Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Materials released into culture medium by transformed and untransformed baby hamster kidney cells labelled with glucosamine, sulfate, fucose or leucine were characterized. Some of the components could also be labelled by iodination of intact cells, indicating their surface origin. Analysis on gradient polyacrylamide sodium lauryl sulfate gels demonstrated that a group of high apparent molecular weight glucosamine-labelled components were more abundant in materials released from Rous sarcoma virus-transformed baby hamster kidney cells than from baby hamster kidney cells or polyoma virus-transformed baby hamster kidney cells. The relative rates of release of glucosamine-labelled components from transformed and untransformed cells were similar except that the transformed baby hamster kidney cells released some large molecular weight components slightly more rapidly than baby hamster kidney cells. Treatment of labelled medium materials with testicular hyaluronidase removed much glucosamine label from the materials but did not affect the amounts of other labels. After treatment with hyaluronidase, the patterns of labelled conditioned media from both transformed and untransformed baby hamster kidney cells were qualitatively and quantitatively very similar, suggesting that the differences seen in untreated labelled conditioned media were due to the presence of hyaluronidase-sensitive materials associated with medium materials rather than to actual differences in glycoproteins.
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PMID:Materials released into culture medium by normal and oncogenic virus-transformed mammalian cells. 18 66

A major cell surface protein, CSP, of chick embryo fibroblasts has been shown to constitute up to 3% of total cell protein, and to be decreased after viral transformation. Its role in normal cell behavior is not known. We have isolated CSP from chick embryo fibroblasts by extraction with 1 M urea and find that these preparations of CSP agglutinate formalinized sheep erythrocytes at protein concentrations of under 2 mug/ml. In extracts of chick embryo cells, the quantity of such hemagglutinating activity parallels that of CSP determined by electrophoresis, and both are substantially decreased in chick cells transformed by the Bryan hightiter strain of Rous sarcoma virus. Both CSP and hemagglutinating activity are progressively adsorbed onto erythrocytes and can be released by 1 M urea. An antiserum to purified CSP specifically blocks the agglutination. The agglutinating activity is destroyed by boiling or treatment with proteases. The agglutination reaction is inhibited by the chelating agents EDTA and EGTA [ethyleneglycol-bis(beta-aminoethyl ether)N,N'-tetraacetic acid]. Agglutination is also inhibited to a lesser degres by amino sugars and other amines, increased osmolarity, and urea. Other monosaccharides, hyaluronidase, DNase, and RNase have little or not effect on the agglutination reaction. This demonstration that CSP has an agglutinating activity that is sensitive to proteases and that requires divalent cations suggests that this molecule may play a role in cell adhesion.
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PMID:The major cell surface glycoprotein of chick embryo fibroblasts is an agglutinin. 105 2

Chondrogenesis, the differentiation of mesenchyme into cartilage, results in a change in composition of the extracellular matrix. The cartilage matrix contains several unique components, including type II collagen and chondroitin sulfate proteoglycan; it also contains fibronectin, a glycoprotein that mediates the interaction of cells with their matrix. We show that chick cartilage fibronectin mRNA contains an unusual pattern of alternatively spliced exons. Specifically, it contains exon IIIB but does not contain exon IIIA whereas fibronectin mRNA from mesenchyme contains both exons IIIB and IIIA. Thus the splicing pattern of the fibronectin mRNA must change from B+A+ to B+A- during chondrogenesis. Most fibronectin mRNA in other mesenchymal tissues contains exon IIIA but little exon IIIB (B-A+). Culturing of chondrocytes (cartilage-producing cells) results in loss of exon IIIB from fibronectin mRNA (B-A-). Manipulation of culture conditions to produce more adhesive chondrocytes (treatment with hyaluronidase, transformation with Rous sarcoma virus, and treatment with retinoic acid) increases the amount of fibronectin mRNA containing exon IIIA. These results suggest that exon IIIB may mediate the interactions of chondrocytes with the unique components of the cartilage matrix and exon IIIA may play a role in chondrocyte adhesion.
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PMID:The splicing pattern of fibronectin mRNA changes during chondrogenesis resulting in an unusual form of the mRNA in cartilage. 200 28

When stained with ruthenium red (RR), chick embryo cells infected with various strains of Rous sarcoma virus (RSV) and with avian leukosis viruses RAV-1 and RAV-3 showed an increase in the layer of acid mucopolysaccharides (AMPS) at their surfaces as compared with uninfected cells. This increase was most prominent in cells infected with the Fujinami strain of RSV. The layer was resistant to digestion with neuraminidase or trypsin but was readily removed by exposure to hyaluronidase. The thickness of this AMPS layer was not correlated with the varying degree of loss of contact inhibition exhibited by cells infected with the different strains of virus. The staining of the cell envelope with a solution of phosphotungstic and chromic acids (PTA-CR) suggested the presence of glycoproteins. The outer surface of the virions showed the same staining as the cell surface with RR and PTA-CR, and the budding virus particle was seen to incorporate the RR layer of the cell into its structure. The RR layers of cells and virions appeared to fuse, as did those between virus particles, suggesting that these layers play a role in the aggregation of virus particles and in their adherence to the surface of the cell.
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PMID:Ultrastructure of the surfaces of cells infected with avian leukosis-sarcoma viruses. 417 56

Hyaluronate is associated with the cell surface of cultured Rous sarcoma virus-transformed chondrocytes. Detachment of these cells from their substratum by a variety of reagents is accompanied by release of 75-100% of this hyaluronate into solution. Treatment of the cells with 200 U/ml protease-free Streptomyces hyaluronidase at 37 degrees C cause release of greater than 90% of the cell surface hyaluronate and complete cell detachment. Treatment with a lower concentration of Streptomyces hyaluronidase (30 U/ml) at 25 degrees C or a corresponding activity of testicular hyaluronidase gives similar results, but only in the presence of mM EGTA. Treatment with the lower activities of either hyaluronidase or with 1 mM EGTA alone release only approximately 45% of the cell surface hyaluronate and does not cause significant cell detachment. It is concluded that there are two populations of cell surface hyaluronate differing in their accessibility or their resistance to dissociation from other components of the cell surface. It is proposed that the less readily released fraction is located between the transformed chondrocyte surface and substratum and is necessary for their interaction.
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PMID:Cell-substratum attachment and cell surface hyaluronate of Rous sarcoma virus-transformed chondrocytes. 624 21

Rat-1 fibroblasts infected with the temperature-sensitive transformation mutant LA 24 of Rous sarcoma virus have a high rate of divalent cation-independent homotypic cell aggregation when grown at the permissive temperature, 34 degrees. Cells grown at the nonpermissive temperature, 39 degrees, have a low rate of homotypic cell aggregation. Hyaluronic acid is involved in the homotypic aggregation of permissively grown cells since aggregation is blocked by either treatment of the cells with hyaluronidase or the presence of exogenously added hyaluronic acid. Despite their low rate of homotypic aggregation, nonpermissively grown cell are capable of heterotypically adhering to premissively grown cells. The formation of heterotypic aggregates is blocked by treatment of the nonpermissively grown cells with hyaluronidase but not by treatment of permissively grown cells with hyaluronidase. These results provide evidence that the divalent cation-independent aggregation of Rat-1 LA 24 cells is mediated by interactions between hyaluronic acid and other adhesive components on the cell surface.
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PMID:Divalent cation-independent aggregation of rat-1 fibroblasts infected with a temperature-sensitive mutant of Rous sarcoma virus. 627 88

Normal and transformed fibroblasts can be discriminated by a flow cytometry assay on the basis of their differential reaction with fluorescamine. The cause of altered reactivity of transformed cells with this fluorescent probe has been investigated by a detailed analysis of its reaction with chicken embryo fibroblasts transformed by a temperature sensitive mutant of Rous sarcoma virus. The subcellular distribution of fluorescent adducts characterized by cell fractionation and gel electrophoresis procedures supports the hypothesis that transformed cells possess a surface barrier which decreases the accessibility of fluorescamine to reactive macromolecules. The barrier has been identified as being composed at least partly of hyaluronic acid, because of the ability of purified and specific hyaluronidase (from Streptomyces hyalurolyticus) to modulate the response of transformed cells to fluorescamine. Enzyme treatment of transformed cells prior to reaction with fluorescamine causes them to resemble nontransformed cells both in the nature of components labeled and in their fluorescence intensity. It is suggested that fluorescamine monitors an altered surface hyaluronic acid composition which occurs upon transformation. Its significance is discussed in terms of the known physical properties of the molecule and the finding that it is an early event in the process of transformation.
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PMID:Detection of transformed cells using a fluorescent probe: the molecular basis for the differential reaction of fluorescamine with normal and transformed cells. 629 84

This paper presents the partial characterization and the identification of an 80-kDa protein detected in bull spermatozoa using a monoclonal antibody directed against a 16-amino acid long peptide from the N-terminal domain of the protooncogene p60(src) from the Rous Sarcoma Virus When subjected to two-dimensional electrophoresis, this 80-kDa protein migrated as several isoforms, with an isoelectric point ranging from 7.4 to 8.2. Amino acid sequence analysis of a peptide obtained following trypsin digestion of the bull sperm protein showed homology to the PH-20/hyaluronidase precursor sperm protein. As for PH-20, this bull sperm 80-kDa protein is located at the plasma membrane surface in the postacrosomal region of the head. An increased immunolabeling in the anterior head region of fixed/permeabilized spermatozoa was observed when these cells were incubated under capacitating conditions, whereas most sperm cells challenged with the calcium ionophore A23187 to acrosome react lost their labeling almost completely. As for the PH-20 protein, the 80-kDa bull sperm protein possesses a hyaluronidase activity that is higher at pH 7.0 than at pH 4.0 in an in-gel assay. Unlike what has been observed in the guinea pig, mouse, and human PH-20, this 80-kDa protein was not released from the surface of bull spermatozoa by treatment with phosphatidylinositol-specific phospholipase C or with trypsin. However, this protein was not sedimented by a 100,000 x g centrifugation after nitrogen cavitation, which suggests that the 80-kDa protein is loosely attached to the sperm membrane by a yet-unknown mechanism. These results suggest that the 80-kDa bull sperm protein shares many homologies with the sperm PH-20 protein reported in the literature and, most likely, is the bull sperm homologue of the PH-20.
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PMID:Characterization of an 80-kilodalton bull sperm protein identified as PH-20. 1146 35