115 is a promising reagent for detecting tumor-associated 44-kd OFA, for assessing immunoregulatory perturbations to the OFA caused by radiation damage and for investigating the immunopathology of OFA-associated radiation damage.
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PMID:Radiation-induced lymphoblastic lymphomas/leukemias and sarcomas of mice express conserved, immunogenic 44-kilodalton oncofetal antigen. 333 9

A single i.v. injection of a mAb 5-1-6 to rats was found to cause massive though transient proteinuria. This mAb 5-1-6, IgG1 was produced by immunization of BALB/c mice with collagenase-treated Wistar rat glomeruli and was highly organ and species specific. Immunoelectron microscopy using immunoperoxidase with the avidin-biotin complex and immunogold staining indicated mAb 5-1-6 to bind in vitro to the surface of glomerular epithelial foot processes, mainly to slit diaphragms. The recognized antigenic molecule was not susceptible to neuraminidase treatment and its Mr was about 51 kDa by immunoprecipitation. A one-shot i.v. injection of this mAb induced proteinuria in rats starting immediately, reaching the peak on day 8 (mean value of 150 mg/24 h), then gradually decreasing to normal level on day 18. The in vivo localization of administrated mAb 5-1-6 changed with time. Linear binding along glomerular capillary walls was observed 2 h after injection. However, 3 days later, it partially shifted to a fine granular pattern. The linear pattern disappeared and the size as well as intensity of the fluorescent granules decreased on day 12 to trace positive on day 18. Immunoelectron microscopy revealed the binding pattern of in vivo injected mAb 5-1-6 after 2 h to be similar to that in vitro. Three days later, injected mAb was observed within multivesicular bodies in glomerular epithelial cells as well as along the surface of foot processes and around slit diaphragms. Twelve days after injection, mAb along the surface of the foot processes and around slit diaphragms decreased but those in multivesicular bodies were observed more frequently. Rat IgG and C3 could not be detected throughout the period of observation. No histologic abnormalities were noted except for partial retraction of epithelial foot processes at the peak of proteinuria on day 8. This mAb thus provides a valuable means for examining the mechanism of proteinuria.
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PMID:Massive proteinuria induced in rats by a single intravenous injection of a monoclonal antibody. 339 34

The effects of a range of commercially available proteases and glycosidases on blastocyst development and hatching were examined on rabbit embryos cultured from the morula stage in a defined medium supplemented with charcoal-treated bovine serum albumin. The proteases tested were trypsin, alpha-chymotrypsin, thrombin, elastase, plasmin, papain, clostripain, collagenase, Streptomyces griseus protease and cathepsin C. The glycosidases tested were neuraminidase, alpha-mannosidase, beta-galactosidase and hyaluronidase. None of these enzymes appeared to stimulate blastocyst growth. The only enzymes which digested the embryonic investments, the zona and mucin coat, sufficiently to cause complete blastocyst hatching were trypsin and Streptomyces griseus protease at relatively low concentrations (250 ng/ml) and chymotrypsin and elastase at higher concentrations.
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PMID:A survey of the effects of proteases and glycosidases on culture of rabbit morulae to blastocysts. 353 6

The adhesion of Erysipelothrix rhusiopathiae (E. rhusiopathiae) to the cultured confluent monolayer of rat aortic endothelial cells (EC) and the role of neuraminidase in the interaction between EC and E. rhusiopathiae were examined. One EC line was obtained by collagenase treatment of rat aorta. The EC showed a typical cobblestone appearance and possessed the factor VIII related antigen. When cultured more than two weeks after reaching confluence, the EC formed a vascular plexus-like appearance. E. rhusiopathiae began to adhere to EC within 2 minutes after the beginning of culture and adhered at a constant rate for 20 minutes. The adhesion of bacteria to EC was closely related to the release of sialic acid from the EC. Significantly more bacteria adhered to neuraminidase treated EC, and bacterial adhesion was inhibited dose-dependently by N-acetylneuraminic-lactose, which is the substrate of bacterial neuraminidase. It is concluded that bacterial neuraminidase plays an essential role in initiating the interaction between EC and E. rhusiopathiae, which would contribute to the genesis of arteritis.
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PMID:Adhesion of Erysipelothrix rhusiopathiae to cultured rat aortic endothelial cells. Role of bacterial neuraminidase in the induction of arteritis. 360 4

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


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