English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Metastatic prostate tumours are responsible for the majority of deaths associated with prostate cancer. The most frequent site of prostate cancer metastasis is to bone; over 80% of men who die of the disease have metastatic bony lesions (Bubendorf et al., 2000). Early detection of prostate cancer remains crucial to effective treatment. However, we are still unable to identify with certainty those tumours requiring aggressive and immediate interventions, which are associated with considerable morbidity, from those where a “watchful waiting” approach may be more appropriate. Currently little is known about inherited determinants of an individual’s propensity to develop tumours that rapidly progress and metastasise (Hunter, 2006). Experimental evidence investigating the role of integrins in tumourigenesis suggests that they play important roles in tumour progression and metastasis, particularly the development of metastatic lesions in bone. Notably, recent evidence indicates that genetic variants in selected integrins influence risk and/or prostate tumour behaviour. The integrins represent a large family of cell surface receptors that are responsible for cell to cell adhesion and complex formation with ligands found within the extracellular matrix (ECM). The integrins have important roles in cell proliferation, cell survival, differentiation and cell migration. Thus, these adhesion receptors play important roles in many physiological processes including normal organ development and wound healing. Integrins are obligate, noncovalent, heterodimeric molecules, composed of a larger α subunit and a smaller β subunit. Each of the subunits extends from within the cytoplasm into the ECM. The ECM tail of the α and β subunits are approximately 700-1000 amino acid residues in length, and the cell membrane is spanned by approximately 20-24 residues. Integrin subunits have a short cytoplasmic tail, approximately 15-58 residues in length, with the exception of β4 which has a cytoplasmic tail approximately 1000 residues (Alghisi and Ruegg, 2006). Within the cytosol they are attached to the cytoskeleton via talin-actin microfilaments. A detailed review on integrin structure can be found in the following publications (Buckley et al., 1999; Humphries et al., 2003; Ivaska and Heino, 2000; Lu et al., 2008). The conservation of integrin structure from more primitive through to higher order organisms highlights their importance to multicellular organisms (Burke, 1999). Upon

Integrins as Determinants of Genetic Susceptibility, Tumour Behaviour and Their Potential as Therapeutic Targets