Disease relevance of Capn2

• In the presence of CaCl2, CANP1 and CANP3 were autolyzed very rapidly, whereas the autolysis of CANP2 was slow and gradual [1].
• Cyclin E both regulates and is regulated by calpain 2, a protease associated with metastatic breast cancer phenotype [2].
• Calpain-2 as a target for limiting prostate cancer invasion [3].

High impact information on Capn2

• Growth factors activate m-calpain (calpain 2, CAPN2) via ERK/mitogen-activated protein kinases, but only when these kinases are localized to the plasma membrane [4].
• Both mu- and m-calpains are heterodimers, consisting of a distinct large 80-kDa catalytic subunit, encoded by the genes Capn1 and Capn2, and a common small 28-kDa regulatory subunit (Capn4) [5].
• An analysis of human breast tumors shows that high levels of cyclin E are coincident with the expression of the low molecular weight isoforms, high levels of calpain 2 protein, and proteolysis of FAK [2].
• Antisense down-regulation of the growth factor-activated calpain-2 (m-calpain) isoform also reduced transmigration and cell motility [3].
• No change was detected in the expression of calpain 2 in the pulmonary epithelium by western blot or immunohistochemistry [6].

Biological context of Capn2

• Mechanical unloading of the failing human heart significantly increased calpain 2 gene expression [7].
• Calpain 2 was first expressed late in embryonic development and localized to the lens epithelium and transition zone [8].
• To test this, transgenic (TG) mice expressing a calpain 2, in which the active site cysteine 105 was mutated to alanine, were produced [9].

Anatomical context of Capn2

• To address the isoform specific functions of calpain 1 and calpain 2 during cell protrusion, we stably introduced small interfering RNAs (siRNAs) targeting each isoform into a fibroblast cell line [10].
• The expression of calpain 1 and calpain 2 in spermatogenic cells and spermatozoa of the mouse [11].
• First, it is conceivable that calpain 2 plays a more dominant role in neurons, and that calpain 1 makes a minor contribution as opposed to its suspected predominant role in the hematopoietic system [12].
• M-calpain levels increase during fusion of myoblasts in the mutant muscular dysgenesis (mdg) mouse [13].

Other interactions of Capn2

• Monoclonal antibodies raised against CANP2 reacted almost equally with CANP1 and CANP3 [1].
• In contrast, calpain 2, Lp85, and calpain 10 may have roles in cell signaling pathways [8].
• Also, two genes with pro-apoptotic functions, calpain-2 and caspase-8-associated protein, increased significantly [14].

Analytical, diagnostic and therapeutic context of Capn2

• Ubiquitous type calpain 2 and calpain 10 and lens specific Lp82 and Lp85 protein distribution were determined using immunohistochemistry and immunoblotting in embryonic and post-natal mouse eyes [8].

References