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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Preferentially expressed antigen in melanoma

This gene encodes an antigen that is predominantly expressed in human melanomas and that is recognized by cytolytic T lymphocytes. It is not expressed in normal tissues, except testis. This expression pattern is similar to that of other CT antigens, such as MAGE, BAGE and GAGE. However, unlike these other CT antigens, this gene is also expressed in acute leukemias. Five alternatively spliced transcript variants encoding the same protein have been observed for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, POLYMERASE, HAD, ACID, NY-ESO-1
Papers on PRAME
Preferentially Expressed Antigen in Melanoma (PRAME) and the PRAME family of Leucine-Rich Repeat Proteins".
Staege et al., Halle, Germany. In Curr Cancer Drug Targets, Jan 2016
UNASSIGNED: Preferentially expressed antigen in melanoma (PRAME) is the best characterized member of the PRAME family of leucine-rich repeat (LRR) proteins.
Diagnostic marker signature for esophageal cancer from transcriptome analysis.
Bollschweiler et al., Köln, Germany. In Tumour Biol, Jan 2016
The markers significantly overexpressed already in earlier tumor stages (pT1-2) of both histological subtypes (n = 19) have been clustered in a "diagnostic signature": PLA2G7, PRAME, MMP1, MMP3, MMP12, LIlRB2, TREM2, CHST2, IGFBP2, IGFBP7, KCNJ8, EMILIN2, CTHRC1, EMR2, WDR72, LPCAT1, COL4A2, CCL4, and SNX10.
Knockdown of PRAME enhances adriamycin-induced apoptosis in chronic myeloid leukemia cells.
Wang et al., Rizhao, China. In Eur Rev Med Pharmacol Sci, Dec 2015
Previous studied has found that Preferentially Expressed Antigen of Melanoma (PRAME) is overexpressed in the leukemia cells, and knockdown of PRAME promoted apoptosis in leukemia K562 cells.
Natural killer cells facilitate PRAME-specific T-cell reactivity against neuroblastoma.
Nierkens et al., Utrecht, Netherlands. In Oncotarget, Dec 2015
We show that oncoprotein PRAME serves as an immunodominant antigen for neuroblastoma as NK-modulated neuroblastoma cells are recognized by PRAMESLLQHLIGL/A2-specific CTL clones.
Leukemic progenitor cells are susceptible to targeting by stimulated cytotoxic T cells against immunogenic leukemia-associated antigens.
Greiner et al., Ulm, Germany. In Int J Cancer, Dec 2015
PRAME (p = 0.0085), RHAMM (p = 0.03), WT1 (p = 0.04) and Proteinase 3 (p = 0.04) showed significant differential expression in LSC compared with HSC.
A Comprehensive Preclinical Model Evaluating the Recombinant PRAME Antigen Combined With the AS15 Immunostimulant to Fight Against PRAME-expressing Tumors.
Louahed et al., Rixensart, Belgium. In J Immunother, Oct 2015
The PRAME tumor antigen is a potential target for immunotherapy.
PRAME Expression and Its Clinical Relevance in Hodgkin's Lymphoma.
Duman et al., Adana, Turkey. In Acta Haematol, Jul 2015
The preferentially expressed antigen of melanoma (PRAME) is a cancer testis antigen and its expression is very scarce or absent in normal tissues.
Rates of MAGE-A3 and PRAME expressing tumors in FFPE tissue specimens from bladder cancer patients: potential targets for antigen-specific cancer immunotherapeutics.
Therasse et al., Leuven, Belgium. In Int J Clin Exp Pathol, 2014
The objectives of this study (NCT01706185) were to assess the rate of expression of the MAGE-A3 and PRAME genes in bladder tumors and to investigate the feasibility of using formalin-fixed paraffin-embedded (FFPE) tumor tissues for testing.
PRAME/EZH2-mediated regulation of TRAIL: a new target for cancer therapy.
Amarante-Mendes et al., Toronto, Canada. In Curr Mol Med, 2013
Our recent discovery that the complex PRAME/EZH2 is able to repress TRAIL expression, in a cancer-specific manner, suggests an alternative approach for combined cancer therapy.
Vaccines in non-small cell lung cancer: rationale, combination strategies and update on clinical trials.
De Braud et al., Milano, Italy. In Crit Rev Oncol Hematol, 2012
In the adjuvant setting the most relevant and promising vaccines are directed against MAGE-A3 and PRAME, respectively.
Epigenetic regulation of PRAME in acute myeloid leukemia is different compared to CD34+ cells from healthy donors: effect of 5-AZA treatment.
Pérez-Simón et al., Salamanca, Spain. In Leuk Res, 2012
PRAME expression is regulated at the epigenetic level. For this reason inhibitors of DNA methylation, such as 5-azacytidine, can modulate the expression of this tumor associated antigen.
Expression and prognostic relevance of PRAME in primary osteosarcoma.
Shen et al., Guangzhou, China. In Biochem Biophys Res Commun, 2012
these results suggest that PRAME plays an important role in cell proliferation and disease progression in osteosarcoma.
Activated human γδ T cells induce peptide-specific CD8+ T-cell responses to tumor-associated self-antigens.
Rossig et al., Münster, Germany. In Cancer Immunol Immunother, 2012
Studies suggest that activated human gammadelta T cells can efficiently present PRAME and STEAP1-derived epitopes and allow breaking tolerance against these tumor-associated self-antigens.
PRAME (preferentially expressed antigen of melanoma) is a novel marker for differentiating serous carcinoma from malignant mesothelioma.
Davidson et al., Oslo, Norway. In Am J Clin Pathol, 2012
PRAME effectively differentiates mullerian carcinoma from malignant mesothelioma at the mRNA and protein levels.
NYESO-1/LAGE-1s and PRAME are targets for antigen specific T cells in chondrosarcoma following treatment with 5-Aza-2-deoxycitabine.
Yee et al., Seattle, United States. In Plos One, 2011
NYESO-1/LAGE-1s and PRAME are targets for antigen specific T cells in chondrosarcoma following treatment with 5-Aza-2-deoxycitabine
[Advancement of peptide vaccines for hematologic malignancies].
Li et al., Guangzhou, China. In Zhongguo Shi Yan Xue Ye Xue Za Zhi, 2011
This review focuses on the late results of clinical trails of peptide vaccination protocols targeting WT1, RHAMM, BCR-ABL, PR1 in hematological malignancies and the development of specific immune responses to PRAME and Survivin peptides.
Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes.
Melief et al., Leiden, Netherlands. In Nat Immunol, 2011
Nardilysin and TOP were required, either together or alone, for the generation of a tumor-specific CTL epitope from PRAME, an immunodominant CTL epitope from Epstein-Barr virus protein EBNA3C, and a clinically important epitope from the melanoma protein MART-1.
Definition of a target for immunotherapy and results of the first Peptide vaccination study in chronic lymphocytic leukemia.
Giannopoulos et al., Lublin, Poland. In Transplant Proc, 2010
RHAMM/CD168, fibromodulin, PRAME, and MPP11 were expressed in CLL patients but not in healthy volunteers.
The human tumor antigen PRAME is a dominant repressor of retinoic acid receptor signaling.
Bernards et al., Amsterdam, Netherlands. In Cell, 2005
The overexpression of PRAME protein frequently observed in human cancers confers growth or survival advantages by antagonizing retinoic acid receptor(RAR) signaling.
Characterization of an antigen that is recognized on a melanoma showing partial HLA loss by CTL expressing an NK inhibitory receptor.
Coulie et al., Brussels, Belgium. In Immunity, 1997
A novel gene, PRAME, encodes the antigen.
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