Increased expression of ribosomal protein S2 in liver tumors, posthepactomized livers, and proliferating hepatocytes in vitro.

• Authors: Piotr Kowalczyk , Marek Woszczyński , Jerzy Ostrowski
• Languages of publication: EN

Abstracts

EN

The ribosomal protein S2 (RPS2) is encoded by a gene from the highly conserved mammalian repetitive gene family LLRep3. It participates in aminoacyl-transfer RNA binding to ribosome, potentially affecting the fidelity of mRNA translation. These studies were designed to measure the expression of RPS2 during increased cell proliferation. Using Western and Northern blot analyses, we found that the levels of RPS2 protein and its corresponding mRNA were higher in mouse hepatocellular carcinoma, in mouse livers after one-third partial hepatectomy, and in serum-starved cultured hepatocytes following serum treatment. Our study shows that the increased expression of RPS2 correlates with increased cell proliferation. However, whether the altered expression of this protein reflects its involvement in cellular proliferation or represents an associated phenomena is still a key question that needs to be explored.

Keywords

EN

ribosomal protein S2; partial hepatectomy; hepatocytes; hepatocellular carcinoma

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2002
• Volume: 49
• Issue: 3
• Pages: 615-624

Dates

published

2002

received

2002-02-28

accepted

2002-08-07

Contributors

author

Piotr Kowalczyk

• Department of Gastroenterology, Medical Center for Postgraduate Education at the Maria Skłodowska-Curie Memorial Cancer Center and Institute of Oncology, Warszawa, Poland

author

Marek Woszczyński

• Department of Animal Genetics, Cancer Center and Institute of Oncology, Warszawa, Poland

author

Jerzy Ostrowski

• Department of Gastroenterology, Medical Center for Postgraduate Education at the Maria Skłodowska-Curie Memorial Cancer Center and Institute of Oncology, Warszawa, Poland

References

• Aloni R, Peleg D, Meyuhas O. (1992) Selective translational control and nonspecific posttranscriptional regulation of ribosomal protein gene expression during development and regeneration of rat liver. Mol Cell Biol.; 12: 2203-12.
• Cartwright CA, Meisler AI, Eckhart W. (1990) Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis. Proc Natl Acad Sci U S A.; 87: 558-62.
• Chen FW, Ioannou Y. (1999) Ribosomal proteins in cell proliferation and apoptosis. Int Rev Immunol.; 18: 429-48.
• Chester KA, Robson L, Begent RHJ, Talbot IC, Pringle JH, Primrose L, Macpherson AJS, Boxer G, Southall P, Malcolm ADB. (1989) Identification of a human ribosomal protein mRNA with increased expression in colorectal tumours. Biochim Biophys Acta.; 1009: 297-300.
• Chiao PJ, Shin DM, Sacks PG, Hong WK, Tainsky MA. (1992) Elevated expression of the ribosomal protein S2 gene in human tumors. Mol Carcinog.; 5: 219-31.
• Dejgaard K, Leffers H, Rasmussen HH, Madsen P, Kruse TA, Gesser B, Nilsen H, Celis JE. (1994) Identification, molecular cloning, expression and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing. J Mol Biol.; 236: 33-48.
• DePhilip RM, Rudert WA, Lieberman I. (1980) Preferential stimulation of ribosomal protein synthesis by insulin and in the absence of ribosomal and messenger ribonucleic acid formation. Biochemistry.; 19: 1662-9.
• Dignam JO, Lebovitz RM, Roeder R. (1983) Accurate transcripition initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res.; 11: 1475-89.
• Fausto N, Mead ME. (1989) Regulation of liver growth: proto-oncogenes and transforming growth factors. Lab Invest.; 60: 4-13.
• Fukunaga R, Hunter T. (1997) MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrate. EMBO J.; 16: 1921-33.
• Hammond ML, Bowman LH. (1988) Insulin stimulates the translation of ribosomal proteins and the transcription of rDNA in mouse myoblasts. J Biol Chem.; 263: 17785-91.
• Ignotz GG, Hokari S, DePhilip RM, Tsukada K, Lieberman I. (1981) Lodish model and regulation of ribosomal protein synthesis by insulin-deficient chick embryo fibroblasts. Biochemistry.; 20: 2550-8.
• Kief DR, Warner JR. (1981) Coordinate control of syntheses of ribosomal ribonucleic acid and ribosomal proteins during nutritional shift-up in Saccharomyces cerevisiae. Mol Cell Biol.; 1: 1007-15.
• Liliensiek B, Rocha M, Umansky V, Benner A, Lin J, Ziegler R, Nawroth PP, Schirrmacher V. (1998) Identification of four genes in endothelial cells whose expression is affected by tumor cells and host immune status - a study in ex vivo - isolated endothelial cells. Blood.; 92: 3394-404.
• Loging WT, Reisman D. (1999) Elevated expression of ribosomal protein genes L37, Rpp-1, and S2 in the presence of mutant p53. Cancer Epidemiol Biomarkers Prev.; 8: 1011-6.
• Lutsch G, Stahl J, Kargel H-J, Noll F, Bielka H. (1990) Immunoelectron microscopic studies on the location of ribosomal proteins on the surface of the 40S ribosomal subunit from rat liver. Eur J Cell Biol.; 51: 140-50.
• Michalopoulos GK. (1990) Liver regeneration: molecular mechanism of growth control. FASEB J.; 4: 176-87.
• Nygard O, Nilsson L. (1990) Translational dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis. Eur J Biochem.; 191: 1-17.
• Pogue-Geile K, Geiser JR, Shu M, Miller C, Wool IG, Meisler AI, Pipas JM. (1991) Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein. Mol Cell Biol.; 11: 3842-9.
• Ostrowski J, Sims JE, Sibley CH, Valentine MA, Dower SK, Meier KE, Bomsztyk K. (1991) A serine/threonine kinase activity is closely associated with a 65-kDa phosphoprotein specifically recognized by the K enhancer element. J Biol Chem.; 266: 12722-33.
• Ostrowski J, Van Seuningen I, Seger R, Rouch CT, Sleath PR, McMullen BA, Bomsztyk K. (1994) Purification, cloning, and expression of a murine phosphoprotein that binds the B motif in vitro identifies it as the homolog of the human hnRNP K protein. Description of a novel DNA-dependent phosphorylation process. J Biol Chem.; 269: 17626-34.
• Ostrowski J, Woszczynski M, Kowalczyk P, Trzeciak L, Hennig E, Bomsztyk K. (2000) Treatment of mice with EGF and orthovanadate activates cytoplasmic and nuclear MAPK, p70S6k, and p90rsk in the liver. J Hepatol.; 32: 965-74.
• Ostrowski J, Kawata Y, Schullery D, Denisenko ON, Abrass CK, Bomsztyk K. (2001). Insulin modifies the hnRNP K protein and alters its interaction with DNA and RNA. Proc Natl Acad Sci U S A.; 98: 9044-9.
• Ostrowski J, Wyrwicz L, Rychlewski L, Bomsztyk K. (2002) Heterogeneous nuclear ribonucleoprotein K protein associates with multiple mitochondrial transcripts within the organelle. J Biol Chem.; 277: 6303-10.
• Ou JH, Yen TS, Wang YF, Kam WK, Rutter WJ. (1987) Cloning and characterization of a human ribosomal protein gene with enhanced expression in fetal and neoplastic cells. Nucleic Acids Res.; 15: 8919-34.
• Scott MR, Westphal K-H, Rigby PW. (1983) Activation of mouse genes in transformed cells. Cell.; 34: 557-67.
• Seshadri T, Uzman JA, Oshima J, Campisi J. (1993) Identification of a transcript that is down-regulated in senescent human fibroblasts. Cloning, sequence analysis, and regulation of the human L7 ribosomal protein gene. J Biol Chem.; 268: 18474-80.
• Shama S, Avni D, Frederickson R, Sonenberg N, Meyuhas O. (1995) Overexpression of initiation factor eIF-4E does not relieve the translational repression of ribosomal protein mRNAs in quiescent cells. Gene Expr.; 4: 241-52.
• Shin DM, Chiao PJ, Sacks PG, Shin HJ, Hong WK, Hittelman WN, Tainsky MA. (1993) Activation of ribosomal protein S2 gene expression in a hamster model of chemically induced oral carcinogenesis. Carcinogenesis.; 14: 163-6.
• Slynn G, Jenner D, Potts W, Elvin P, Morten JEN. (1990) Human cDNA sequence homologous to the mouse LLRep3 gene family. Nucleic Acids Res.; 18: 681.
• Squinto SP, Block AL, Doucet JP. (1989) Epidermal growth factor induction of cellular proliferation and protooncogene expression in growth-arrested rat H4IIE hepatoma cells: role of cyclic adenosine monophosphate. Mol Endocrinol.; 3: 433-46.
• Stanners CP, Adams ME, Harkins JL, Pollard JW. (1979) Transformed cells have lost control of ribosome number through their growth cycle. J Cell Physiol.; 100: 127-38.
• Starkey C, Levy L. (1995) Identification of differentially expressed genes in T-lymphoid malignancies in an animal model system. Int J Cancer.; 62: 325-31.
• Taub R. (1996) Transcriptional control of liver regeneration. FASEB J.; 10: 413-27.
• Tushinski RJ, Warner JR. (1982) Ribosomal proteins are synthesized preferentially in cells commencing growth. J Cell Physiol.; 112: 128-35.
• Van Seuingen I, Ostrowski J, Bomsztyk K. (1995) Description of an IL-1-responsive kinase that phosphorylates the K protein. Enhancement of phosphorylation by selective DNA and RNA motifs. Biochemistry.; 34: 5644-50.
• Warner JR, Nierras CR. (1998) Trapping human ribosomal protein genes. Genome Res.; 8: 419-21.