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Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+.

Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+. Research Abstract Details 

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  • Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+. Abstract Text:

    a onoA Ono,m kawakitaM Kawakita,

    The effects of thapsigargin (Tg), a specific inhibitor of Ca(2+)-ATPase of the endoplasmic reticulum (ER), on replication of Sendai virus (HVJ) in BALB3T3 cells were examined. In the presence of Tg, the cells infected with HVJ did not release viral particles to the culture medium. Tg inhibited almost completely the expression of viral envelope proteins, HN and F0, on the cell surface, although it did not affect the synthesis of viral proteins. Two other inhibitors of Ca(2+)-ATPase of the ER, 2,5-di(tert-butyl)-1,4-benzohydroquinone (BHQ) and cyclopiazonic acid (CPA), as well as Ca(2+)-ionophores such as A23187 and ionomycin, also inhibited the expression of HN protein on the cell surface. Tg seemed to inhibit the intracellular transport or maturation of the viral membrane proteins by perturbing intracellular distribution of Ca2+ ions. In the presence of Tg, HN protein remained sensitive to endoglycosidaseH (endoH) for 3 h after its synthesis. On the other hand, F0 protein became resistant to endoH and sensitive to neuraminidase even in the presence of Tg. These results indicate that the transport of HN protein is blocked at the ER or the cis-Golgi region, while that of F0 protein is blocked at the post-Golgi stage in the presence of Tg.

    Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+. Publishing Authors By Initials

    a onoA Ono,m kawakitaM Kawakita,

    For similar biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus replication research abstracts see: biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus replication research

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    Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 116

    Page Numbers: 649-56

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Sep

    YEAR: 1994

    Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+. Keywords Mesh Terms:

    KEYWORDS: Virus Replication

    MESH TERMS: drug effects

    Chemical & Substance for Abstract: Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+. Information

    Substance Name: Calcium-Transporting ATPases

    Registry Number: EC 3.6.1.8

    Grant and Affiliation Information for Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+.

    AFFILIATION: Department of Physiological Chemistry, Tokyo Metropolitan Institute of Medical Science.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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    Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+ Related Publications

     

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