Elevated expression of the ribosomal protein S2 gene in human tumors

Chiao, Paul J.; Shin, Dong M.; Sacks, Peter G.; Hong, Waun Ki; Tainsky, Michael A.

doi:10.1002/mc.2940050309

Cited by 57 publications

(29 citation statements)

References 44 publications

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“…Reports have also been published that observed the altered expression of some ribosomal proteins in human cancers (21)(22)(23)(24)(25). The present study is the first to compare L13 mRNA expression levels in tumor versus normal tissue; it demonstrated that the level of L13 mRNA was higher in 28% of gastric, 41% of colorectal and 20% of liver cancer tissues.…”

Section: Discussionsupporting

confidence: 56%

“…For example, the gene encoding ribosomal protein S19 is mutated in approximately 25% of patients with DiamondBlackfan anemia, which is a rare congenital erythroblastopenia (20). Also, a differential expression of specific ribosomal protein genes was reported earlier as general characteristics of various tumor cell types (21)(22)(23)(24)(25).…”

Section: Introductionmentioning

confidence: 99%

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Activation of the ribosomal protein L13 gene in human gastrointestinal cancer

Kobayashi

Sasaki²,

Oshima³

et al. 2006

Int J Mol Med

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Abstract. Although ribosomal proteins are major components of ribosomes, recent data have shown them to have extraribosomal functions apart from ribosome and protein biosynthesis. In our earlier study, we showed that ribosomal protein L13 mRNA was up-regulated in response to DNA damage in hamster cells. We report here that L13 expression is up-regulated in human gastrointestinal cancers. We also examined the biological role of L13 on human cancer cells. Knocking down L13 expression using small interfering RNA (siRNA) resulted in drastic attenuation of cancer cell growth with significant G1 and G2/M arrest of the cell cycle. Moreover, L13 siRNA significantly enhanced the cellular sensitivity to certain DNA damaging agents and, concordantly, L13-overexpressing cells demonstrated greater chemoresistance compared to parent cells, suggesting an inverse correlation between L13 expression and chemosensitivity. By using semiquantitative RT-PCR, we analyzed expression of L13 in freshly resected cancer tissue of the stomach, colorectum and liver. Up-regulation of L13 mRNA expression was observed in 10 (28%) of 36 gastric, 19 (41%) of 46 colorectal and 5 (20%) of 25 liver cancer tissue samples compared to adjacent normal tissue samples. We also found that increased expression of the L13 gene correlated with clinical staging in gastric cancers. The results of this study suggest that L13 plays an essential role in the progression of some gastrointestinal malignancies.

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Section: Discussionsupporting

confidence: 56%

Section: Introductionmentioning

confidence: 99%

Activation of the ribosomal protein L13 gene in human gastrointestinal cancer

Kobayashi

Sasaki²,

Oshima³

et al. 2006

Int J Mol Med

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“…For example, several reports have shown that RPS3a and L19 possess oncogenic activities (9). The overexpression of RPS2 has been reported in human squamous cell carcinoma, breast tumor samples (10), and prostate cancer (7). RPS2 is also overexpressed in cells transformed by ras, SV-40, polyoma virus, Rous sarcoma virus, Abelson murine leukemia virus, and chemical carcinogen (11)(12)(13).…”

Section: R E T R a Cmentioning

confidence: 99%

Role of Ribosomal Protein RPS2 in Controlling let-7a Expression in Human Prostate Cancer

Wang

Hu²,

Amatangelo³

et al. 2011

Molecular Cancer Research

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We discovered that an inverse relationship exists in the expression of ras/c-myc and ribosomal protein RPS2 with pre-let-7a-1/let-7a/let-7f miRNA and prostate tumor cell malignancy. Nonmalignant IBC-10a cells expressed low levels of ras/RPS2 and elevated pre-let-7a-1/let-7a/let-7f miRNA, whereas the reverse occurred in malignant PCa-20a and PC-3ML cells. Stable transfection of IBC-10a cells with pBABE.ras and pBABE.RPS2 induced ras, c-myc, and RPS2 expression, whereas the levels of let-7a/let-7f miRNA dropped to near zero. Conversely, in pBABE.pre-let-7a-1 transfected PCa-20a and PC-3ML clones, let-7a/let-7f increased whereas ras, RPS2, and c-myc dropped greater than 5-fold. Electrophoretic mobility shift assays, antibody "supershift" assays and immunoprecipitation assays revealed that RPS2 specifically binds pre-let-7a-1 to block RNA processing. Immunoflourescent studies and Northern blots confirmed that RPS2 complexes with pre-let-7a-1 (i.e., in episomal structures) to block processing to let-7a/let-7f, indicating RPS2 may prevent let-7a miRNA expression to indirectly promote oncogene expression. Functional studies further showed that the colony-forming ability (CFA) and invasive activities of IBC-10a cells were significantly enhanced in pBABE-ras.IBC-10a and pBABE-RPS2-IBC-10a clones. Conversely, with the "knockdown" of ras and RPS2 in malignant PC-3ML cells (i.e., in pLKO. TRC.shRNA.ras.PC3-ML, pLKO.TRC.shRNA.RPS2.PC-3ML transfected cells), there was both a loss of these functions and a loss of tumorigenesis in SCID mice. Likewise, with the overexpression of let-7a/let-7f in pBABE. pre-let-7a-1.PC-3ML clones (and PCa-20a clones), CFAs, invasive activities in vitro, and tumorigenesis in vivo were significantly reduced. These results show for the first time that RPS2 blocks pre-let-7a-1 processing to enable ras and c-myc expression and the transformation of primary tumor cells. Mol Cancer Res; 9(1); 36-50. Ó2011 AACR.

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“…Moreover, rp S3 was found to act as an endonuclease in the DNA-repairing system [2]. Finally, some data indicate that tumor diseases may be accompanied by overexpression of rp genes 13,4) and by chromosomal rearrangements in regions of rp genes [ S ] . Therefore, structural analysis of these proteins is necessary for complete understanding of their fundamental role in the cell.…”

mentioning

confidence: 99%

Characterization of the Human Small‐Ribosomal‐Subunit Proteins by N‐Terminal and Internal Sequencing, and Mass Spectrometry

Vladimirov

Ivanov

Карпова

et al. 1996

European Journal of Biochemistry

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Reverse-phase HPLC was used to fractionate 40s ribosomal proteins from human placenta. Application of a C, reverse-phase column allowed us to obtain 27 well-resolved peaks. The protein composition of each chromatographic fraction was established by two-dimensional polyacrylamide gel electrophoresis and N-terminal sequencing. N-terminally blocked proteins were cleaved with endoproteinase Lys-C, and suitable peptides were sequenced. All sequences were compared with those of ribosomal proteins available from data bases. This allowed us to identify all proteins from the 40s human ribosomal subunit in the HPLC elution profile. By matrix-assisted laser-desorption ionization mass spectrometry the masses of the 40s proteins were determined and checked for the presence of post-translational modifications. For several proteins differences to the deduced sequences and the calculated masses were found to be due to post-translational modifications.Keywords: human ribosomal proteins ; HPLC ; N-terminal and internal amino acid sequencing ; matrixassisted-laser-desorption ionization MS ; post-translational modifications.Human ribosornd proteins are the main components of the fundamental processes which translate genetic information into proteins at the ribosome. Some ribosomal proteins (rp) are further involved in non-ribosomal functions. Recently, rp L7 was shown to contain the basic-region-leucine-zipper sequence which mediates the stable binding of this protein to DNA [I]. Moreover, rp S3 was found to act as an endonuclease in the DNA-repairing system [2]. Finally, some data indicate that tumor diseases may be accompanied by overexpression of rp genes 13, 4) and by chromosomal rearrangements in regions of rp genes [ S ] . Therefore, structural analysis of these proteins is necessary for complete understanding of their fundamental role in the cell. The task of structure determination of rat rp has been almost fully resolved by the application of recombinant-DNA technology ; details are reviewed in [6]. However, knowledge of the cDNA sequences does not provide information concerning post-translational modifications of the proteins after their biosynthesis and assembly into the ribosomal subunits. Several modifications of rp have been determined in the eubacterial ribosome [7, 81, and the eukaryotic rprotein S6 is known to be phosphorylated 191. This phosphorylation was shown to be connected with cell growth [I 01 and cell cycle control [I I]. At least seven 40s proteins from HeLa cells were found to be methylated, and the level of their methylation was shown to be altered in the Abbreviations. MALDI, matrix-assisted laser-desorption ionization ; Lys-C, endoproteinase Lys-C; RP, reverse-phase; rp, ribosomal protein ; S-proteins, proteins of the small ribosomal subunit; 40S, small ribosomal subunit; TP40, total protein mixture of the small ribosomal subunit; TOF, time-of-flight ; Pth-Xaa, phenylthiohydantoin -amino-acid.course of the cell cycle [12]. It is also known that ribosomal proteins may be acetylated 17, 13, 141. However...

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Elevated expression of the ribosomal protein S2 gene in human tumors

Cited by 57 publications

References 44 publications

Activation of the ribosomal protein L13 gene in human gastrointestinal cancer

Activation of the ribosomal protein L13 gene in human gastrointestinal cancer

Role of Ribosomal Protein RPS2 in Controlling let-7a Expression in Human Prostate Cancer

Characterization of the Human Small‐Ribosomal‐Subunit Proteins by N‐Terminal and Internal Sequencing, and Mass Spectrometry

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