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H Ceri

Publications and source records attributed to H Ceri.

50 records · Page 3Linked to original sources
PubMed1983

Interaction of a rat lung lectin with the exopolysaccharides of Pseudomonas aeruginosa.

The specific interaction between the exopolysaccharide purified from a number of Pseudomonas aeruginosa isolates from cystic fibrosis patients and a rat lung heparin-lectin was assayed. The polysaccharide prepared from Homma serotypes M, B, I, and G did not act as hapten inhibitors of lectin activity, whereas the polymers prepared from ca. 80% of strains that did not type with Homma serum did act as hapten inhibitors. Inhibition was shown not to be due to lipopolysaccharide. The infrared spectrums of both inhibitory and noninhibitory polymers appeared very similar, although small amounts of glucose and an unidentified amino sugar were found only in the nontypable strains. This evidence suggests that rat lung lectin recognizes and distinguishes a specific type of alginate-like polymer prevalent on the Homma nontypable P. aeruginosa.

Animals↗
PubMed1981

Heparin-inhibitable lectin. Purification from chicken liver and embryonic chicken muscle.

The heparin-inhibitable lectin activity from adult chicken liver and embryonic chick pectoral muscle has been purified by gel filtration on Sepharose CL-2B followed by affinity chromatography on heparin-Sepharose. Specific activity of this abundant material was increased about 70-fold with about 28% recovery of activity. The purified lectin, which behaved as a large aggregate, could be dissociated into two proteins with apparent molecular weights of 13,000 and 16,000 upon electrophoresis in sodium dodecyl sulfate. 125I-tryptic peptide maps of these proteins showed that they were distinct from each other and also from lectins of similar molecular weight previously purified from chicken. Agglutination activity of the lectin, tested with specially prepared rabbit erythrocytes, was very sensitive to heparin which inhibited 50% at concentrations of approximately 10(-5) mM. Dermatan sulfate and heparan sulfate were also potent inhibitors, whereas other glycosaminoglycans were not. The most potent monosaccharide hapten inhibitor was N-acetyl-D-galactosamine. Because of its properties, we operationally refer to this material as chicken heparin-lectin, recognizing that this does not necessarily indicate that it functionally interacts with heparin in vivo.

Animals↗
PubMed1981

Heparin-inhibitable lectins: marked similarities in chicken and rat.

Extracts of young rat lung contain a heparin-inhibitable lectin that closely resembles one recently purified from chicken liver. Both lectins interact with heparin and N-acetyl-D-galactosamine, and were purified by gel filtration on Sepharose CL-2B followed by affinity chromatography on heparin-Sepharose. They both behave as high molecular weight aggregates that can be dissociated into two peptides with apparent molecular weights of 13,000 and 16,000 by gel electrophoresis in SDS. Samples of purified lectin contained up to 20% DNA by weight, and the degree of lectin aggregation and hemagglutination activity was greatly reduced by treatment with micrococcal nuclease without inhibiting heparin-binding activity. Association of lectin with DNA is an artifact of homogenization in high salt, since only 2% of the lectin is found associated with a purified nuclear fraction.

Animals↗
PubMed1979

Extracellular lectin and its glycosaminoglycan inhibitor in chick muscle cultures.

Embryonic chick muscle contains two developmentally regulated lectins, which may be involved in cell interactions. These endogenous lectins are assayed as agglutinins of appropriate test erythrocytes. One of these, called lectin-2, interacts with specific glycosaminoglycans, especially heparin and dermatan sulfate. Lectin-2 is present at constant levels in both chick fibroblast and chick muscle cells throughout 14 days of culture but is released into the medium of cultured embryonic muscle after 7-8 days of culture, soon after myoblast fusion. Lectin-2 interacts strongly with a component of substrate-attached material in embryonic muscle cultures which is extractable from the cutlure dishes with alkali after the cells have been removed with ethylediaminetetraacetic acid. The active component in the substrate-attached material appears to be a glycosaminoglycan that is a more potent inhibitor of lectin-2 agglutination activity than any of the known glycosaminoglycans that we have tested. The active material is degraded by chondroitinase ABC but not by chondrotinase AC, hyaluronidase, or proteolytic enzymes and thus appears to be similar to dermatan sulfate. The results of these studies raise the possibility that lectin-2 functions by interacting with glycosaminoglycans, either associated with the cell surface or with the extracellular matrix.

Animals↗
PubMed1977

Pretreatment of hamster cells with phenethyl alcohol alters cell surface glycoproteins and inhibits vesicular stomatitis virus growth.

Chinese hamster ovary cells cultured in the presence of phenethyl alcohol exhibit obvious changes in cell surface galactose and galactosamine glycoproteins as determined by the galactose-oxidase[3H]borohydride technique and SDS gel electrophoresis. Cells pretreated with phenethyl alcohol (drug was removed before infection) were not as effective as hosts for vesicular stomatitis virus as untreated cultures. A minimum pretreatment time with 0.1% phenethyl alcohol of about 8 h was required before a reduction in virus growth was observed. It is proposed that phenethyl alcohol pretreatment as outlined in this report leads to a modification of the host cellular membrane resulting in the inhibition of virus replication.

Cell Line↗