Proteome Analyses Reveal Positive Association of COL2A1, MPO, TYMS, and IGFBP5 with Canine Mammary Gland Malignancy
Purpose To identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female dogs and include different types. Experimental design Frozen tissue specimens of normal mammary gland (n = 7), lobular hyperplasia (n = 6),...
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Published in | Proteomics. Clinical applications Vol. 13; no. 4; pp. e1800151 - n/a |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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01.07.2019
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Abstract | Purpose
To identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female dogs and include different types.
Experimental design
Frozen tissue specimens of normal mammary gland (n = 7), lobular hyperplasia (n = 6), simple carcinoma (n = 6), and complex carcinoma (n = 6) are collected from 11 CMT cases. Tissue homogenates are comparatively analyzed by the isobaric tags for relative and absolute quantification (iTRAQ) combined with LC‐MS/MS to identify proteins differentially expressed in different‐type CMT tissues.
Results
Among 3795 proteins identified and quantified among all groups, 133, 127, and 98 proteins are particularly overexpressed in simple carcinoma, complex carcinoma, and both types, respectively, compared with normal and hyperplastic tissues. Moreover, collagen type II alpha 1 chain (COL2A), myeloperoxidase (MPO), thymidylate synthetase (TYMS), and insulin‐like growth factor‐binding protein 5 (IGFBP5) are validated to be highly expressed in different‐type CMT tissues using immunoblotting and immunohistochemistry. Notably, COL2A1 and IGFBP5 levels are correlated with clinical stages.
Conclusions and clinical relevance
COL2A1, MPO, TYMS, and IGFBP5 protein levels are positively associated with CMT development. Data expedite further investigations to improve treatment regimens for CMT. |
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AbstractList | To identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female dogs and include different types.PURPOSETo identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female dogs and include different types.Frozen tissue specimens of normal mammary gland (n = 7), lobular hyperplasia (n = 6), simple carcinoma (n = 6), and complex carcinoma (n = 6) are collected from 11 CMT cases. Tissue homogenates are comparatively analyzed by the isobaric tags for relative and absolute quantification (iTRAQ) combined with LC-MS/MS to identify proteins differentially expressed in different-type CMT tissues.EXPERIMENTAL DESIGNFrozen tissue specimens of normal mammary gland (n = 7), lobular hyperplasia (n = 6), simple carcinoma (n = 6), and complex carcinoma (n = 6) are collected from 11 CMT cases. Tissue homogenates are comparatively analyzed by the isobaric tags for relative and absolute quantification (iTRAQ) combined with LC-MS/MS to identify proteins differentially expressed in different-type CMT tissues.Among 3795 proteins identified and quantified among all groups, 133, 127, and 98 proteins are particularly overexpressed in simple carcinoma, complex carcinoma, and both types, respectively, compared with normal and hyperplastic tissues. Moreover, collagen type II alpha 1 chain (COL2A), myeloperoxidase (MPO), thymidylate synthetase (TYMS), and insulin-like growth factor-binding protein 5 (IGFBP5) are validated to be highly expressed in different-type CMT tissues using immunoblotting and immunohistochemistry. Notably, COL2A1 and IGFBP5 levels are correlated with clinical stages.RESULTSAmong 3795 proteins identified and quantified among all groups, 133, 127, and 98 proteins are particularly overexpressed in simple carcinoma, complex carcinoma, and both types, respectively, compared with normal and hyperplastic tissues. Moreover, collagen type II alpha 1 chain (COL2A), myeloperoxidase (MPO), thymidylate synthetase (TYMS), and insulin-like growth factor-binding protein 5 (IGFBP5) are validated to be highly expressed in different-type CMT tissues using immunoblotting and immunohistochemistry. Notably, COL2A1 and IGFBP5 levels are correlated with clinical stages.COL2A1, MPO, TYMS, and IGFBP5 protein levels are positively associated with CMT development. Data expedite further investigations to improve treatment regimens for CMT.CONCLUSIONS AND CLINICAL RELEVANCECOL2A1, MPO, TYMS, and IGFBP5 protein levels are positively associated with CMT development. Data expedite further investigations to improve treatment regimens for CMT. Purpose To identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female dogs and include different types. Experimental design Frozen tissue specimens of normal mammary gland (n = 7), lobular hyperplasia (n = 6), simple carcinoma (n = 6), and complex carcinoma (n = 6) are collected from 11 CMT cases. Tissue homogenates are comparatively analyzed by the isobaric tags for relative and absolute quantification (iTRAQ) combined with LC‐MS/MS to identify proteins differentially expressed in different‐type CMT tissues. Results Among 3795 proteins identified and quantified among all groups, 133, 127, and 98 proteins are particularly overexpressed in simple carcinoma, complex carcinoma, and both types, respectively, compared with normal and hyperplastic tissues. Moreover, collagen type II alpha 1 chain (COL2A), myeloperoxidase (MPO), thymidylate synthetase (TYMS), and insulin‐like growth factor‐binding protein 5 (IGFBP5) are validated to be highly expressed in different‐type CMT tissues using immunoblotting and immunohistochemistry. Notably, COL2A1 and IGFBP5 levels are correlated with clinical stages. Conclusions and clinical relevance COL2A1, MPO, TYMS, and IGFBP5 protein levels are positively associated with CMT development. Data expedite further investigations to improve treatment regimens for CMT. To identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female dogs and include different types. Frozen tissue specimens of normal mammary gland (n = 7), lobular hyperplasia (n = 6), simple carcinoma (n = 6), and complex carcinoma (n = 6) are collected from 11 CMT cases. Tissue homogenates are comparatively analyzed by the isobaric tags for relative and absolute quantification (iTRAQ) combined with LC-MS/MS to identify proteins differentially expressed in different-type CMT tissues. Among 3795 proteins identified and quantified among all groups, 133, 127, and 98 proteins are particularly overexpressed in simple carcinoma, complex carcinoma, and both types, respectively, compared with normal and hyperplastic tissues. Moreover, collagen type II alpha 1 chain (COL2A), myeloperoxidase (MPO), thymidylate synthetase (TYMS), and insulin-like growth factor-binding protein 5 (IGFBP5) are validated to be highly expressed in different-type CMT tissues using immunoblotting and immunohistochemistry. Notably, COL2A1 and IGFBP5 levels are correlated with clinical stages. COL2A1, MPO, TYMS, and IGFBP5 protein levels are positively associated with CMT development. Data expedite further investigations to improve treatment regimens for CMT. PurposeTo identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female dogs and include different types.Experimental designFrozen tissue specimens of normal mammary gland (n = 7), lobular hyperplasia (n = 6), simple carcinoma (n = 6), and complex carcinoma (n = 6) are collected from 11 CMT cases. Tissue homogenates are comparatively analyzed by the isobaric tags for relative and absolute quantification (iTRAQ) combined with LC‐MS/MS to identify proteins differentially expressed in different‐type CMT tissues.ResultsAmong 3795 proteins identified and quantified among all groups, 133, 127, and 98 proteins are particularly overexpressed in simple carcinoma, complex carcinoma, and both types, respectively, compared with normal and hyperplastic tissues. Moreover, collagen type II alpha 1 chain (COL2A), myeloperoxidase (MPO), thymidylate synthetase (TYMS), and insulin‐like growth factor‐binding protein 5 (IGFBP5) are validated to be highly expressed in different‐type CMT tissues using immunoblotting and immunohistochemistry. Notably, COL2A1 and IGFBP5 levels are correlated with clinical stages.Conclusions and clinical relevanceCOL2A1, MPO, TYMS, and IGFBP5 protein levels are positively associated with CMT development. Data expedite further investigations to improve treatment regimens for CMT. |
Author | Liu, Hao‐Ping Wu, Chih‐Ching Chu, Hao‐Wei Chang, Shih‐Chieh Huang, Yenlin Zeng, Guang‐You |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30578659$$D View this record in MEDLINE/PubMed |
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Keywords | thymidylate synthetase canine mammary tumor insulin-like growth factor-binding protein 5 isobaric tags for relative and absolute quantification (iTRAQ) collagen type II alpha 1 chain |
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To identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female... To identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female dogs... PurposeTo identify aberrantly expressed proteins contributing to pathogenesis of canine mammary tumors (CMTs) which are the most prevalent neoplasms in female... |
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SubjectTerms | Animals Breast cancer canine mammary tumor Collagen (type II) Collagen Type II - metabolism collagen type II alpha 1 chain Design of experiments Dogs Female Growth factors Hyperplasia Immunoblotting Immunohistochemistry Insulin Insulin-Like Growth Factor Binding Protein 5 - metabolism Insulin-like growth factor-binding protein 5 isobaric tags for relative and absolute quantification (iTRAQ) Malignancy Mammary gland Mammary glands Mammary Neoplasms, Animal - metabolism Mammary Neoplasms, Animal - pathology Neoplasia Neoplasm Proteins - metabolism Neoplasms Pathogenesis Peroxidase Peroxidase - metabolism Proteins Proteome - metabolism Proteomes Thymidylate Synthase - metabolism thymidylate synthetase Tumors |
Title | Proteome Analyses Reveal Positive Association of COL2A1, MPO, TYMS, and IGFBP5 with Canine Mammary Gland Malignancy |
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