A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2

Sharp, Michael; Elvin, Paul; Walker, Rosemary A.; Brammar, William J.; Varley, Jennifer

doi:10.1038/bjc.1990.19

Cited by 33 publications

(21 citation statements)

References 42 publications

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“…These data parallel our previous findings that the acidic ribosomal phosphoprotein P2 also has higher expression levels in the benign breast tumours (Sharp et al, 1990). In situ hybridisation has shown these genes to be expressed predominantly in the epithelium of breast tumours.…”

supporting

confidence: 81%

“…We have isolated sequences with higher expression in the benign tissue (fibroadenoma) compared with the malignant tissue (carcinoma), and shown them to specify elongation factor-la (EF-1a) and human ubiquitin carboxyl extension protein (HUBCEP80); both proteins involved in translation. We have previously reported that the gene for another translation-associated protein, acidic ribosomal phosphoprotein P2, isolated as encoding a metastasis-related protein by Elvin et al (1988), has higher levels of RNA expression in benign tumours compared with malignant tumours (Sharp et al, 1990).…”

mentioning

confidence: 99%

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Differential expression of translation-associated genes in benign and malignant human breast tumours

Sharp¹,

Walker²,

Brammar³

et al. 1992

Br J Cancer

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Summary The human gene sequences encoding the translation-associated functions of a-subunit of elongation factor 1 (EF-la) and the ubiquitin carboxyl extension protein (HUBCEP80) have been isolated by differential cDNA screening, and found to have significantly higher levels of expression in fibroadenomas (benign) compared with carcinomas (malignant) of the breast. These data parallel our previous findings that the acidic ribosomal phosphoprotein P2 also has higher expression levels in the benign breast tumours (Sharp et al., 1990). In situ hybridisation has shown these genes to be expressed predominantly in the epithelium of breast tumours.

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supporting

confidence: 81%

mentioning

confidence: 99%

Differential expression of translation-associated genes in benign and malignant human breast tumours

Sharp¹,

Walker²,

Brammar³

et al. 1992

Br J Cancer

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“…The ribosomal proteins are thought to facilitate the folding and maintenance of an optimal configuration of the rRNAs (32), perhaps in this way conferring speed and accuracy on protein synthesis. Recently, the involvement of the ribosomal proteins in cell proliferation (33)(34)(35)(36)(37), differentiation (38), and apoptosis (39) has been demonstrated. It has been show that S10 protein can be cross-linked to eukaryotic initiation factor 3 (40), an observation suggesting that S10 protein forms part of the domain involved in binding of the initiation factor to the 40S subunit at the start of the translation (40).…”

Section: Discussionmentioning

confidence: 99%

Pituitary Tumor-transforming Gene Protein Associates with Ribosomal Protein S10 and a Novel Human Homologue of DnaJ in Testicular Cells

Pei

1999

Journal of Biological Chemistry

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Pituitary tumor-transforming gene (PTTG) is a recently characterized proto-oncogene that is expressed specifically in adult testis. In this study, we have used in situ hybridization and developmental Northern blot assays to demonstrate that PTTG mRNA is expressed stage-specifically in spermatocytes and spermatids during rat spermatogenic cycle. We have used the yeast two-hybrid system to identify proteins that interact with PTTG in testicular cells. Two positive clones were characterized. One of the clones is the ribosomal protein S10, the other encodes a novel human DnaJ homologue designated HSJ2. Northern blot analysis showed that testis contains higher levels of HSJ2 mRNA than other tissues examined, and the expression pattern of HSJ2 mRNA in postnatal rat testis is similar to PTTG. S10 mRNA levels do not vary remarkably among different tissues and remains unchanged during testicular germ cell differentiation. In vitro binding assays demonstrated that both S10 and HSJ2 bind to PTTG specifically and that PTTG can be co-immunoprecipitated with S10 and HSJ2 from transfected cells. Moreover, the binding sites for both proteins were located within the C-terminal 75 amino acids of the PTTG protein. These results suggest that PTTG may play a role in spermatogenesis. Pituitary tumor-transforming gene (PTTG)1 was originally isolated from a rat pituitary tumor cell line by RNA differential display (1). Overexpression of PTTG resulted in cell transformation in fibroblasts and tumor formation in nude mice (1). PTTG mRNA was found to be highly expressed in a variety of tumor cell lines, suggesting a possible role of PTTG in tumorigenesis outside the pituitary gland.2 Testis is one of the few normal adult tissues where a shorter form of PTTG mRNA is expressed (1). The genomic structure of the rat PTTG has recently been characterized (2). A transcriptional enhancer element was identified in the PTTG 5Ј-flanking region that was required for transcriptional activation of PTTG in a testicular germ cell line, GC2 (2). This enhancer element also contains the binding sites for multiple nuclear proteins, two of which are germ cell-specific (2).Although PTTG mRNA is expressed in various testicular cell lines, including Sertoli, Leydig, and germ cells (2), the expression pattern of PTTG in normal testis is unknown. In this study, we have used in situ hybridization and developmental Northern blot assays to determine the cell type and the differentiation stage in which PTTG mRNA is expressed during the spermatogenic cycle. Our results showed that PTTG mRNA is expressed predominantly in spermatocytes and spermatids in a stage-specific manner, suggesting that PTTG may play a role in spermatogenesis. Because the amino acid sequence of PTTG does not reveal any identifiable structural or functional motifs, it is difficult to deduce its possible functions. To further our understanding of the role of PTTG in spermatogenesis, an in vivo strategy was employed to identify proteins capable of physically associating with PTTG. The yeast two-hybri...

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“…The first one was isolated representing mRNA associated with tumor progression and metastasis in 1988 and was identified as RPP2 in 1990 [14,15]. RPL31 cDNA was selected from a normal colon cDNA library on the basis of overexpression in familial adenomatous polyposis (FAP).…”

Section: Ribosomal Proteins and Colorectal Car-cinomamentioning

confidence: 99%

Ribosomal Proteins and Colorectal Cancer

Lai

Xu²

2007

124

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Abstract:The ribosome is essential for protein synthesis. The composition and structure of ribosomes from several organisms have been determined, and it is well documented that ribosomal RNAs (rRNAs) and ribosomal proteins (RPs) constitute this important organelle. Many RPs also fill various roles that are independent of protein biosynthesis, called extraribosomal functions. These functions include DNA replication, transcription and repair, RNA splicing and modification, cell growth and proliferation, regulation of apoptosis and development, and cellular transformation. Previous investigations have revealed that RP regulation in colorectal carcinomas (CRC) differs from that found in colorectal adenoma or normal mucosa, with some RPs being up-regulated while others are down-regulated. The expression patterns of RPs are associated with the differentiation, progression or metastasis of CRC. Additionally, the recent literature has shown that the perturbation of specific RPs may promote certain genetic diseases and tumorigenesis. Because of the implications of RPs in disease, especially malignancy, our review sought to address several questions. Why do expression levels or categories of RPs differ in different diseases, most notably in CRC? Is this a cause or consequence of the diseases? What are their possible roles in the diseases? We review the known extraribosomal functions of RPs and associated changes in colorectal cancer and attempt to clarify the possible roles of RPs in colonic malignancy.

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A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2

Cited by 33 publications

References 42 publications

Differential expression of translation-associated genes in benign and malignant human breast tumours

Differential expression of translation-associated genes in benign and malignant human breast tumours

Pituitary Tumor-transforming Gene Protein Associates with Ribosomal Protein S10 and a Novel Human Homologue of DnaJ in Testicular Cells

Ribosomal Proteins and Colorectal Cancer

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