Literature DB >> 3036074

Sendai-viral HN and F glycoproteins as probes of plasma-membrane protein catabolism in HTC cells. Studies with fusogenic reconstituted Sendai-viral envelopes.

R T Earl, E E Billett, I M Hunneyball, R J Mayer.   

Abstract

Reconstituted Sendai-viral envelopes (RSVE) were produced by the method of Vainstein, Hershkovitz, Israel & Loyter [(1984) Biochim. Biophys. Acta 773, 181-188]. RSVE are fusogenic unilamellar vesicles containing two transmembrane glycoproteins: the HN (haemagglutinin-neuraminidase) protein and the F (fusion) factor. The fate of the viral proteins after fusion-mediated transplantation of RSVE into hepatoma (HTC) cell plasma membranes was studied to probe plasma-membrane protein degradation. Both protein species are degraded at similar, relatively slow, rates (t1/2 = 67 h) in HTC cells fused with RSVE in suspension. Even slower degradation rates for HN and F proteins (t1/2 = 93 h) were measured when RSVE were fused with HTC cells in monolayer. Lysosomal degradation of the transplanted viral proteins is strongly implicated by the finding that degradation of HN and F proteins is sensitive to inhibition by 10 mM-NH4Cl (81%) and by 50 micrograms of leupeptin/ml (70%).

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Year:  1987        PMID: 3036074      PMCID: PMC1147633          DOI: 10.1042/bj2410801

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  30 in total

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  3 in total

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Journal:  Biochem J       Date:  1987-02-01       Impact factor: 3.857

2.  Mechanisms of intracellular protein catabolism. Intracellular fate of microinjected polypeptides translated in vitro.

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3.  A putative protein-sequestration site involving intermediate filaments for protein degradation by autophagy. Studies with transplanted Sendai-viral envelope proteins in HTC cells.

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  3 in total

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