gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Calpain 2,

calpain 2, m-Calpain, CAPN2, mCANP
The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 2. Multiple heterogeneous transcriptional start sites in the 5' UTR have been reported. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2009] (from NCBI)
Top mentioned proteins: Calpain, calpastatin, CAN, PrP, HAD
Papers on calpain 2
Calpain restrains the stem cells compartment in breast cancer.
Demarchi et al., Trieste, Italy. In Cell Cycle, Feb 2016
CAPNS1 is essential for the stability and function of ubiquitous CAPN1 and CAPN2.
Early post mortem expression of genes related to tenderization in two Italian Simmental young bulls' skeletal muscles differing in contractile type.
Piasentier et al., Udine, Italy. In Anim Sci J, Dec 2015
The messenger RNA (mRNA) abundances of calpain-1, calpain-2, calpastatin, caspase 3, caspase 9, heat shock protein 27 (Hsp27), Hsp40 and Hsp70 were detected by quantitative PCR.
Airway epithelial dual oxidase 1 mediates allergen-induced IL-33 secretion and activation of type 2 immune responses.
van der Vliet et al., Budapest, Hungary. In J Allergy Clin Immunol, Dec 2015
RESULTS: In vitro or in vivo allergen challenge resulted in rapid airway epithelial IL-33 secretion, which depended critically on DUOX1-mediated activation of epithelial epidermal growth factor receptor and the protease calpain-2 through a redox-dependent mechanism involving cysteine oxidation within epidermal growth factor receptor and the tyrosine kinase Src.
LOX-1 in macrophage migration in response to ox-LDL and the involvement of calpains.
Mehta et al., Xinxiang, China. In Biochem Biophys Res Commun, Dec 2015
Our results showed that ox-LDL stimulated LOX-1 and calpain-2 expression, and inhibited calpain-1 expression in a dose- and time-dependent manner.
Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions.
Wang et al., Shanghai, China. In J Biol Chem, Nov 2015
A yeast two-hybrid screen for proteins interacting with LeuRS, a representative MSC member, identified calpain 2, a calcium-activated neutral cysteine protease.
The combination of lithium and l-Dopa/Carbidopa reduces MPTP-induced abnormal involuntary movements (AIMs) via calpain-1 inhibition in a mouse model: Relevance for Parkinson׳s disease therapy.
Kim et al., Dover, United States. In Brain Res, Nov 2015
Mechanistically, lithium was found to suppress MPTP-induced calpain activities in vivo coinciding with down-regulation of calpain-1 but not calpain-2 expression in both the striatum (ST) and the brain stem (BS).
Calpain Determines the Propensity of Adult Hippocampal Neural Stem Cells to Autophagic Cell Death Following Insulin Withdrawal.
Yu et al., Taegu, South Korea. In Stem Cells, Oct 2015
Our results indicate that low calpain activity, due to absence of calpain 1 and degradation of calpain 2, results in a preference for ACD over apoptosis in insulin-deprived HCN cells.
Activation of Calpain-2 by Mediators in Pulmonary Vascular Remodeling of Pulmonary Arterial Hypertension.
Su et al., Augusta, United States. In Am J Respir Cell Mol Biol, Sep 2015
The calcium chelator BAPTA/AM did not affect calpain activation but the extracellular signal-regulated kinase 1/2 (ERK1/2) inhibitor PD98059 and knocking down of calpain-2 prevented calpain activation in PAH mediator-treated PASMCs.
Physiological Roles of Calpain 1 Associated to Multiprotein NMDA Receptor Complex.
Melloni et al., Genova, Italy. In Plos One, 2014
We have recently demonstrated that in resting conditions calpain 1, but not calpain 2, is specifically associated to the N-Methyl-D-Aspartate receptor (NMDAR) multiprotein complex.
A New Insight into the Role of Calpains in Post-mortem Meat Tenderization in Domestic Animals: A review.
Liu et al., China. In Asian-australas J Anim Sci, 2013
In this review, we summarize the role of CAPN1, calpain II (CAPN2) and CAST in post-mortem meat tenderization, and analyse the relationship between CAPN3 and tenderness in domestic animals.
Structure-function relationships in calpains.
Davies et al., Kingston, Canada. In Biochem J, 2012
Structures of calpain-2, both Ca2+-free and bound to calpastatin in the activated Ca2+-bound state, have provided a wealth of information about the enzyme's structure-function relationships and activation.
Passive stretch reduces calpain activity through nitric oxide pathway in unloaded soleus muscles.
Yu et al., Xi'an, China. In Mol Cell Biochem, 2012
passive stretch on soleus muscles may prevent in part unloading-induced atrophy through a calpain signal pathway
Calpain 2 activated through N-methyl-D-aspartic acid receptor signaling cleaves CPEB3 and abrogates CPEB3-repressed translation in neurons.
Huang et al., Taipei, Taiwan. In Mol Cell Biol, 2012
cleavage of CPEB3 by NMDA-activated calpain 2 accounts for the activity-related translation of CPEB3-targeted RNAs
Global profiling of proteolytically modified proteins in human metastatic hepatocellular carcinoma cell lines reveals CAPN2 centered network.
Yang et al., Shanghai, China. In Proteomics, 2012
Two human hepatocellular carcinoma cell lines were researched using proteomics. A proteolysis network was built up, of which the CAPN2 centered subnetwork, including SPTBN1, ATP5B, and VIM, was more active in the highly metastatic HCC cell line.
m-Calpain induction in vascular endothelial cells on human and mouse atheromas and its roles in VE-cadherin disorganization and atherosclerosis.
Miyazaki et al., Tokyo, Japan. In Circulation, 2012
Subtype-selective induction of m-calpain in aorta during atherosclerotic progression is associated with proteolytic disorganization of VE-cadherin and proatherogenic hyperpermeability in cells.
Immunhistochemical analysis for expression of calpain 1, calpain 2 and calpastatin in ovarian cancer.
Friedrich et al., Krefeld, Germany. In Eur J Gynaecol Oncol, 2010
Staining intensity of calpain 2 in ovarian carcinoma decreased with increasing lymph node status.
Calpain chronicle--an enzyme family under multidisciplinary characterization.
Ono et al., Tokyo, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2010
In the human genome, 15 genes--CAPN1, CAPN2, etc.--encode a calpain-like protease domain.
Regulation of calpain-2 in neurons: implications for synaptic plasticity.
Baudry et al., Los Angeles, United States. In Mol Neurobiol, 2010
In brain, calpain-2 plays critical roles in developmental and adult synaptic plasticity.
Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin.
Davies et al., Kingston, Canada. In Nature, 2008
2.4-A-resolution crystal structure of the calcium-bound calpain 2 heterodimer bound by one of the four inhibitory domains of calpastatin
The calpains: modular designs and functional diversity.
Ersfeld et al., United States. In Genome Biol, 2006
The calpain family is named for the calcium dependence of the papain-like, thiol protease activity of the well-studied ubiquitous vertebrate enzymes calpain-1 (mu-calpain) and calpain-2 (m-calpain).
share on facebooktweetadd +1mail to friends