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This Article Full Text Full Text (PDF) All Versions of this Article: ERC-08-0179v1 ERC-08-0179v2 16/1/1    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Alam, S. M. Articles by Lin, M.-F. Search for Related Content PubMed PubMed Citation Articles by Alam, S. M. Articles by Lin, M.-F.

¹ Department of Biochemistry and Molecular Biology, College of Medicine, University of Nebraska Medical Center, 985870 Nebraska Medical Center, Omaha, Nebraska 68198-5870, USA² Eppley Institute for Cancer Research, University of Nebraska Medical Center, Omaha, Nebraska 68198, USA

(Correspondence should be addressed to M-F Lin; Email: mlin{at}unmc.edu)

^* S M Alam and M Rajendran contributed equally to this work

Tyrosine phosphorylation plays a critical role in growth regulation, and its aberrant regulation can be involved in carcinogenesis. The association of Shc (Src homolog and collagen homolog) adaptor protein family members in tyrosine phosphorylation signaling pathway is well recognized. Shc adaptor proteins transmit activated tyrosine phosphorylation signaling that suggest their plausible role in growth regulation including carcinogenesis and metastasis. In parallel, by sharing a similar mechanism of carcinogenesis, the steroids are involved in the early stage of carcinogenesis as well as the regulation of cancer progression and metastatic processes. Recent evidence indicates a cross-talk between tyrosine phosphorylation signaling and steroid hormone action in epithelial cells, including prostate and breast cancer cells. Therefore, the members of Shc proteins may function as mediators between tyrosine phosphorylation and steroid signaling in steroid-regulated cell proliferation and carcinogenesis. In this communication, we discuss the novel roles of Shc proteins, specifically p52^Shc and p66^Shc, in steroid hormone-regulated cancers and a novel molecular mechanism by which redox signaling induced by p66^Shc mediates steroid action via a non-genomic pathway. The p66^Shc protein may serve as an effective biomarker for predicting cancer prognosis as well as a useful target for treatment.