Expression profiling identifies new function of collapsin response mediator protein 4 as a metastasis-suppressor in prostate cancer

Metastasis is the chief cause of mortality from cancer, but the mechanisms leading to metastasis are poorly understood. We used a proteomics approach to screen for metastasis-associated proteins and found that collapsin response mediator protein-4 (CRMP4) expression was inversely associated with the...

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Published inOncogene Vol. 29; no. 32; pp. 4555 - 4566
Main Authors Gao, X, Pang, J, Li, L-Y, Liu, W-P, Di, J-M, Sun, Q-P, Fang, Y-Q, Liu, X-P, Pu, X-Y, He, D, Li, M-T, Su, Z-L, Li, B-Y
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Published London Nature Publishing Group UK 12.08.2010
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Abstract Metastasis is the chief cause of mortality from cancer, but the mechanisms leading to metastasis are poorly understood. We used a proteomics approach to screen for metastasis-associated proteins and found that collapsin response mediator protein-4 (CRMP4) expression was inversely associated with the lymph node metastasis of prostate cancer (PCa). Subsequent in vitro and in vivo studies revealed that overexpression of CRMP4 not only suppressed the invasion ability of PCa cells, but also strongly inhibited tumor metastasis in an animal model. Furthermore, methylation of a CpG island within the promoter region of the CRMP4 gene is responsible for downregulation of CRMP4 expression. Thus, in this study, we show new function of CRMP4 as a metastasis-suppressor in PCa. The findings provide new mechanistic insights into metastasis and therapeutic potential for this most common male cancer.
AbstractList Metastasis is the chief cause of mortality from cancer, but the mechanisms leading to metastasis are poorly understood. We used a proteomics approach to screen for metastasis-associated proteins and found that collapsin response mediator protein-4 (CRMP4) expression was inversely associated with the lymph node metastasis of prostate cancer (PCa). Subsequent in vitro and in vivo studies revealed that overexpression of CRMP4 not only suppressed the invasion ability of PCa cells, but also strongly inhibited tumor metastasis in an animal model. Furthermore, methylation of a CpG island within the promoter region of the CRMP4 gene is responsible for downregulation of CRMP4 expression. Thus, in this study, we show new function of CRMP4 as a metastasis-suppressor in PCa. The findings provide new mechanistic insights into metastasis and therapeutic potential for this most common male cancer.
Metastasis is the chief cause of mortality from cancer, but the mechanisms leading to metastasis are poorly understood. We used a proteomics approach to screen for metastasis-associated proteins and found that collapsin response mediator protein-4 (CRMP4) expression was inversely associated with the lymph node metastasis of prostate cancer (PCa). Subsequent in vitro and in vivo studies revealed that overexpression of CRMP4 not only suppressed the invasion ability of PCa cells, but also strongly inhibited tumor metastasis in an animal model. Furthermore, methylation of a CpG island within the promoter region of the CRMP4 gene is responsible for downregulation of CRMP4 expression. Thus, in this study, we show new function of CRMP4 as a metastasis-suppressor in PCa. The findings provide new mechanistic insights into metastasis and therapeutic potential for this most common male cancer.
Metastasis is the chief cause of mortality from cancer, but the mechanisms leading to metastasis are poorly understood. We used a proteomics approach to screen for metastasis-associated proteins and found that collapsin response mediator protein-4 (CRMP4) expression was inversely associated with the lymph node metastasis of prostate cancer (PCa). Subsequent in vitro and in vivo studies revealed that overexpression of CRMP4 not only suppressed the invasion ability of PCa cells, but also strongly inhibited tumor metastasis in an animal model. Furthermore, methylation of a CpG island within the promoter region of the CRMP4 gene is responsible for downregulation of CRMP4 expression. Thus, in this study, we show new function of CRMP4 as a metastasis-suppressor in PCa. The findings provide new mechanistic insights into metastasis and therapeutic potential for this most common male cancer. [PUBLICATION ABSTRACT]
Metastasis is the chief cause of mortality from cancer, but the mechanisms leading to metastasis are poorly understood. We used a proteomics approach to screen for metastasis-associated proteins and found that collapsin response mediator protein-4 (CRMP4) expression was inversely associated with the lymph node metastasis of prostate cancer (PCa). Subsequent in vitro and in vivo studies revealed that overexpression of CRMP4 not only suppressed the invasion ability of PCa cells, but also strongly inhibited tumor metastasis in an animal model. Furthermore, methylation of a CpG island within the promoter region of the CRMP4 gene is responsible for downregulation of CRMP4 expression. Thus, in this study, we show new function of CRMP4 as a metastasis-suppressor in PCa. The findings provide new mechanistic insights into metastasis and therapeutic potential for this most common male cancer. Oncogene (2010) 29, 4555-566; doi: 10.1038/onc.2010.213; published online 14 June 2010 Keywords: prostate cancer; proteomics; collapsin response mediator protein-4; metastasis-suppressor gene; methylation
Audience Academic
Author Di, J-M
Fang, Y-Q
Li, M-T
Liu, W-P
Li, L-Y
Liu, X-P
Su, Z-L
He, D
Pang, J
Gao, X
Pu, X-Y
Sun, Q-P
Li, B-Y
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  surname: Li
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  organization: Department of Urology, University of Kansas Medical Center
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Issue 32
Keywords prostate cancer
proteomics
collapsin response mediator protein-4
methylation
metastasis-suppressor gene
Urinary system disease
Prostate disease
Identification
Malignant tumor
Metastasis
Carcinogenesis
Protein
Gene expression profile
Metastasis suppressor gene
Proteomics
Methylation
Male genital diseases
Prostate cancer
Cancer
Language English
License CC BY 4.0
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    fullname: JC Brandes
– volume: 13
  start-page: 1303
  year: 2004
  ident: BFonc2010213_CR29
  publication-title: Hum Mol Genet
  doi: 10.1093/hmg/ddh155
  contributor:
    fullname: PL Paris
– volume: 8
  start-page: 828
  year: 2002
  ident: BFonc2010213_CR43
  publication-title: Clin Cancer Res
  contributor:
    fullname: K Uzawa
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Snippet Metastasis is the chief cause of mortality from cancer, but the mechanisms leading to metastasis are poorly understood. We used a proteomics approach to screen...
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SubjectTerms 631/337/475
631/67/322
631/67/589/466
Animal models
Animals
Apoptosis
Biological and medical sciences
Care and treatment
Cell Biology
Cell Line, Tumor
Cell physiology
Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes
Cellular proteins
CpG islands
CpG Islands - genetics
Development and progression
DNA Methylation
Electrophoresis, Gel, Two-Dimensional
Fundamental and applied biological sciences. Psychology
Gene expression
Gene Expression Profiling
Gene Expression Regulation, Neoplastic
Genetic aspects
Genetics
Gynecology. Andrology. Obstetrics
Health aspects
Human Genetics
Humans
Internal Medicine
Lymph nodes
Lymphatic Metastasis
Male
Male genital diseases
Mediator protein
Medical sciences
Medicine
Medicine & Public Health
Metastases
Metastasis
Mice
Molecular and cellular biology
Mortality
Muscle Proteins - genetics
Muscle Proteins - metabolism
Nephrology. Urinary tract diseases
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Oncology
original-article
Promoter Regions, Genetic - genetics
Prostate cancer
Prostatic Neoplasms - genetics
Prostatic Neoplasms - pathology
Prostatic Neoplasms - surgery
Proteomics
Recurrence
Reproducibility of Results
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tumors
Tumors of the urinary system
Urinary tract. Prostate gland
Vascular Endothelial Growth Factor A - metabolism
Title Expression profiling identifies new function of collapsin response mediator protein 4 as a metastasis-suppressor in prostate cancer
URI http://dx.doi.org/10.1038/onc.2010.213
https://link.springer.com/article/10.1038/onc.2010.213
https://www.ncbi.nlm.nih.gov/pubmed/20543870
https://www.proquest.com/docview/2641406970
https://www.proquest.com/docview/742648326
https://search.proquest.com/docview/748942540
https://search.proquest.com/docview/754889845
Volume 29
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