Publication: Focal adhesion kinase and cancer
Authors
Golubovskaya1, Vita M. ; Kweh, Frederick A. ; Cance, William G.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase that resides at the sites of
integrin clustering, known as focal adhesions. The FAK
protein has a molecular mass of 125kDa and is encoded
by the FAK gene located on human chromosome 8q24.
Structurally, FAK consists of an amino-terminal
regulatory FERM domain, a central catalytic kinase
domain, two proline-rich motifs, and a carboxy-terminal
focal adhesion targeting domain. FAK has been shown to
be an important mediator of cell growth, cell
proliferation, cell survival and cell migration, all of
which are often dysfunctional in cancer cells. Our lab
was the first to isolate FAK from primary human tissue
and link it to the process of tumorigenesis. We analyzed
FAK mRNA expression in normal, invasive and
metastatic human tissues and demonstrated through
Northern blot analysis that normal tissues had very low
levels of FAK mRNA while primary and metastatic
tumors significantly overexpressed FAK. We also
demonstrated and confirmed FAK overexpression in
colorectal carcinoma and liver metastases with real-time
PCR. In this review we summarized immunohistochemical data of FAK expression and role in
different cancer types tumors and discussed FAK
inhibition therapy approaches.
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