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Calpain Protease Regulates Cellular Mechanics

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Metastatic tumor progression, the process by which tumor cells disseminate from their primary site of development, is dependent upon the disruption of both cell-cell and cell-matrix adhesions. These in turn are governed by the multiprotein complexes of Cadherin-dependent adheren junctions and integrin-linked FA (Focal Adhesion) attachment sites. Disruption of these complexes leads to enhanced cell motility and invasion of the surrounding tissue matrix. Calpain-mediated proteolytic degradation of the Cadherin and FA complexes represent a mechanism for disassembly of these complexes (Ref.1).

Calpains are a highly conserved family of intracellular, non-lysosomal, calcium-dependent cysteine proteinases with numerous isoforms in organisms ranging from mammals to Drosophila melanogaster and Caenorhabditis elegans and with homologs in yeast and bacteria. They function in Ca2+ signaling by [...]


1.Cleavage of focal adhesion kinase by different proteases during SRC-regulated transformation and apoptosis. Distinct roles for calpain and caspases.
Carragher NO, Fincham VJ, Riley D, Frame MC.
J Biol Chem. 2001 Feb 9; 276(6): 4270-5.
2.A Ca (2+) switch aligns the active site of calpain.
Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL.
Cell. 2002 Mar 8; 108(5): 649-60.
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