mannoside/sarcoma

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Cyclic AMP-induced morphological transformation of cells infected by temperature-sensitive mouse sarcoma virus. Expression of transformation-associated markers.

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Normal rat kidney (NRK) cells infected with a temperature-sensitive (ts) mutant of mouse sarcoma virus (NRK [MSV-1b]) express the transformed phenotype when grown under permissive conditions, but acquire the normal phenotype when grown under restrictive conditions. Addition of 3', 5' cyclic

Comparison of N-acetylglucosaminyltransferase V activities in Rous sarcoma-transformed baby hamster kidney (RS-BHK) and BHK cells.

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Recent studies have demonstrated that Rous sarcoma virus-transformed baby hamster kidney (RS-BHK) cells express twofold higher levels of those N-linked oligosaccharides that contain the sequence [GlcNAc-beta(1,6)Man (1,6)] compared to nontransformed parental BHK cells (Pierce and Arango, J.

Lectin affinity chromatography of Sindbis and Rous sarcoma virus glycopeptides and oligosaccharides.

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Glycopeptides and endogly cosidase-digested oligosaccharides from [3H]mannose-labeled Rous sarcoma virus and Sinbis virus have been fractionated by lentil lectin-Sepharose and concanavalin A-agarose affinity chromatography and subsequently analyzed by BioGel P-4 gel filtration. Only a specific

Basement membrane carbohydrate as a target for bacterial adhesion: binding of type I fimbriae of Salmonella enterica and Escherichia coli to laminin.

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Adherence of type-1-fimbriate Salmonella enterica and Escherichia coli to immobilized proteins of the extracellular matrix and reconstituted basement membranes was studied. The type-1-fimbriate strain SH401 of S. enterica serovar Enteritidis showed good adherence to laminin, whereas the adherence to

An enzyme-linked immunosorbent assay for N-acetylglucosaminyltransferase-V.

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The development of an enzyme-linked immunosorbent assay (ELISA) for uridine 5'-diphospho-N-acetyl-glucosamine: alpha mannoside beta 1----6 N-acetylglucosaminyltransferase (GnT-V) is reported. The assay quantitates the enzymatic conversion of the specific synthetic GnT-V acceptor GlcNAc beta

Lectin potentiation of BCG-contact-mediated antitumor action.

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Concanavalin A (Con A) potentiated the BCG-contact-mediated antitumor action when both Con A (10 microgram) and BCG (50 micrograms) were injected with fibrosarcoma cells (5 x 10(4)) into inbred Swiss mice. BCG (50 micrograms) alone had no antitumor effect. The Con A-potentiated BCG-contact-mediated

Regulation of glycosylation. The influence of protein structure on N-linked oligosaccharide processing.

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The Sindbis virus glycoproteins, E1 and E2, comprise a useful model system for evaluating the effects of local protein structure on the processing of N-linked oligosaccharides by Golgi enzymes. The conversion of oligomannose to N-acetyllactosamine (complex) oligosaccharides is hindered to different

Differential effects of oncogenic transformation on N-linked oligosaccharide processing at individual glycosylation sites of viral glycoproteins.

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Hamster sarcoma virus (HSV) transformation of Nil-8 fibroblasts is associated with an increase in the average size of N-acetyllactosamine (complex) type N-linked glycans due to an increase in both the average number of branches/chain and in the fraction of N-linked glycans containing

Reactivity of avian RNA tumor viruses with lectins.

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The infectivity of avian RNA tumor viruses was inactivated to varying degrees by treatment with either concanavalin A (Con A) or phytohemagglutinin but not by treatment with wheat germ agglutinin. In general, leukosis viruses reacted preferentially with Con A, whereas sarcoma viruses showed more

Liver membrane proteome glycosylation changes in mice bearing an extra-hepatic tumor.

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Cancer is well known to be associated with alterations in membrane protein glycosylation (Bird, N. C., Mangnall, D., and Majeed, A. W. (2006) Biology of colorectal liver metastases: A review. J. Surg. Oncol. 94, 68-80; Dimitroff, C. J., Pera, P., Dall'Olio, F., Matta, K. L., Chandrasekaran, E. V.,

[Induction of tumor necrosis factor alpha by Mycoplasma penetrans isolated from patients with AIDS].

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The activity of induce tumor necrosis factor alpha (TNF alpha) production of several mycoplasmas, including AIDS associated mycoplasmas was investigated. M. penetrans which was detected and isolated from urine and tissue of Kaposi's sarcoma of patients with AIDS markedly exhibited the induction of

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