Regulation of 2',5'-oligoadenylate synthetase gene expression by interferons and platelet-derived growth factor.

García-Blanco, Mariano A.; Lengyel, Péter; Morrison, Elizabeth D.; Brownlee, Clare; Stiles, C D; Rutherford, Michael N.; Hannigan, Gregory E.; Williams, Bryan R.G.

doi:10.1128/mcb.9.3.1060

Cited by 33 publications

(11 citation statements)

References 49 publications

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“…The increase of 2-5(A)synthetase activity in sperm cells did not affect their ability to penetrate zona-free hamster eggs. The assay involving human sperm penetration of zona free hamster eggs has been reported to be a measure of capacitation status of s erm cells strated the presence of in R ibin in the seminal plasma, that binding TGF$ a inity with the double-stranded RNA such as (Gould et al, 1983). Our data indicate t K at sperm motility and capacitation of sperm cells were not affected by an increase of 50 kDa protein related to 2-5(A)synthetase.…”

Section: Discussioncontrasting

confidence: 50%

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Transforming growth factor β₁ enhances expression of 50 kDa protein related to 2′‐5′ oligoadenylate synthetase in human sperm cells

Naz

Kumar

1991

Journal Cellular Physiology

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Human cellular polypeptide factors, namely interferon-alpha, interferon-gamma transforming growth factor (TGF)-alpha, and TGF-beta 1, were analyzed for their effect on motility of human sperm cells. Both interferons caused an inhibition of sperm cell motility due to direct cytotoxic effects without inducing 2'-5' oligoadenylate [2-5(A)]synthetase activity. TGF-alpha affected neither motility nor the levels of 2-5(A) synthetase in sperm cells. TGF-beta 1 had no affect on sperm motility, yet it caused an induction of 2-5(A)synthetase activity. Western immunoblot analysis of TGF-beta 1-treated sperm indicated an enhancement of a 50 kDa protein. Metabolic labeling of sperm cells revealed biosynthesis of one major protein of 50 kDa and at least five minor proteins in the range of 30-92 kDa; the level of 50 kDa protein increased after treatment with TGF-beta 1. The treatment of sperm cells with TGF-beta 1 did not affect their penetration in zona-free hamster eggs (SPA). These results indicate that TGF-beta 1 enhances expression of a 50 kDa protein related to 2-5(A) synthetase in human sperm cells along with other minor proteins, and this increase does not affect sperm motility and SPA.

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Section: Discussioncontrasting

confidence: 50%

“…Moreover, in other cell types, IFNs have been shown to induce 2-5(A)synthetase activity within 8 hr of treatment (Garcia-Blanco et al, 1989;Kumar and Mendelsohn, 1989). As shown in Figure lA, there was no induction of 2-5(A)synthetase activity in sperm cells treated with 100 or 1,000 unitdm1 of IFN-a or IFN-y for 8 hr.…”

Section: Resultsmentioning

confidence: 96%

Transforming growth factor β₁ enhances expression of 50 kDa protein related to 2′‐5′ oligoadenylate synthetase in human sperm cells

Naz

Kumar

1991

Journal Cellular Physiology

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“…This occurs in the absence of new protein synthesis and is a direct effect on transcription [91]. The 2-SA synthetase ISRE sequence is PDGF responsive, and PDGF treatment of BALB/c 3T3 fibroblasts results in the binding of nuclear factors to the ISRE [91]. Interestingly, the PDGF-induced and IFN-a-induced ISRE binding of factors appears to occur through the activation of different signaling pathways [71].…”

Section: Pdgf Induction Of the Isrementioning

confidence: 99%

Transcriptional regulation of interferon‐stimulated genes

Williams¹

1991

European Journal of Biochemistry

182

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Interferons (IFN) stimulate the expression of a number of genes following interaction with specific highaffinity plasma membrane receptors. The products of these genes either singly or coordinately mediate the antiviral, growth inhibitory or immunoregulatory activities attributed to IFN. While the gene products in some cases have been well characterized, other IFN-regulated genes encode proteins whose functions have yet to be elucidated. A feature common to all IFN-stimulated genes characterized thus far is the presence of a DNA element which constitutes an IFN-responsive enhancer, usually present in the 5' upstream region of the genes. This element, termed interferon-stimulated response element (ISRE) binds a nuclear factor(s) translocated from the cytoplasm to the nucleus following IFN-receptor-triggered signal transduction. The binding of these factors to the ISRE represents the initiating event in stimulating RNA-polymerase-11-mediated transcription from IFN-responsive genes. Depending on the nature of the cells responding to IFN and the genes involved, induced transcription may be prolonged or rapidly terminated. The rapid termination of transcription is dependent in some cases on IFNinduced protein synthesis and also involves factor binding to the ISRE. Recent progress in detailing these events will be discussed including IFN-receptor interactions, signal-transduction pathways, comparing and contrasting IFN-regulated genes and elucidation of IFN-regulated factors. IFN-receptor interactionsThe biological activity of IFN is initiated by the interaction with high-affinity receptors in the plasma membrane. Where this interaction has been analysed in kinetic experiments and compared to IFN-induced transcriptional responses [l], the data suggest that the degree of receptor occupancy in IFNsensitive cells is the rate-limiting step in determining the extent of the primary transcriptional response to IFN the chromosome-9-encoded binding component, being required for transduction of biological activity [S]. Similarly, the mouse IFN y receptor expressed in human cells binds mouse IFN y but does not transduce a signal to the cells [6]. While the cDNA for the human IFN type-I receptor encodes a functional activity, transfected clones expressing this activity exhibit low sensitivity to human IFN fl and to some human IFN a subspecies. This is consistent with data reporting a dissociation of IFN a and fl activities and suggest that other accessory molecules are involved in contributing to the expression of a high-affinity receptor and signal transduction [7]. Changes in receptor affinity associated with cell-growth arrest [8] Signal transduction by IFN CL and yThe elucidation of the sequences of the IFNa and y receptors has yielded little information about possible signal-transduction mechanisms. The human IFN a receptor has a short (100 amino acid) cytoplasmic domain with none of the conserved kinase domains necessary to impart protein kinase activity [9]. However, there are potential kinase sites in this domain and it ...

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“…For example, the synthesis of some proteins characteristically induced by the IFNs was also shown to be inducible by tumor necrosis factor (TNF) or interleukin 1 (IL-1) (18)(19)(20)(21)(22) or by growth factors (17,23,24). Furthermore, IL-1 (25) or TNF (26)(27)(28) were shown to stimulate IFN-p synthesis in some cells.…”

mentioning

confidence: 99%

Induction of the transcription factor IRF-1 and interferon-beta mRNAs by cytokines and activators of second-messenger pathways.

Fujita

Reis

Watanabe

et al. 1989

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

271

157

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Nuclear protein IRF-1 (interferon regulatory factor 1) was earlier shown to bind to cis-acting regulatory elements present on interferon (IFN)-a/fi genes and some IFN-inducible genes. Here we show that in both human FS-4 and murine L929 cells, steady-state levels of IRF-1 mRNA were increased by treatment with tumor necrosis factor (TNF), interleukin 1 (IL-1), poly(I)-poly(C), or IFN-fi. IRF-1 mRNA induction was also demonstrated in cells treated with calcium ionophore A23187 or with phorbol 12-myristate 13-acetate, but not with epidermal growth factor, dibutyryl-cAMP, or the adenylate cyclase activator forskolin. To determine whether stimulation of IRF-1 mRNA levels correlates with IFN-f3 induction, we compared IRF-1 and IFN-.8 mRNA levels in cells exposed to various stimuli. In L929 cells, treatment with poly(I)-poly(C) under conditions that failed to induce significant levels of IFN-I3 mRNA led to a very low induction of IRF-1 mRNA, but "priming" cells with IFN prior to the addition of poly(I)-poly(C) greatly increased both IRF-1 and IFN-fi mRNAs. In FS-4 cells an increase in IFN-8 mRNA (examined by the polymerase chain reaction) was seen after treatment with TNF, IL-1, A23187, or poly(I) poly(C), but not with IFN-P3 epidermal growth factor, dibutyryl-cAMP, or forskolin. Thus, all treatments that increased steady-state levels of IFN-j3 mRNA also enhanced IRF-1 mRNA levels. However, treatment with IFN-,B, which caused a marked stimulation in IRF-1 mRNA, failed to produce a detectable increase in IFN-fJ mRNA. It appears that IRF-1 may be necessary but not sufficient for IFN-/8 induction. The ability of TNF and IL-1 to increase both IRF-1 and IFN-f8 mRNAs may be responsible for some similarities in the actions of TNF, IL-1, and the IFNs.The induced expression of interferon (IFN)-a/P is controlled by sequences present in the 5' flanking region of the IFN-a/P3 genes (1-3). The regulatory region of the human IFN-p gene is composed of distinct functional domains, and inducibility by viruses or double-stranded RNA is thought to be regulated by the interaction of several trans-acting nuclear factors with these sequences (3-9). Virus-induced transcriptional activation of the human 8 (10) or IFN-a (11) genes can be mediated by specific repetitive hexanucleotide sequences present within the enhancer region. A nuclear factor termed IRF-1 (interferon regulatory factor 1) was identified on the basis of its ability to bind to these hexameric sequences (5). IRF-1, whose synthesis is strongly inducible by virus infection, acts as a positive transcription factor for the expression of IFN-a/,8 genes (12, 13).Recent observations suggest that regulatory mechanisms governing the expression of IFN-inducible genes partly overlap the mechanisms regulating the expression of the IFN-a/,3 genes themselves. This conclusion is based on the observations of similarities between the sequences controlling inducibility in IFN-a/,B genes and several IFN-induced genes (14-16). In addition, it was shown that some IFN-induced genes are also...

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Regulation of 2',5'-oligoadenylate synthetase gene expression by interferons and platelet-derived growth factor.

Cited by 33 publications

References 49 publications

Transforming growth factor β₁ enhances expression of 50 kDa protein related to 2′‐5′ oligoadenylate synthetase in human sperm cells

Transforming growth factor β₁ enhances expression of 50 kDa protein related to 2′‐5′ oligoadenylate synthetase in human sperm cells

Transcriptional regulation of interferon‐stimulated genes

Induction of the transcription factor IRF-1 and interferon-beta mRNAs by cytokines and activators of second-messenger pathways.

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Regulation of 2',5'-oligoadenylate synthetase gene expression by interferons and platelet-derived growth factor.

Cited by 33 publications

References 49 publications

Transforming growth factor β1 enhances expression of 50 kDa protein related to 2′‐5′ oligoadenylate synthetase in human sperm cells

Transforming growth factor β1 enhances expression of 50 kDa protein related to 2′‐5′ oligoadenylate synthetase in human sperm cells

Transcriptional regulation of interferon‐stimulated genes

Induction of the transcription factor IRF-1 and interferon-beta mRNAs by cytokines and activators of second-messenger pathways.

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Transforming growth factor β₁ enhances expression of 50 kDa protein related to 2′‐5′ oligoadenylate synthetase in human sperm cells

Transforming growth factor β₁ enhances expression of 50 kDa protein related to 2′‐5′ oligoadenylate synthetase in human sperm cells