Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Somatic cell and molecular genetics 12 (1986), S. 403-408 
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The low-molecular-weight human 2–5A synthetase gene has been assigned to chromosome 12 using rodent-human somatic cell hybrids and filter hybridization analysis of cell hybrid DNA. A cDNA probe representing almost all the coding sequences of the 2–5A synthetase gene hybridizes to four fragments of human DNA digested with the restriction enzyme EcoR1. By correlating the presence of these fragments in somatic cell hybrid DNA with the human chromosome content of the hybrids, the 2–5A synthetase gene can be mapped to chromosome 12. This contrasts with a previous assignment of this gene to chromosome 11 using an enzyme activity assay. The reason for this discrepancy remains unclear.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 38 (1988), S. 261-267 
    ISSN: 0730-2312
    Keywords: platelet extract ; PDGF ; chloramphenicol acetyl transferase ; gel retardation ; transfection ; induced expression ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We assayed fragments of the 5′ flanking sequence of the human 2-5A synthetase gene for their ability to respond to interferon-α (IFN) and platelet-derived growth factor (PDGF). Transient transfection assays identified a 40-base pair fragment, which, regardless of orientation, could confer IFN-inducibility on the thymidine kinase promoter. This same fragment was active in monkey and mouse cells and in the latter was responsive to PDGF. The effect of PDGF could be inhibited by anti-interferon antibodies. Gel retardation assays, using the 40-base pair probe, detected the presence of IFN-modulated DNA-binding factors in nuclear extracts from monkey cells. In mouse cells both IFN and PDGF induced the binding of nuclear factors to a synthetic 2-5A synthetase response sequence. Thus, both IFN and growth factors directly or indirectly modulate the binding of nuclear factors to the same region of the 2-5A synthetase gene.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We studied the effects of recombinant, interferon, 12-O-tetradecanoylphorbol13-acetate (TPA), and phorbol 12,13 dibutyrate (PDB) on surface immunoglobulin expression by Daudi cells. Incubation of cells with recombinant alpha2interferon (IFN-α2) caused a 2.5-fold (60%) decrease in slgM expression as measured by relative fluorescence index (RFI) using a flow cytometer. This decrease in slgM expression was independent of inhibitory effects on proliferation and cell cycle progression. TPA or PDB also caused a threefold (67%) decrease in slgM expression, while enhancing proliferation and cell cycle progression. Coincubation of cells with IFN-α2 or TPA decreased slgM expression by more than fourfold (〉75%), which was greater than the decrease induced by the optimal concentration of either agent alone. Molecular studies demonstrated that the treatment of cells with IFN-α2 or TPA decreased the steady-state levels of mRNA for the heavy chain of IgM (cμ), suggesting that down-regulation of slgM occurred at a pretranslational level. Activation of the cell membrane sodium/proton antiport did not play an integral role in the IFN-α2 or phorbol-ester-induced pathway of slgM down-regulation. Whereas IFN-α2 induced an increase in the activity of 2′,5′-oligoadenylate (2-5A) synthetase, the addition of TPA to IFN-α2 caused a significant decrease in the activity of this enzyme. Although IFN-α2 and TPA exhibited additive effects on slgM expression, they had opposing effects on cell proliferation, cell cycle progression, and induction of 2-5A synthetase activity, suggesting that these agents down-regulate slgM expression through independent pathways.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...