Progress on the role of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells

LI Ying-hua; HU Zhen-lin; ZHANG Jun-ping

doi:10.3969/j.issn.1006-0111.2012.03.003

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Volume 30 Issue 3

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Article Navigation > Journal of Pharmaceutical Practice and Service > 2012 > 30(3): 165-167,225

LI Ying-hua, HU Zhen-lin, ZHANG Jun-ping. Progress on the role of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells[J]. Journal of Pharmaceutical Practice and Service, 2012, 30(3): 165-167,225. doi: 10.3969/j.issn.1006-0111.2012.03.003

Citation:

LI Ying-hua, HU Zhen-lin, ZHANG Jun-ping. Progress on the role of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells[J]. Journal of Pharmaceutical Practice and Service, 2012, 30(3): 165-167,225. doi: 10.3969/j.issn.1006-0111.2012.03.003

Progress on the role of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells

doi: 10.3969/j.issn.1006-0111.2012.03.003

Department of Biochemical Pharmacy, School of Pharmacy, Second Military Medical University, Shanghai 200433 China

Received Date: 2011-04-18
Rev Recd Date: 2011-10-28

Abstract

Objective To review the role of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells. Methods The relevant literatures were collected to make a summary of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells. Result and Conclusion Ribosomal Protein S3a played an important role in protein synthesis and also had unique extra-ribosomal functions, such as DNA repair, cell growth and cell differentiation. In recent years, it was found that the expression of Ribosomal Protein S3a was enhancedin tumor cells. It was involved in the regulation of proliferation, differentiation, and apoptosis of tumor cells by affecting the expression of oncogenes and tumor suppressor genes.
- Ribosomal Protein S3a,
- tumor cell,
- proliferation,
- differentiation and apoptosis

References

[1]	Lindstrom MS. Emerging functions of ribosomal proteins in gene-specific transcription and translation[J]. Biochem Biophys Res Commun,2009,379(2):167.
[2]	Dai MS, Sears R. Feedback regulation of c-Myc by ribosomal protein L11[J]. Cell Cycle, 2007,6:2735.
[3]	Khanna N, Sen S, Sharma H,et al. S29 ribosomal protein induces apoptosis in H520 cells and sensitizes them to chemotherapy[J]. Biochem Biophys Res Commun,2003,304:26.
[4]	Wan F, Anderson DE, Barnitz RA,et al. Ribosomal protein S3:KH domain subunit in NF-kappaB complexes that mediates selective gene regulation[J]. Cell,2007,131:927.
[5]	Kho CJ. Fte-1, a v-fos transformation effector gene, encodes the mammalian homologue of a yeast gene involved in protein import into mitochondria[J]. PNAS, 1992,89: 2200.
[6]	Lecomte F. The S3a ribosomal protein gene is identical to the Fte-1(v-fos transformation effector) gene and the TNF-alpha-induced TU-11 gene, and its transcript level is altered in transformed and tumor cells[J]. Gene 1997,186(2): 271.
[7]	Naora H, Nishida T, Shindo Y, et al. Association of nbl gene expression and glucocorticoid induced apoptosis in mouse thymus in vivo[J]. Immunology, 1995,85(1): 63.
[8]	Nygard O,Nilsson L. Translational dynamics:interactions between the translational factors, tRNA and ribosomes during eucaryotic protein synthesis[J]. Eur J Biochem, 1990,191:1.
[9]	Tarantul VZ, Nikolaev AI. Differential gene expression in B-cell non-Hodgkin's lymphoma of SIV-infected monkey[J]. AIDS Res Hum Retroviruses, 2000,16(2):173.
[10]	Zhu HX, Zhai BJ. Establishent and clinical significance of the gene expression map of normal peripheral blood mononuclear cells[J]. Tianjin Med J,2008,36(11):856.
[11]	Slizhikova DK, Vinogradova TV. The NOLA2 and RPS3a genes as highly informative markers for human squamous cell lung cancer[J]. Bioorg Khim, 2005 ,31(2):195.
[12]	Angelastro JM, Torocsik B, Greene LA. Nerve growth factor selectively regeulates expressionof transcripts encoding ribosomal proteins[J]. BMC Neuroscience,2002,3(1):3 .
[13]	Zhou ZD, Lei B, Liu DG,et al. Low content of protein S29 in ribosomes of human lung cancer cell line A549:detected by two-dimensional electrophoresis[J]. Protein Pept Lett,2003,10(1);91.
[14]	Jeremy L,Goodin,Charles L,et al. Characterization of human ribosomal S3a gene expression during adenosine 3:5cyclic monophosphate induced neuroendocrine differentiation of LNCaP cells. Regulation of S3a gene expression in LNCaP[J]. Molecular Biology Reports, 2002,29: 301.
[15]	Kho CJ, Wang Y, Zarbl H,et al. Effect of decreased fte-1 gene expression on protein synthesis, cell growth, and transformation [J]. Cell Growth Differ, 1996, 7(9): 1157.
[16]	Pandolfi PP. Dose the ribosome transelate cancer[J]. Nat Rev Cancer, 2003,3(3):179.
[17]	Ira G,Wool.Extraribosomal functions of ribosomal proteins[J].Trends Biochem Sci,1996,21:164.
[18]	Cui K , Margaret Coutts, Joachim Stahl,et al. Novel interaction between the transcription factor CHOP(GADD153) and the ribosomal protein FTE/S3a modulates erythropoiesis[J]. J Biol Chem ,2000,275(11):7591.
[19]	Naora H,Nishida T,Shindo Y. Constitutively enhanced nbl expression is associated with the induction of internuclesomal DNA cleavage by actinomycine D[J]. Biochem Biophys Res Commun,1996,224(1):258.
[20]	Russell L,Naora H. Down-regulated RPS3a/nbl expression during retinoid-induced differentiation of HL-60 cells: A close association with diminished susceptibility to actinomycin D-stimulated apoptosis[J]. Cell Struct Funct, 2000,25(2): 103.
[21]	Naora H. Involvement of ribosomal proteins in regulating cell growth and apoptosis: translational modulation or recruitment for extraribosomal activity[J]. Immunol Cell Biol, 1999,77(3): 197.
[22]	Naora H, Takai I, Adachi M, et al. Altered cellular responses by varying expression of a ribosomal protein gene: Sequential coor-dination of enhancement and suppression of ribosomal protein S3a gene expression induces apoptosis[J]. J Cell Biol,1998,141(3):741.
[23]	Naora H,Nishida T,Shindo Y. Antisense sequences of nbl gene induce apoptosis in the human promyelocytic leukemia cell line HL-60[J]. Leukemia ,1998,12:532.
[24]	Hu ZB, Minden MD, McCulloch EA,et al. Regulation of drug sensibility by ribosomal protein S3a[J]. Blood, 2000,95(3): 1047.
[25]	Demao S, Shuji S,Taketoshi T,et al. Inhibition of poly(ADP-ribose) polymerase activity by Bcl-2 in association with the Ribosomal Protein S3a[J]. Biochem, 2002,41 (3), 929.
[26]	Elena K, Mariya Y,Krisztina S, et al. Epstein-Barr virus-encoded EBNA-5 binds to Epstein-Barr virus-induced Fte1/S3a protein[J]. Exp Cell Res,2005,303:47.
[27]	缪扣荣,徐卫,李建勇. p53基因信号通路的新成员miRNA[J]. 中国实验血液学杂志,2009,17(2):500.
[28]	Aparicio S, Eaves CJ. p53: a new kingpin in the stem cell arena[J]. Cell,2009,138(6):1060.
[29]	徐恩相,李峰. p14^ARF、p53蛋白与脑胶质瘤发生发展的相关性研究[J].实用全科医学,2007,5(5):390.

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通讯作者: 陈斌, bchen63@163.com

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Progress on the role of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells

Department of Biochemical Pharmacy, School of Pharmacy, Second Military Medical University, Shanghai 200433 China

Received Date: 2011-04-18

Rev Recd Date: 2011-10-28

Key words:

Abstract: Objective To review the role of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells. Methods The relevant literatures were collected to make a summary of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells. Result and Conclusion Ribosomal Protein S3a played an important role in protein synthesis and also had unique extra-ribosomal functions, such as DNA repair, cell growth and cell differentiation. In recent years, it was found that the expression of Ribosomal Protein S3a was enhancedin tumor cells. It was involved in the regulation of proliferation, differentiation, and apoptosis of tumor cells by affecting the expression of oncogenes and tumor suppressor genes.

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Reference (29)

[1]	Lindstrom MS. Emerging functions of ribosomal proteins in gene-specific transcription and translation[J]. Biochem Biophys Res Commun,2009,379(2):167.
[2]	Dai MS, Sears R. Feedback regulation of c-Myc by ribosomal protein L11[J]. Cell Cycle, 2007,6:2735.
[3]	Khanna N, Sen S, Sharma H,et al. S29 ribosomal protein induces apoptosis in H520 cells and sensitizes them to chemotherapy[J]. Biochem Biophys Res Commun,2003,304:26.
[4]	Wan F, Anderson DE, Barnitz RA,et al. Ribosomal protein S3:KH domain subunit in NF-kappaB complexes that mediates selective gene regulation[J]. Cell,2007,131:927.
[5]	Kho CJ. Fte-1, a v-fos transformation effector gene, encodes the mammalian homologue of a yeast gene involved in protein import into mitochondria[J]. PNAS, 1992,89: 2200.
[6]	Lecomte F. The S3a ribosomal protein gene is identical to the Fte-1(v-fos transformation effector) gene and the TNF-alpha-induced TU-11 gene, and its transcript level is altered in transformed and tumor cells[J]. Gene 1997,186(2): 271.
[7]	Naora H, Nishida T, Shindo Y, et al. Association of nbl gene expression and glucocorticoid induced apoptosis in mouse thymus in vivo[J]. Immunology, 1995,85(1): 63.
[8]	Nygard O,Nilsson L. Translational dynamics:interactions between the translational factors, tRNA and ribosomes during eucaryotic protein synthesis[J]. Eur J Biochem, 1990,191:1.
[9]	Tarantul VZ, Nikolaev AI. Differential gene expression in B-cell non-Hodgkin's lymphoma of SIV-infected monkey[J]. AIDS Res Hum Retroviruses, 2000,16(2):173.
[10]	Zhu HX, Zhai BJ. Establishent and clinical significance of the gene expression map of normal peripheral blood mononuclear cells[J]. Tianjin Med J,2008,36(11):856.
[11]	Slizhikova DK, Vinogradova TV. The NOLA2 and RPS3a genes as highly informative markers for human squamous cell lung cancer[J]. Bioorg Khim, 2005 ,31(2):195.
[12]	Angelastro JM, Torocsik B, Greene LA. Nerve growth factor selectively regeulates expressionof transcripts encoding ribosomal proteins[J]. BMC Neuroscience,2002,3(1):3 .
[13]	Zhou ZD, Lei B, Liu DG,et al. Low content of protein S29 in ribosomes of human lung cancer cell line A549:detected by two-dimensional electrophoresis[J]. Protein Pept Lett,2003,10(1);91.
[14]	Jeremy L,Goodin,Charles L,et al. Characterization of human ribosomal S3a gene expression during adenosine 3:5cyclic monophosphate induced neuroendocrine differentiation of LNCaP cells. Regulation of S3a gene expression in LNCaP[J]. Molecular Biology Reports, 2002,29: 301.
[15]	Kho CJ, Wang Y, Zarbl H,et al. Effect of decreased fte-1 gene expression on protein synthesis, cell growth, and transformation [J]. Cell Growth Differ, 1996, 7(9): 1157.
[16]	Pandolfi PP. Dose the ribosome transelate cancer[J]. Nat Rev Cancer, 2003,3(3):179.
[17]	Ira G,Wool.Extraribosomal functions of ribosomal proteins[J].Trends Biochem Sci,1996,21:164.
[18]	Cui K , Margaret Coutts, Joachim Stahl,et al. Novel interaction between the transcription factor CHOP(GADD153) and the ribosomal protein FTE/S3a modulates erythropoiesis[J]. J Biol Chem ,2000,275(11):7591.
[19]	Naora H,Nishida T,Shindo Y. Constitutively enhanced nbl expression is associated with the induction of internuclesomal DNA cleavage by actinomycine D[J]. Biochem Biophys Res Commun,1996,224(1):258.
[20]	Russell L,Naora H. Down-regulated RPS3a/nbl expression during retinoid-induced differentiation of HL-60 cells: A close association with diminished susceptibility to actinomycin D-stimulated apoptosis[J]. Cell Struct Funct, 2000,25(2): 103.
[21]	Naora H. Involvement of ribosomal proteins in regulating cell growth and apoptosis: translational modulation or recruitment for extraribosomal activity[J]. Immunol Cell Biol, 1999,77(3): 197.
[22]	Naora H, Takai I, Adachi M, et al. Altered cellular responses by varying expression of a ribosomal protein gene: Sequential coor-dination of enhancement and suppression of ribosomal protein S3a gene expression induces apoptosis[J]. J Cell Biol,1998,141(3):741.
[23]	Naora H,Nishida T,Shindo Y. Antisense sequences of nbl gene induce apoptosis in the human promyelocytic leukemia cell line HL-60[J]. Leukemia ,1998,12:532.
[24]	Hu ZB, Minden MD, McCulloch EA,et al. Regulation of drug sensibility by ribosomal protein S3a[J]. Blood, 2000,95(3): 1047.
[25]	Demao S, Shuji S,Taketoshi T,et al. Inhibition of poly(ADP-ribose) polymerase activity by Bcl-2 in association with the Ribosomal Protein S3a[J]. Biochem, 2002,41 (3), 929.
[26]	Elena K, Mariya Y,Krisztina S, et al. Epstein-Barr virus-encoded EBNA-5 binds to Epstein-Barr virus-induced Fte1/S3a protein[J]. Exp Cell Res,2005,303:47.
[27]	缪扣荣,徐卫,李建勇. p53基因信号通路的新成员miRNA[J]. 中国实验血液学杂志,2009,17(2):500.
[28]	Aparicio S, Eaves CJ. p53: a new kingpin in the stem cell arena[J]. Cell,2009,138(6):1060.
[29]	徐恩相,李峰. p14^ARF、p53蛋白与脑胶质瘤发生发展的相关性研究[J].实用全科医学,2007,5(5):390.

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Progress on the role of Ribosomal Protein S3a in regulation of proliferation, differentiation and apoptosis in tumor cells

doi: 10.3969/j.issn.1006-0111.2012.03.003

Abstract

References

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通讯作者: 陈斌, bchen63@163.com

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