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Differential occurrence of S 100 A 7 in breast cancer tissues: A proteomic‐based investigation
Author(s) -
Cancemi Patrizia,
Di Cara Gianluca,
Albanese Nadia Ninfa,
Costantini Francesca,
Marabeti Maria Rita,
Musso Rosa,
Riili Ignazio,
Lupo Carmelo,
Roz Elena,
PucciMinafra Ida
Publication year - 2012
Publication title -
proteomics – clinical applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.948
H-Index - 54
eISSN - 1862-8354
pISSN - 1862-8346
DOI - 10.1002/prca.201100072
Subject(s) - gene isoform , proteomics , breast cancer , heat shock protein , biology , blot , subcellular localization , in silico , protein isoform , cancer , immunohistochemistry , cancer research , microbiology and biotechnology , biochemistry , cytoplasm , immunology , gene , alternative splicing , genetics
Purpose The present study reports for the first time a large‐scale proteomic screening of the occurrence, subcellular localization and relative quantification of the S 100 A 7 protein among a group of 100 patients, clinically grouped for the diagnosis of infiltrating ductal carcinoma ( IDC ). Experimental design To this purpose, the methods of differential proteomics, W estern blotting, and immunohistochemistry were used. Results The identity of two isoforms of the protein was assessed by mass spectrometry and immunologically confirmed. Moreover, we proved by immunocytochemical applications the exclusive localization of the protein within the neoplastic cells. The correlation of S 100 A 7 expression levels with the collective profile of cancer patients’ proteomics predicted functional interactions, distinct for the two isoforms. The S 100 A 7 b isoform was significantly correlated with specific protein clusters (calcium binding, signaling and cell motion, heat shock and folding) and intercrossing pathways (antioxidant, metabolic and apoptotic pathways), while the more acidic isoform was correlated with a narrow number of proteins mainly unrelated to the b isoform. Conclusions and clinical relevance This study is the first proteomic‐based report on S 100 A 7 in a large series of IDC patients. The correlation with in silico data may significantly contribute the knowledge of possible pathways for S 100 A 7, providing novel insights into the mechanism of action of this protein. We suggest that each S 100 A 7 isoform is involved in critical phases of the breast cancer growth and progression, probably through interaction with different partner proteins.