Contributions of integrin-linked kinase to breast cancer metastasis and tumourigenesis

DSpace/Manakin Repository

Contributions of integrin-linked kinase to breast cancer metastasis and tumourigenesis

Citable link to this page

 

 
Title: Contributions of integrin-linked kinase to breast cancer metastasis and tumourigenesis
Author: Hinton, Cimona V; Avraham, Shalom; Avraham, Hava Karsenty

Note: Order does not necessarily reflect citation order of authors.

Citation: Hinton, Cimona V, Shalom Avraham, and Hava Karsenty Avraham. 2008. “Contributions of integrin-linked kinase to breast cancer metastasis and tumourigenesis.” Journal of Cellular and Molecular Medicine 12 (5a): 1517-1526. doi:10.1111/j.1582-4934.2008.00300.x. http://dx.doi.org/10.1111/j.1582-4934.2008.00300.x.
Full Text & Related Files:
Abstract: Abstract Metastasis contributes to more than 90% of mortality in breast cancer. Critical stages in the development of aggressive breast cancer include growth of the primary tumours, and their abilities to spread to distant organs, colonize and establish an independent blood supply. The integrin family of cell adhesion receptors is essential to breast cancer progression. Furthermore, integrin-linked kinase can ‘convert’ localized breast cancer cells into invasive and metastatic cells. Upon stimulation by growth factors and chemokine ligands, integrin-linked kinase mediates the phosphorylation of Akt Ser473, and glycogen synthase kinase-3. The current notion is that overexpression of integrin-linked kinase resulted in an invasive, metastatic phenotype in several cancer model systems in vivo and in vitro, thus, implicating a role for integrin-linked kinase in oncogenic transformation, angiogenesis and metastasis. Here, we will review the role of integrin-linked kinase in breast cancer metastasis. Elucidation of signalling events important for breast tumour metastasis should provide insights into successful breast cancer therapies.
Published Version: doi:10.1111/j.1582-4934.2008.00300.x
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3918067/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:15035058
Downloads of this work:

Show full Dublin Core record

This item appears in the following Collection(s)

 
 

Search DASH


Advanced Search
 
 

Submitters