Identification of collapsin response mediator protein-2 as a potential marker of colorectal carcinoma by comparative analysis of cancer cell secretomes

The cancer cell secretome may contain many potentially useful biomarkers. We therefore sought to identify proteins in the conditioned media of colorectal carcinoma (CRC) cell lines but not in those from other cancer cell lines. The secretomes of 21 cancer cell lines derived from 12 cancer types were...

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Published inProteomics (Weinheim) Vol. 8; no. 2; pp. 316 - 332
Main Authors Wu, Chih-Ching, Chen, Hua-Chien, Chen, Su-Jen, Liu, Hao-Ping, Hsieh, Yi-Yueh, Yu, Chia-Jung, Tang, Reiping, Hsieh, Ling-Ling, Yu, Jau-Song, Chang, Yu-Sun
Format Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 01.01.2008
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Abstract The cancer cell secretome may contain many potentially useful biomarkers. We therefore sought to identify proteins in the conditioned media of colorectal carcinoma (CRC) cell lines but not in those from other cancer cell lines. The secretomes of 21 cancer cell lines derived from 12 cancer types were analyzed by SDS-PAGE combined with MALDI-TOF MS. Among the 325 proteins identified, collapsin response mediator protein-2 (CRMP-2) was chosen for evaluation as a potential CRC biomarker, since it was selectively detected in the CRC cell line secretome and has never been reported as a cancer biomarker. Immunohistochemical analysis of 169 CRC specimens showed that CRMP-2 was positively detected in 58.6% of the tumors, but weakly or not detected in >90% of the adjacent nontumor epithelial cells. Moreover, the CRMP-2-positive rate was significantly increased in earlier stage tumors and lymph node metastasis. Plasma CRMP-2 levels were significantly higher in CRC patients (N = 201) versus healthy controls (N = 201) (61.3 ± 34.6 vs. 40.2 ± 24.3 ng/mL, p = 0.001). Our results indicate that comparative analysis of cancer cell secretome is a feasible strategy for identifying potential cancer biomarkers, and that CRMP-2 may be a novel CRC biomarker.
AbstractList The cancer cell secretome may contain many potentially useful biomarkers. We therefore sought to identify proteins in the conditioned media of colorectal carcinoma (CRC) cell lines but not in those from other cancer cell lines. The secretomes of 21 cancer cell lines derived from 12 cancer types were analyzed by SDS-PAGE combined with MALDI-TOF MS. Among the 325 proteins identified, collapsin response mediator protein-2 (CRMP-2) was chosen for evaluation as a potential CRC biomarker, since it was selectively detected in the CRC cell line secretome and has never been reported as a cancer biomarker. Immunohistochemical analysis of 169 CRC specimens showed that CRMP-2 was positively detected in 58.6% of the tumors, but weakly or not detected in >90% of the adjacent nontumor epithelial cells. Moreover, the CRMP-2-positive rate was significantly increased in earlier stage tumors and lymph node metastasis. Plasma CRMP-2 levels were significantly higher in CRC patients (N = 201) versus healthy controls (N = 201) (61.3 +/- 34.6 vs. 40.2 +/- 24.3 ng/mL, p = 0.001). Our results indicate that comparative analysis of cancer cell secretome is a feasible strategy for identifying potential cancer biomarkers, and that CRMP-2 may be a novel CRC biomarker.The cancer cell secretome may contain many potentially useful biomarkers. We therefore sought to identify proteins in the conditioned media of colorectal carcinoma (CRC) cell lines but not in those from other cancer cell lines. The secretomes of 21 cancer cell lines derived from 12 cancer types were analyzed by SDS-PAGE combined with MALDI-TOF MS. Among the 325 proteins identified, collapsin response mediator protein-2 (CRMP-2) was chosen for evaluation as a potential CRC biomarker, since it was selectively detected in the CRC cell line secretome and has never been reported as a cancer biomarker. Immunohistochemical analysis of 169 CRC specimens showed that CRMP-2 was positively detected in 58.6% of the tumors, but weakly or not detected in >90% of the adjacent nontumor epithelial cells. Moreover, the CRMP-2-positive rate was significantly increased in earlier stage tumors and lymph node metastasis. Plasma CRMP-2 levels were significantly higher in CRC patients (N = 201) versus healthy controls (N = 201) (61.3 +/- 34.6 vs. 40.2 +/- 24.3 ng/mL, p = 0.001). Our results indicate that comparative analysis of cancer cell secretome is a feasible strategy for identifying potential cancer biomarkers, and that CRMP-2 may be a novel CRC biomarker.
The cancer cell secretome may contain many potentially useful biomarkers. We therefore sought to identify proteins in the conditioned media of colorectal carcinoma (CRC) cell lines but not in those from other cancer cell lines. The secretomes of 21 cancer cell lines derived from 12 cancer types were analyzed by SDS‐PAGE combined with MALDI‐TOF MS. Among the 325 proteins identified, collapsin response mediator protein‐2 (CRMP‐2) was chosen for evaluation as a potential CRC biomarker, since it was selectively detected in the CRC cell line secretome and has never been reported as a cancer biomarker. Immunohistochemical analysis of 169 CRC specimens showed that CRMP‐2 was positively detected in 58.6% of the tumors, but weakly or not detected in >90% of the adjacent nontumor epithelial cells. Moreover, the CRMP‐2‐positive rate was significantly increased in earlier stage tumors and lymph node metastasis. Plasma CRMP‐2 levels were significantly higher in CRC patients ( N  = 201) versus healthy controls ( N  = 201) (61.3 ± 34.6 vs. 40.2 ± 24.3 ng/mL, p  = 0.001). Our results indicate that comparative analysis of cancer cell secretome is a feasible strategy for identifying potential cancer biomarkers, and that CRMP‐2 may be a novel CRC biomarker.
The cancer cell secretome may contain many potentially useful biomarkers. We therefore sought to identify proteins in the conditioned media of colorectal carcinoma (CRC) cell lines but not in those from other cancer cell lines. The secretomes of 21 cancer cell lines derived from 12 cancer types were analyzed by SDS-PAGE combined with MALDI-TOF MS. Among the 325 proteins identified, collapsin response mediator protein-2 (CRMP-2) was chosen for evaluation as a potential CRC biomarker, since it was selectively detected in the CRC cell line secretome and has never been reported as a cancer biomarker. Immunohistochemical analysis of 169 CRC specimens showed that CRMP-2 was positively detected in 58.6% of the tumors, but weakly or not detected in >90% of the adjacent nontumor epithelial cells. Moreover, the CRMP-2-positive rate was significantly increased in earlier stage tumors and lymph node metastasis. Plasma CRMP-2 levels were significantly higher in CRC patients (N = 201) versus healthy controls (N = 201) (61.3 ± 34.6 vs. 40.2 ± 24.3 ng/mL, p = 0.001). Our results indicate that comparative analysis of cancer cell secretome is a feasible strategy for identifying potential cancer biomarkers, and that CRMP-2 may be a novel CRC biomarker.
The cancer cell secretome may contain many potentially useful biomarkers. We therefore sought to identify proteins in the conditioned media of colorectal carcinoma (CRC) cell lines but not in those from other cancer cell lines. The secretomes of 21 cancer cell lines derived from 12 cancer types were analyzed by SDS-PAGE combined with MALDI-TOF MS. Among the 325 proteins identified, collapsin response mediator protein-2 (CRMP-2) was chosen for evaluation as a potential CRC biomarker, since it was selectively detected in the CRC cell line secretome and has never been reported as a cancer biomarker. Immunohistochemical analysis of 169 CRC specimens showed that CRMP-2 was positively detected in 58.6% of the tumors, but weakly or not detected in >90% of the adjacent nontumor epithelial cells. Moreover, the CRMP-2-positive rate was significantly increased in earlier stage tumors and lymph node metastasis. Plasma CRMP-2 levels were significantly higher in CRC patients (N = 201) versus healthy controls (N = 201) (61.3 +/- 34.6 vs. 40.2 +/- 24.3 ng/mL, p = 0.001). Our results indicate that comparative analysis of cancer cell secretome is a feasible strategy for identifying potential cancer biomarkers, and that CRMP-2 may be a novel CRC biomarker.
Author Chen, Su-Jen
Chang, Yu-Sun
Wu, Chih-Ching
Tang, Reiping
Liu, Hao-Ping
Yu, Jau-Song
Chen, Hua-Chien
Hsieh, Yi-Yueh
Yu, Chia-Jung
Hsieh, Ling-Ling
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  fullname: Chang, Yu-Sun
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https://www.ncbi.nlm.nih.gov/pubmed/18203259$$D View this record in MEDLINE/PubMed
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Issue 2
Keywords Rectal disease
Colorectal carcinoma
Colorectal cancer
Identification
Secretome
Malignant tumor
CRMP-2
Protein
Colonic disease
Tumor marker
Proteomics
Digestive diseases
Intestinal disease
Cancer
Language English
License CC BY 4.0
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Chang Gung University and Memorial Hospital - No. CMRPD32038; No. CMRPD140041
National Science Council of Taiwan - No. NSC94-2745-B-182-003-URD
Additional corresponding author
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PMID 18203259
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  year: 2008
  text: 2008-01-01
  day: 01
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PublicationTitle Proteomics (Weinheim)
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PublicationYear 2008
Publisher Wiley-VCH Verlag
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WILEY‐VCH Verlag
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Snippet The cancer cell secretome may contain many potentially useful biomarkers. We therefore sought to identify proteins in the conditioned media of colorectal...
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SubjectTerms Analytical, structural and metabolic biochemistry
Biological and medical sciences
Biomarkers, Tumor - analysis
Cell Line, Tumor
Colorectal carcinoma
Colorectal Neoplasms - secretion
CRMP-2
Electrophoresis, Polyacrylamide Gel
Female
Fundamental and applied biological sciences. Psychology
Gastroenterology. Liver. Pancreas. Abdomen
Humans
Intercellular Signaling Peptides and Proteins - analysis
Male
Medical sciences
Middle Aged
Miscellaneous
Nerve Tissue Proteins - analysis
Proteins
Proteome - analysis
Secretome
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Stomach. Duodenum. Small intestine. Colon. Rectum. Anus
Tumor marker
Tumors
Title Identification of collapsin response mediator protein-2 as a potential marker of colorectal carcinoma by comparative analysis of cancer cell secretomes
URI https://api.istex.fr/ark:/67375/WNG-KKBTL792-L/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fpmic.200700819
https://www.ncbi.nlm.nih.gov/pubmed/18203259
https://www.proquest.com/docview/47534293
https://www.proquest.com/docview/70238403
Volume 8
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