Modulation of GAPDH expression and cellular localization after vaccinia virus infection of human adherent monocytes

• Autorzy: Nahlik K. W. , Mleczko A.K. , Gawlik M.K. , Rokita H.B.
• Języki publikacji: EN

Abstrakty

EN

Vaccinia virus is able to replicate in many cell types and is known to modulate apoptosis in infected cells. In this study, expression of apoptosis-related genes was screened in human adherent monocytes after vaccinia infection using a DNA array. A marked increase of the key glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) expression was found. Increased expression and nuclear translocation of GAPDH have recently been reported to participate in apoptosis of many cell types. To confirm the array results, levels of GAPDH mRNA were estimated by RT-PCR, showing an increase at 4 h p.i. followed by a slight decrease, which corre­lated with the viral anti-apoptotic E3L gene transcript levels. Subcellular localization of the enzyme in human monocytes was examined by Western blot and immunostaining of the infected cells. Both experiments revealed accumulation of GAPDH in the nucleus at 14 h p.i., which was completely suppressed at 24 h p.i. This might indicate GAPDH as a novel target for vaccinia anti-apoptotic modulation.

Słowa kluczowe

EN

cellular localization; vaccinia virus; man; Poxviridae; glyceraldehyde-3-phosphate dehydrogenase; monocyte; DNA virus; apoptosis; human adherent monocyte

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 3
• Opis fizyczny: p.667-676,fig.

Twórcy

autor

Nahlik K. W.

• Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland

autor

Mleczko A.K.

autor

Gawlik M.K.

autor

Rokita H.B.

Bibliografia

• Baxi MD, Vishwanatha JK. (1995) Uracil DNA glycosylase/glyceraldehydes-3-phosphate dehydrogenase is an Ap4 binding protein. Biochemistry..; 34: 9700-7.
• Burleson FG, Chambers TM, Wiedbank DL. (1991) Introduction to quantal virus assays. In Virology: a laboratory manual. Burleson FG, Chambers TM, Wiedbrauk DL. eds, pp 53-57. Academic Press, San Diego.
• Chomczynski P, Sacchi N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol- chlorophorm extraction. Anal Biochem.; 162: 156-9.
• Cooney EL, Mc Elrath MJ, Corey L, Hu S, Collier AC, Arditti D, Hoffman M, Coombs RW, Smith GE, Greenberg PD. (1993) Enhanced immunity to human immunodeficiency virus (HIV) envelope elicited by a combined vaccine regimen consisting of priming with a vaccinia recombinant expressing HIV envelope and boosting with gp160 protein. Proc Natl AcadSci USA.; 90: 1882-6.
• Dastoor Z, Dreyer JL. (2001) Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress. J Cell Sci.; 114: 1643-53.
• Davis LG, Dibner MD, Battey JF. (1986) Protein methods. In Basic methods in molecular biology. Elsevier Science Publishing Co.
• Dignam JD. (1990) Preparation of extracts from higher eukaryotes. Methods Enzymol.; 182: 194-203.
• Guzdek A, Stalinska K, Guzik K, Koj A. (2000) Differential responses of hematopoietic and non-hematopoietic cells to anti-inflammatory cytokines: IL-4, IL-13 and IL-10. J Physiol Pharmacol.; 51: 387-99.
• Harris JI, Waters M. (1976) Glyceraldehyde-3- phosphate dehydrogenase. In The ezymes. 3rd edn., Boyer PD. ed, Academic Press, New York.
• Henderson DA, Moss B. (1999) Smallpox and vaccinia. In Vaccines, 3rd edition, chapter 6. Plotkin SA, Orenstein WA. eds. W.B. Saunders Company, Philadelphia.
• Ishitani R, Chuang DM. (1996) Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons. Proc. natl. Acad. Sci. U.S.A. .; 93: 9937-41.
• Ishitani R, Tanaka M, Sunaga K. (1998) Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis. Mol Pharmacol.; 53: 701-7.
• Kettle S, Alcami A, Khanna A. (1997) Vaccinia virus serpin B13 R (SPI-2) inhibits interleukin-1beta-converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1beta-induced fever. J Gen Virol.; 78: 677-85.
• Kibler K, Shors T, Perkins K, Zeman C, Banaszak M, Biesterfeldt J, Langland J, Jacobs B. (1997) Double-stranded RNA is a trigger for apoptosis in vaccinia virus-infected cells. J Virol.; 71: 1992-2003.
• Kyhse-Andersen J. (1984) Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J Biochem Biophys Methods.; 10: 203-9.
• Maruyama W, Akao Y, Moussa BH, Davis BA, Naoi M. (2001) Transfection-enforced Bcl-2 overexpression and an anti-
• Parkinson drug, rasagiline, prevent nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase induced by an endogenous dopaminergic neurotoxin, N-methylsalsolinol. JNeurochem.; 78: 727-35.
• McFadden G, Barry M. (1998) How poxviruses oppose apoptosis. Semin Virol.; 8: 429-42.
• Morero RD, Lopez Vinals A. (1985) Fusion of phospholipid vesicles induced by muscle glyceraldehyde-3-phosphate dehydrogenase in the absence of calcium. Biochemistry.; 24: 1904-9.
• Moss B. (1994) Vaccinia virus transcription. In Transcription: mechanisms and regulation. Conaway RC, Conaway JW. eds, pp 185-205. Raven Press Ltd., New York.
• Moss B. (2001) Poxviridae: The viruses and their replication. In Fields virology, 4th edn. Knipe DM, Howley PM. eds, pp 2849-83. Lippincott Williams & Wilkins, Philadelphia.
• Moss B. (1996) Genetically engineered poxviruses for recombinant gene expression, vaccination and safety. Proc Natl Acad Sci US A.; 93: 11341-8.
• Ogden RC, Adams DA. (1987) Electrophoresis in agarose and acrylamide gels. Methods Enzymol.; 152: 61-87.
• Saunders PA, Chen RW, Chuang DM. (1999) Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase isoforms during neuronal apoptosis. JNeurochem.; 72: 925-32.
• Sawa A, Khan A, Hester L, Snyder S. (1997) Glyceraldehyde-3-phosphate dehydrogenase: Nuclear translocation participates in neuronal and nonneuronal cell death. Proc Natl Acad Sci US A.; 94: 11669-74.
• Shashidaran P, Chalmers-Redman RM, Carlile GW, Rodic V, Gurvich N, Yuen T, Tatton WG, Sealfon SC. (1999) Nuclear translocation of GAPDH-GFP fusion protein during apoptosis. NeuroReport.; 10: 1149-53.
• Shrager RL, Weiss GH. (1969) Rate zonal centrifugation in a Ficoll gradient. AnalBiochem.; 29: 230-7.
• Singh R, Green MR. (1993) Sequence-specifity binding of transfer RNA by glyceraldehydes- 3-phosphate dehydrogenase. Science.; 259: 365-8.
• Sirover M. (1999) New insight into an old protein: the functional diversity of mammalian glyceraldehydes-3-phosphate dehydrogenase. Biochim Biophys Acta.; 1432: 159-84.
• Smith PK, Krohn RI, Hermanson GT, Mallo AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC. (1985) Measurement of protein using bicinchoninic acid. Anal Biochem.; 150: 76-85.
• Suzuki YJ, Mizuno M, Packer L. (1994) Signal transduction for nuclear factor-kappa B activation. Proposed location of antioxidant-inhibitable step. J Immunol.; 153: 5008-15.
• Slezak K, Guzik K, Rokita H. (2000) Regulation of interleukin 12 and interleukin 10 expression in vaccinia virus-infected human monocytes and U-937 cell line. Cytokine.; 12: 900-8.
• Tisdale EJ. (2002) Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota/lambda and plays a role in microtubule dynamics in the early secretory pathway. J Biol Chem.; 277: 3334-41.
• Xiang Y, Condit RC, Vijaysri S, Jacobs B, Williams BR, Silverman RH. (2002) Blockade of interferon induction and action by the E3L double-stranded RNA binding proteins of vaccinia virus. J Virol.; 76: 5251-9.