Among integrin receptors, several bind to laminins, major compone

Among integrin receptors, several bind to laminins, major components of the basal lamina. In particular, integrin alpha6 beta1 and alpha6 beta4 can bind to laminins 111, 332 and 511. A specific feature of integrin alpha6 beta4 is its participation to hemidesmosomes, anchorage junctions found in epithelia (skin, intestine), which are the devices by which epithelial cells attach to the basal lamina. In the cells, molecular interactions of alpha6 beta4 with plakins results ultimately

with the establishment of a connection with the keratin intermediate filament network. Hemidesmosomes provide cells with resistance against mechanical stress, and it has been largely documented that molecular alterations of hemidesmosomal composition leads to tissue integrity ATM Kinase Inhibitor mw defects such as epidermolysis bullosa. In

addition to this structural role, hemidesmosomes are also signalling entities since plakins or integrin cytoplasmic tails recruit signalling Selleckchem Capmatinib molecules. By regulating cell fundamental behaviours (adhesion, migration, proliferation, survival), integrin signalling pathways contribute to the control of tissue integrity and homeostasis. To be able to analyze the functions and signalling these of integrin alpha6 beta4 in vivo in different tissues, we have generated a conditional integrin alpha6-floxed mutant line. We are using this mouse model to study the functional role of integrin alpha6 beta4 in intestinal physiology and pathology. Poster No. 66 CD151 Expression and Prostate cancer Progression Sujitra Detchokul 1 , Bradley Newell1, Jian Ang1, Michael W. Parker2, Elizabeth D. Williams3, Albert G. Frauman1 1 Department of Medicine (Austin Health/Northern Health), The University of Melbourne, Heidelberg, Victoria, Australia, 2

Structural Biology Laboratory, St. Vincent’s Institute of Medical Research, Melbourne, Victoria, Australia, 3 Monash Institute of Medical Research, Monash University, Clayton, Victoria, Australia Despite improvement in earlier detection and treatment, prostate cancer (PCa) still remains a leading cause of death in most Western countries. CD151, a member of the tetraspanin superfamily is involved in cell signaling, cell motility, cell adhesion, and tumour metastasis by acting as a molecular facilitator recruiting groups of specific cell-surface proteins and thus stabilizing functional signaling complexes1. CD151 was identified to be the first tetraspanin member to be linked as a promoter of metastasis2.

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