ribonucleoprotein

出典: meddic

リボ核タンパク質リボヌクレオタンパク質リボ核タンパクRNAタンパク質

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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/04/15 11:41:01」(JST)

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英文文献

  • S100A7 overexpression is a predictive marker for high risk of malignant transformation in oral dysplasia.
  • Kaur J, Matta A, Kak I, Srivastava G, Assi J, Leong I, Witterick I, Colgan TJ, Macmillan C, Siu KW, Walfish PG, Ralhan R.Author information Alex and Simona Shnaider Laboratory in Molecular Oncology, Mount Sinai Hospital, Joseph & Wolf Lebovic Health Complex, Toronto, ON, Canada.AbstractEarly detection of oral lesions (OLs) at high risk of cancer development is of utmost importance for intervention. There is an urgent unmet clinical need for biomarkers that allow identification of high-risk OLs. Recently, we identified and verified a panel of five candidate protein biomarkers namely S100A7, prothymosin alpha, 14-3-3ζ, 14-3-3σ and heterogeneous nuclear ribonucleoprotein K using proteomics to distinguish OLs with dysplasia and oral cancers from normal oral tissues. The objective of our study was to evaluate the potential of these candidate protein biomarkers for identification of oral dysplastic lesions at high risk of cancer development. Using immunohistochemistry, we analyzed expressions of these five candidate protein biomarkers in 110 patients with biopsy-proven oral dysplasia and known clinical outcome and determined their correlations with p16 expression and HPV 16/18 status. Kaplan-Meier survival analysis showed reduced oral cancer-free survival (OCFS) of 68.6 months (p = 0.007) in patients showing cytoplasmic S100A7 overexpression when compared to patients with weak or no S100A7 immunostaining in cytoplasm (mean OCFS = 122.8 months). Multivariate Cox regression analysis revealed cytoplasmic S100A7 overexpression as the most significant candidate marker associated with cancer development in dysplastic lesions (p = 0.041, hazard ratio = 2.36). In conclusion, our study suggested the potential of S100A7 overexpression in identifying OLs with dysplasia at high risk of cancer development.
  • International journal of cancer. Journal international du cancer.Int J Cancer.2014 Mar 15;134(6):1379-88. doi: 10.1002/ijc.28473. Epub 2013 Oct 8.
  • Early detection of oral lesions (OLs) at high risk of cancer development is of utmost importance for intervention. There is an urgent unmet clinical need for biomarkers that allow identification of high-risk OLs. Recently, we identified and verified a panel of five candidate protein biomarkers namel
  • PMID 24122701
  • Transcriptional analysis of hnRNPA0, A1, A2, B1, and A3 in lung cancer cell lines in response to acidosis, hypoxia, and serum deprivation conditions.
  • Romero-Garcia S, Prado-Garcia H, Lopez-Gonzalez JS.Author information Department of Chronic-Degenerative Diseases, National Institute of Respiratory Diseases "Ismael Cosío Villegas," Mexico City , Mexico.AbstractABSTRACT The ribonucleoproteins (hnRNPs) have important roles in multiple aspects of nucleic acid metabolism and in the regulation of different cellular processes. Abnormal expression of hnRNPs has been reported in several types of cancer including lung, pancreatic, and gastric carcinomas. Heterogenous tumor cell populations generate a tumor microenvironment that can present normoxic, hypoxic, or acidic regions. The analysis of hnRNP transcriptional responses considering the changing nature of the tumor microenvironment is important to understand tumor cell survival under stress conditions. We analyzed the transcriptional response of hnRNPA0, A1, A2, B1, and A3 in lung tumor cell lines under acidosis, hypoxia, and serum deprivation conditions. We used qRT-PCR to obtain a relative quantification of the hnRNPA/B transcript levels. We found that the hnRNPA2 transcript was the most abundant, followed by B1, A0, and A1. Expression of hnRNPA3 was the lowest, although its transcript levels were the most constant. hnRNPA/B transcript levels in lung tumor cell lines responded to changes in the microenvironment; however, hnRNPB1 transcript levels relative to hnRNPA2 expression did no change in all tested stress conditions, indicating that the alternative splicing between these isoforms was constant. hnRNPA1, A2, and B1 transcript levels were upregulated under serum deprivation conditions; possibly to promote a migration phenotype. Our data provide new insights into the transcriptional responses of ribonucleoproteins that might favor tumor cell survival and migration.
  • Experimental lung research.Exp Lung Res.2014 Feb;40(1):12-21. doi: 10.3109/01902148.2013.856049. Epub 2013 Nov 18.
  • ABSTRACT The ribonucleoproteins (hnRNPs) have important roles in multiple aspects of nucleic acid metabolism and in the regulation of different cellular processes. Abnormal expression of hnRNPs has been reported in several types of cancer including lung, pancreatic, and gastric carcinomas. Heterogen
  • PMID 24246049
  • Catalytically active telomerase holoenzyme is assembled in the dense fibrillar component of the nucleolus during S phase.
  • Lee JH, Lee YS, Jeong SA, Khadka P, Roth J, Chung IK.Author information Department of Integrated Omics for Biomedical Science, Graduate School of Yonsei University, 134 Shinchon-dong, Seoul, 120-749, Korea.AbstractThe maintenance of human telomeres requires the ribonucleoprotein enzyme telomerase, which is composed of telomerase reverse transcriptase (TERT), telomerase RNA component, and several additional proteins for assembly and activity. Telomere elongation by telomerase in human cancer cells involves multiple steps including telomerase RNA biogenesis, holoenzyme assembly, intranuclear trafficking, and telomerase recruitment to telomeres. Although telomerase has been shown to accumulate in Cajal bodies for association with telomeric chromatin, it is unclear where and how the assembly and trafficking of catalytically active telomerase is regulated in the context of nuclear architecture. Here, we show that the catalytically active holoenzyme is initially assembled in the dense fibrillar component of the nucleolus during S phase. The telomerase RNP is retained in nucleoli through the interaction of hTERT with nucleolin, a major nucleolar phosphoprotein. Upon association with TCAB1 in S phase, the telomerase RNP is transported from nucleoli to Cajal bodies, suggesting that TCAB1 acts as an S-phase-specific holoenzyme component. Furthermore, depletion of TCAB1 caused an increase in the amount of telomerase RNP associated with nucleolin. These results suggest that the TCAB1-dependent trafficking of telomerase to Cajal bodies occurs in a step separate from the holoenzyme assembly in nucleoli. Thus, we propose that the dense fibrillar component is the provider of active telomerase RNP for supporting the continued proliferation of cancer and stem cells.
  • Histochemistry and cell biology.Histochem Cell Biol.2014 Feb;141(2):137-52. doi: 10.1007/s00418-013-1166-x. Epub 2013 Dec 7.
  • The maintenance of human telomeres requires the ribonucleoprotein enzyme telomerase, which is composed of telomerase reverse transcriptase (TERT), telomerase RNA component, and several additional proteins for assembly and activity. Telomere elongation by telomerase in human cancer cells involves mul
  • PMID 24318571

和文文献

  • Reversible response of protein localization and microtubule organization to nutrient stress during Drosophila early oogenesis
  • Shimada Yuko,Burn K. Mahala,Ryusuke Niwa Ryusuke Niwa,Cooley Lynn,丹羽 隆介
  • Developmental biology 355(2), 250-262, 2011-07
  • … Under nutrient stress, Yps and other components of the oskar ribonucleoprotein complex accumulated in large processing bodies in nurse cells, accompanied by MT reorganization. …
  • NAID 80021814863
  • The Contribution of Peripheral Stem-Loops to the Catalytic Activity of Archaeal RNase P RNA from Pyrococcus horikoshii OT3
  • HARA Tadashi,TERADA Atsushi,YAMAGUCHI Hiroki,NAKASHIMA Takashi,KAKUTA Yoshimitsu,KIMURA Makoto
  • Bioscience, biotechnology, and biochemistry 75(4), 816-819, 2011-04-23
  • We investigated the contribution of peripheral stem-loops to the catalytic activity of an archaeal RNase P RNA, PhopRNA, from Pyrococcus horikoshii OT3. PhopRNA mutants, in which the stem-loops were i …
  • NAID 10028272110
  • PP-504 Identification of RAM (ribonucleoprotein associated molecule) overexpressed in highgrade prostate cancer cells
  • 庵地 孝嗣,田村 賢司,降幡 睦夫,佐古田 初音,川田 千明,佐竹 宏文,執印 太郎
  • 日本泌尿器科學會雜誌 102(2), 488, 2011-03-20
  • NAID 110008612877

関連リンク

ribonucleoprotein /ri·bo·nu·cleo·pro·tein/ (-noo″kle-o-pro´tēn) a substance composed of both protein and ribonucleic acid. Abbreviated RNP. ri·bo·nu·cle·o·pro·tein (r b-n kl--pr t n) n. Abbr. RNP A nucleoprotein that contains RNA. ...
ribonucleoprotein ri·bo·nu·cle·o·pro·tein (rī'bō-nōō'klē-ō-prō'tēn, -tē-ĭn, -nyōō'-) n. Abbr. RNP A nucleoprotein that contains RNA.

関連画像

Interplay of PIWI/Argonaute protein MIWI Figure 2: A model for the recruitment of Chaperoning ribonucleoprotein biogenesis Heterogeneous nuclear ribonucleoproteinSmall nuclear ribonucleoprotein Small nuclear ribonucleoprotein


★リンクテーブル★
リンク元リボ核タンパク質」「RNAタンパク質」「RNP」「リボ核蛋白質
拡張検索U4-U6 small nuclear ribonucleoprotein」「U5 small nuclear ribonucleoprotein」「small cytoplasmic ribonucleoprotein」「deoxyribonucleoprotein

リボ核タンパク質」

  [★]

ribonucleoprotein RNP
リボ核蛋白質、リボ核蛋白、リボ核タンパクリボヌクレオタンパク質
[show details]


  • RNAとタンパク質の複合体。
  • ウイルス:ゲノムRNAとタンパク質との複合体
  • 真核生物:pre-mRNAと核のスプライシング酵素との複合体


RNAタンパク質」

  [★]

ribonucleoprotein
リボ核タンパクリボ核タンパク質リボヌクレオタンパク質

RNP」

  [★] リボ核タンパク質 ribonucleoprotein

リボ核蛋白質」

  [★]

ribonucleoprotein, RNP


U4-U6 small nuclear ribonucleoprotein」

  [★]

U4-U6核内低分子リボヌクレオタンパク質

U4-U6 snRNP

U5 small nuclear ribonucleoprotein」

  [★]

U5核内低分子リボヌクレオタンパク質

U5 snRNP

small cytoplasmic ribonucleoprotein」

  [★]

deoxyribonucleoprotein」

  [★]




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