2′‐Phosphodiesterase Activity in Human Cell Lines Treated or Untreated with Human Interferon

Verhaegen-Lewalle, M.

doi:10.1111/j.1432-1033.1982.tb06828.x

Cited by 15 publications

(5 citation statements)

References 34 publications

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“…The core molecules could be merely end-products devoid of activity. However, there is no evidence for such a specific phosphatase, whereas the pathway involving a 2'-phosphodiesterase seems well documented (22,23,29). An independent origin for the core molecules would imply a 2-5A synthetase working differently from that already described.…”

Section: Resultsmentioning

confidence: 99%

Immunological evidence for the in vivo occurrence of (2'-5')adenylyladenosine oligonucleotides in eukaryotes and prokaryotes.

Laurence¹,

Marti²,

Roux³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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A monoclonal antibody highly specific for (2'-5')adenylyladenosine oligonucleotides was used together with a 125I-labeled analog of this compound to detect and quantify phosphorylated and nonphosphorylated (2'-5')adenylyladenosine oligonucleotides in a variety of tissues and cells. These oligonucleotides were first assayed as a whole in perchloric acid extracts and then further individually characterized by HPLC analysis. Their sensitivity to alkaline phosphatase, snake venon phosphodiesterase, and T2 RNase was systematically checked.

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Section: Resultsmentioning

confidence: 99%

Immunological evidence for the in vivo occurrence of (2'-5')adenylyladenosine oligonucleotides in eukaryotes and prokaryotes.

Laurence¹,

Marti²,

Roux³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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“…However, such procedures did not permit quantitative assessment of the structural requirements of the 2-5A analogs for RNase L activation, i.e. because of the membrane damage ensuing from these procedures as well as the low stability of 2-5A itself [8,30-321. At least two other enzymes are involved in the 2-5A pathway: (i) a phosphodiesterase, which specifically cleaves (2' -5 ')-phosphodiester linkages, starting at the 2'-terminus; the induction of this enzyme by IFN has been demonstrated only in mouse L cells [33] and its role in intact cells is not yet understood [34]; (ii) one or several phosphatases able to dephosphorylate 2-5A to its core; the occurrence of this (these) enzyme(s) in intact cells are/is also not clear [28]. The presence of these two enzymes may account for the rapid degradation of 2-5A in intact cells and cell extracts.…”

Section: -Sa Analogmentioning

confidence: 99%

Antiviral activity of a chemically stabilized 2‐5A analog upon microinjection into HeLa cells

et al. 1986

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2‐5A[ppp(A2'p) n 5'A] has been implicated as a mediator in the antiviral action of interferon. Its direct evaluation as an indicator of virus replication is hampered by two limitations: its inability to penetrate intact cells, and its rapid intracellular degradation by (2'–5')phosphodiesterase. These problems could be overcome by using a microinjection technique whereby a phosphodiesterase‐resistant analog of 2‐A, in which the 2'‐terminals adenosine residue is replaced by 2‐(9‐adenyl)‐6‐hydroxy‐methyl‐4‐hexylmorpholine, was injected into individual HeLa cells before infection with mengovirus or vesicular stomatitis virus (VSV). This comparative assay with two representatives of different virus classes in a single experimental system pointed to the high sensitivity of VSV to inhibition by 2‐5A oligonucleotides, in contrast with the low sensitivity of mengovirus. Microinjection of the hexylmorpholine 2‐5A analog led to a much greater reduction in mengovirus yield than did microinjection of 2‐5A itself.

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“…2-5As that lack a 5'-terminal dior triphosphate or that are composed of less than three adenylate residues are not capable of activating the endonu-clease (15,33). Phosphodiesterase levels were found to be unaffected in a variety of interferon-treated cells (1,30,36,37), although the induction of phosphodiesterase was observed in some systems (17,20,27).…”

mentioning

confidence: 99%

Accumulation of 2',5'-oligoadenylates in encephalomyocarditis virus-infected mice

Hearl¹,

Johnston²

1987

J Virol

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Levels of 2',5'-oligoadenylates (2-5A) in various tissues of murine encephalomyocarditis virus (EMCV)infected mice were determined and compared with those found in pathogen-free mice and in mice treated with the interferon inducer poly(I) * poly(C). In control, pathogen-free mice, liver, spleen, brain, and kidney tissues possessed levels of 2-5A below 1 pmol/g of tissue, demonstrating that 2-5A was not a major component of uninfected mouse tissue. All control tissues had low basal levels (0.3 to 2.0 pmol/h per g) of 2-5A synthetase, the enzyme responsible for 2-5A production. After mice were injected intravenously with the interferon inducer poly(I) * poly(C), circulating interferon, 2-5A synthetase, and 2-5A were elevated with increasing doses of double-stranded RNA. The greatest response to poly(I) poly(C) occurred in the kidney, in which enyme levels increased 5-fold and 2-5A levels increased 24-fold to 15 pmol/g. Mice that were infected with EMCV also * Corresponding author. MATERIALS AND METHODS Reagents. Poly(I) poly(C), pppA2'pA2'pA, and A2'pA2'pA were purchased from Pharmacia, Inc., Piscat-1586 Vol. 61, No. 5 on September 17, 2020 by guest http://jvi.asm.org/ Downloaded from 2',5'-OLIGOADENYLATES IN EMCV-INFECTED MICE 1587 away, N.J. C18 and silica Sep-paks and C18 ,uBondapak columns were obtained from Waters Associates, Inc., Milford, Mass. Microtiter plates (Immunolon I) were purchased from Dynatech Laboratories, Inc., Alexandria, Va. Biotinylated goat anti-rabbit immunoglobulin G, biotinylated rabbit anti-mouse immunoglobulin G, and streptavidin horseradish peroxidase were obtained from Bethesda Research Laboratories, Inc., Gaithersburg, Md. Radioactive pppA2'pA2'pA2'pA3'[32P]pCp was generously provided by

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2′‐Phosphodiesterase Activity in Human Cell Lines Treated or Untreated with Human Interferon

Cited by 15 publications

References 34 publications

Immunological evidence for the in vivo occurrence of (2'-5')adenylyladenosine oligonucleotides in eukaryotes and prokaryotes.

Immunological evidence for the in vivo occurrence of (2'-5')adenylyladenosine oligonucleotides in eukaryotes and prokaryotes.

Antiviral activity of a chemically stabilized 2‐5A analog upon microinjection into HeLa cells

Accumulation of 2',5'-oligoadenylates in encephalomyocarditis virus-infected mice

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