Molecular Playground/IntegrinBeta1: Difference between revisions

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Integrins are a class of surface proteins that bind to extracellular matrix components and transmit chemical and mechanical cues to internal signaling pathways. Integrin beta 1 binds many proteins when dimerized with an alpha subunit, including collagen, laminin and fibronectin.  Integrin adhesion to the extra cellular matrix is key for cell ability to adhere, migrate and proliferate in both 2D and 3D systems. These will eventually form adhesion complexes, which regulate actomyocin polymerization. During migration, cells continually form new focal adhesions at the leading edge of the cell and release adhesion complexes at the back of the cell, enabling forward movement.
Integrins are a class of surface proteins that bind to extracellular matrix components and transmit chemical and mechanical cues to internal signaling pathways. Integrin beta 1 binds many proteins when dimerized with an alpha subunit, including collagen, laminin and fibronectin.  Integrin adhesion to the extra cellular matrix is key for cell ability to adhere, migrate and proliferate in both 2D and 3D systems. These will eventually form adhesion complexes, which regulate actomyocin polymerization. During migration, cells continually form new focal adhesions at the leading edge of the cell and release adhesion complexes at the back of the cell, enabling forward movement.


Here are the <scene name='60/609772/N-acetyl-d-glucosamine/2'>N-acetyl-d-glucosamine locations!</scene> N-acetyl-D-glucosamine may regulate integrin signaling during cancer cell migration.[1]
Here are the <scene name='60/609772/N-acetyl-d-glucosamine/2'>N-acetyl-d-glucosamine locations!</scene> N-acetyl-D-glucosamine may regulate integrin signaling during cancer cell migration<ref>PMID:19755493</ref>.


==Integrins and cancer==
==Integrins and cancer==


Integrins binding to the extracellular matrix provide cells the ability to migrate and remodel the surrounding microenvironment. Integrins are extremely important in cancer metastasis and the progression of solid tumors. Cells bind to extracellular matrix proteins, like<scene name='60/609772/Rgd_bound/2'> peptide RGD (black) on fibronectin</scene>, with integrins to stimulate survival, migration/invasion, and proliferation  [2]. Though high expression of integrin beta 1 has been shown to drive primary tumor progression and metastasis, targeting integrins for cancer treatment has seen limited clinical efficacy [3]. These failures stem from differential integrin expression between cancer cells, but new technologies to screen cancer cell populations are being developed to affective therapies on a patient-specific level [4]. These technologies will likely allow for more selective treatment and better clinical efficacy for integrin inhibitors.  
Integrins binding to the extracellular matrix provide cells the ability to migrate and remodel the surrounding microenvironment. Integrins are extremely important in cancer metastasis and the progression of solid tumors. Cells bind to extracellular matrix proteins, like<scene name='60/609772/Rgd_bound/2'> peptide RGD (black) on fibronectin</scene>, with integrins to stimulate survival, migration/invasion, and proliferation  <ref>PMID:20029421</ref>. Though high expression of integrin beta 1 has been shown to drive primary tumor progression and metastasis, targeting integrins for cancer treatment has seen limited clinical efficacy <ref>PMID:22894137</ref>. These failures stem from differential integrin expression between cancer cells, but new technologies to screen cancer cell populations are being developed to affective therapies on a patient-specific level <ref> Barney LE, Dandley EC, Jansen LE, Reich NG, Mercurio AM, Peyton SR. “A Cell-ECM Screening Method to Predict Breast Cancer Metastasis”. (2014) In Review.</ref>. These technologies will likely allow for more selective treatment and better clinical efficacy for integrin inhibitors.  


==Studying Integrin Beta-1'' in vitro''==
==Studying Integrin Beta-1'' in vitro''==
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==References==
==References==
<references/>
<references/>
[1] C. Saravanan, F. Liu, I.K. Gipson and N. Panjwani1. Galectin-3 promotes lamellipodia formation in epithelial cells by interacting with complex N-glycans on 31 integrin. Journal of Cell Science 122, 3684-3693 Published by The Company of Biologists (2009). doi:10.1242/jcs.045674.
[2] Desgrossellier JS,  and Cheresh DA. Integrins in cancer: biological implications and therapeutic opportunities. Nature Reviews Cancer 10, 9-22 (January 2010) | doi:10.1038/nrc2748
[3]Dos Santos PB, Zanetti JS, Ribeiro-Silva A, Beltrão EIC. Beta 1 integrin predicts survival in breast cancer: a clinicopathological and immunohistochemical study. Diagn Pathol 7:104.(2012)
[4] Barney LE, Dandley EC, Jansen LE, Reich NG, Mercurio AM, Peyton SR. “A Cell-ECM Screening Method to Predict Breast Cancer Metastasis”. (2014) In Review.