LC/MS-based quantitative proteomic analysis of paraffin-embedded archival melanomas reveals potential proteomic biomarkers associated with metastasis

Melanoma metastasis status is highly associated with the overall survival of patients; yet, little is known about proteomic changes during melanoma tumor progression. To better understand the changes in protein expression involved in melanoma progression and metastasis, and to identify potential bio...

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Veröffentlicht in:PloS one 2009-02, Vol.4 (2), p.e4430-e4430
Hauptverfasser: Huang, Sharon K, Darfler, Marlene M, Nicholl, Michael B, You, Jinsam, Bemis, Kerry G, Tegeler, Tony J, Wang, Mu, Wery, Jean-Pierre, Chong, Kelly K, Nguyen, Linhda, Scolyer, Richard A, Hoon, Dave S B
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container_title PloS one
container_volume 4
creator Huang, Sharon K
Darfler, Marlene M
Nicholl, Michael B
You, Jinsam
Bemis, Kerry G
Tegeler, Tony J
Wang, Mu
Wery, Jean-Pierre
Chong, Kelly K
Nguyen, Linhda
Scolyer, Richard A
Hoon, Dave S B
description Melanoma metastasis status is highly associated with the overall survival of patients; yet, little is known about proteomic changes during melanoma tumor progression. To better understand the changes in protein expression involved in melanoma progression and metastasis, and to identify potential biomarkers, we conducted a global quantitative proteomic analysis on archival metastatic and primary melanomas. A total of 16 metastatic and 8 primary cutaneous melanomas were assessed. Proteins were extracted from laser captured microdissected formalin fixed paraffin-embedded archival tissues by liquefying tissue cells. These preparations were analyzed by a LC/MS-based label-free protein quantification method. More than 1500 proteins were identified in the tissue lysates with a peptide ID confidence level of >75%. This approach identified 120 significant changes in protein levels. These proteins were identified from multiple peptides with high confidence identification and were expressed at significantly different levels in metastases as compared with primary melanomas (q-Value
doi_str_mv 10.1371/journal.pone.0004430
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To better understand the changes in protein expression involved in melanoma progression and metastasis, and to identify potential biomarkers, we conducted a global quantitative proteomic analysis on archival metastatic and primary melanomas. A total of 16 metastatic and 8 primary cutaneous melanomas were assessed. Proteins were extracted from laser captured microdissected formalin fixed paraffin-embedded archival tissues by liquefying tissue cells. These preparations were analyzed by a LC/MS-based label-free protein quantification method. More than 1500 proteins were identified in the tissue lysates with a peptide ID confidence level of &gt;75%. This approach identified 120 significant changes in protein levels. These proteins were identified from multiple peptides with high confidence identification and were expressed at significantly different levels in metastases as compared with primary melanomas (q-Value&lt;0.05). The differentially expressed proteins were classified by biological process or mapped into biological system networks, and several proteins were implicated by these analyses as cancer- or metastasis-related. These proteins represent potential biomarkers for tumor progression. 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To better understand the changes in protein expression involved in melanoma progression and metastasis, and to identify potential biomarkers, we conducted a global quantitative proteomic analysis on archival metastatic and primary melanomas. A total of 16 metastatic and 8 primary cutaneous melanomas were assessed. Proteins were extracted from laser captured microdissected formalin fixed paraffin-embedded archival tissues by liquefying tissue cells. These preparations were analyzed by a LC/MS-based label-free protein quantification method. More than 1500 proteins were identified in the tissue lysates with a peptide ID confidence level of &gt;75%. This approach identified 120 significant changes in protein levels. These proteins were identified from multiple peptides with high confidence identification and were expressed at significantly different levels in metastases as compared with primary melanomas (q-Value&lt;0.05). The differentially expressed proteins were classified by biological process or mapped into biological system networks, and several proteins were implicated by these analyses as cancer- or metastasis-related. These proteins represent potential biomarkers for tumor progression. 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To better understand the changes in protein expression involved in melanoma progression and metastasis, and to identify potential biomarkers, we conducted a global quantitative proteomic analysis on archival metastatic and primary melanomas. A total of 16 metastatic and 8 primary cutaneous melanomas were assessed. Proteins were extracted from laser captured microdissected formalin fixed paraffin-embedded archival tissues by liquefying tissue cells. These preparations were analyzed by a LC/MS-based label-free protein quantification method. More than 1500 proteins were identified in the tissue lysates with a peptide ID confidence level of &gt;75%. This approach identified 120 significant changes in protein levels. These proteins were identified from multiple peptides with high confidence identification and were expressed at significantly different levels in metastases as compared with primary melanomas (q-Value&lt;0.05). The differentially expressed proteins were classified by biological process or mapped into biological system networks, and several proteins were implicated by these analyses as cancer- or metastasis-related. These proteins represent potential biomarkers for tumor progression. The study successfully identified proteins that are differentially expressed in formalin fixed paraffin-embedded specimens of metastatic and primary melanoma.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>19221597</pmid><doi>10.1371/journal.pone.0004430</doi><tpages>e4430</tpages><oa>free_for_read</oa></addata></record>
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source Electronic Journals Library; Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; PubMed Central; Free Full-Text Journals in Chemistry
subjects Analysis
Animals
Biological activity
Biological markers
Biomarkers
Biomarkers, Tumor - analysis
Biotechnology/Protein Chemistry and Proteomics
Cancer
Cancer metastasis
Chromatography
Chromatography, Liquid - methods
Confidence intervals
Databases, Protein
Dehydrogenases
Formaldehyde
Gene expression
Humans
Hypoxia
Kinases
Leukemia
Liquefaction
Lysates
Mass spectrometry
Mass Spectrometry - methods
Melanoma
Melanoma - chemistry
Melanoma - pathology
Metabolism
Metastases
Metastasis
Molecular Sequence Data
Neoplasm Metastasis
Neoplasm Proteins - analysis
Oncology
Oncology/Skin Cancers
Paraffin
Paraffin Embedding
Pathology
Pathology/Molecular Pathology
Peptides
Physiology
Protein expression
Proteins
Proteome - analysis
Proteomics
Rodents
Scientific imaging
Tissues
Tumors
title LC/MS-based quantitative proteomic analysis of paraffin-embedded archival melanomas reveals potential proteomic biomarkers associated with metastasis
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