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calpastatin, calpain inhibitor I
The protein encoded by this gene is an endogenous calpain (calcium-dependent cysteine protease) inhibitor. It consists of an N-terminal domain L and four repetitive calpain-inhibition domains (domains 1-4), and it is involved in the proteolysis of amyloid precursor protein. The calpain/calpastatin system is involved in numerous membrane fusion events, such as neural vesicle exocytosis and platelet and red-cell aggregation. The encoded protein is also thought to affect the expression levels of genes encoding structural or regulatory proteins. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jun 2010] (from NCBI)
Top mentioned proteins: Calpain, calpain 2, HAD, CAN, PrP
Papers using calpastatin antibodies
Calpastatin levels affect calpain activation and calpain proteolytic activity in APP transgenic mouse model of Alzheimer's disease
Joyashiki Eri et al., In BMC Complementary and Alternative Medicine, 2006
... A monoclonal antibody against μ-calpain and a polyclonal antibody against calpastatin were purchased from Biosource (Camarillo, CA, USA) and Santa Cruz Biotechnology (Santa Cruz CA ...
Targeted proteolysis sustains calcineurin activation.
Csernoch Ladzlo, In PLoS ONE, 2004
... 8 weeks-old Calpastatin transgenic female mice (CPST) on ...
EGF receptor regulation of cell motilityEGF induces disassembly of focal adhesions independently of the motility-associated PLC γ signaling pathway
Wells Alan et al., In The Journal of Cell Biology, 1997
... Calpain inhibitor I was purchased from Biomol.
Papers on calpastatin
Calpastatin inhibits motor neuron death and increases survival of hSOD1(G93A) mice.
Nixon et al., New York City, United States. In J Neurochem, Feb 2016
Given that calpains mediate neurodegeneration in other pathological states and are abnormally activated in ALS, we investigated the possible ameliorative effects of inhibiting calpain overactivation in hSOD1(G93A) transgenic (Tg) mice in vivo by neuron specific overexpression of calpastatin (CAST), the highly selective endogenous inhibitor of calpains.
Targeting host calpain proteases decreases influenza A virus infection.
Si-Tahar et al., Hong Kong, Hong Kong. In Am J Physiol Lung Cell Mol Physiol, Feb 2016
Using siRNA gene silencing, specific synthetic inhibitors of calpains and mice overexpressing calpastatin, we found that calpain inhibition dampens IAV replication as well as IAV-triggered secretion of pro-inflammatory mediators and leukocyte infiltration.
Implementing meta-analysis from genome-wide association studies for pork quality traits.
Steibel et al., In J Anim Sci, Dec 2015
A search for annotated genes retrieved genes previously reported as candidates for shear force (calpain-1 catalytic subunit [] and calpastatin []), as well as for ultimate pH, purge loss, and cook loss (protein kinase, AMP-activated, γ 3 noncatalytic subunit []).
The role of extracellular and intracellular proteolytic systems in aneurysms of the ascending aorta.
Beiras-Fernandez et al., Frankfurt am Main, Germany. In Histol Histopathol, Dec 2015
Calpastatin specifically inhibits the proteolytic activity of calpain-I and -II.
Resuscitation of a dead cardiomyocyte.
Tyagi et al., Louisville, United States. In Heart Fail Rev, Nov 2015
The activation of calpains beyond the calpastatin-mediated inhibition due to extensive calcium harbor can lead to titin degradation, damage to the sarcomere and contractile dysfunction.
Calpain in Breast Cancer: Role in Disease Progression and Treatment Response.
Martin et al., Nottingham, United Kingdom. In Pathobiology, Sep 2015
The ubiquitously expressed micro (µ)-calpain and milli (m)-calpain are archetypal family members that require calcium for function and can be inhibited by their endogenous inhibitor calpastatin.
C/EBPβ-LAP*/LAP Expression Is Mediated by RSK/eIF4B-Dependent Signalling and Boosted by Increased Protein Stability in Models of Monocytic Differentiation.
Brand et al., Hannover, Germany. In Plos One, 2014
Furthermore, under our conditions a marked stabilisation of LAP*/LAP protein occurred, accompanied by reduced chymotrypsin-like proteasome/calpain activities and increased calpastatin levels.
[Advances in the research of the relationship between calpains and post-burn skeletal muscle wasting].
Chai et al., Beijing, China. In Zhonghua Shao Shang Za Zhi, 2013
Skeletal muscle tissue mainly expresses m-calpain, µ-caplain, n-calpain, and their endogenous inhibitor calpastatin.
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
Abundant evidence has testified that calpains (CAPNs) including calpain I (CAPN1) and calpastatin (CAST) have the closest relationship with tenderness in livestock.
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.
Deletion of the presynaptic scaffold CAST reduces active zone size in rod photoreceptors and impairs visual processing.
Moser et al., Frankfurt am Main, Germany. In J Neurosci, 2012
CAST supports large active zone size and high rates of transmission at rod ribbon synapses, which are required for normal vision.
Calpastatin overexpression limits calpain-mediated proteolysis and behavioral deficits following traumatic brain injury.
Saatman et al., Lexington, United States. In Exp Neurol, 2012
Calpastatin overexpression reduces calpain-mediated proteolysis and behavioral impairment after traumatic brain injury.
Calpastatin upregulation in Mycoplasma hyorhinis-infected cells is promoted by the mycoplasma lipoproteins via the NF-κB pathway.
Kosower et al., Tel Aviv-Yafo, Israel. In Cell Microbiol, 2012
Mycoplasma hyorhinis membrane lipoproteins induce calpastatin upregulation in human cells
Effects of genetic variants for the calpastatin gene on calpastatin activity and meat tenderness in Hanwoo (Korean cattle).
Davis et al., Ch'ŏnan, South Korea. In Meat Sci, 2012
The CAST28 genotypes showing allele frequencies of C (0.429) and T (0.571) were significantly associated with calpastatin activity and Warner-Bratzler Shear Force in beef.
Mechanistic involvement of the calpain-calpastatin system in Alzheimer neuropathology.
Saido et al., Wako, Japan. In Faseb J, 2012
Data show that genetic deficiency of calpastatin (CS) augmented Abeta amyloidosis, tau phosphorylation, microgliosis, and somatodendritic dystrophy, and increased mortality in amyloid precursor protein (APP) transgenic mice.
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
Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains.
Green et al., Memphis, United States. In Nature, 2008
3.0 A structure of Ca(2+)-bound m-calpain in complex with the first calpastatin repeat, both from rat, revealing the mechanism of exclusive specificity
Cleavage of the plasma membrane Na+/Ca2+ exchanger in excitotoxicity.
Nicotera et al., Leicester, United Kingdom. In Cell, 2005
Inhibition of Ca2+-activated proteases (calpains) by overexpressing their endogenous inhibitor protein, calpastatin or the expression of an NCX isoform not cleaved by calpains, prevented Ca2+ overload and rescued neurons from excitotoxic death.
The calpain system.
Cong et al., Tucson, United States. In Physiol Rev, 2003
The calpain system originally comprised three molecules: two Ca2+-dependent proteases, mu-calpain and m-calpain, and a third polypeptide, calpastatin, whose only known function is to inhibit the two calpains.
A Ca(2+) switch aligns the active site of calpain.
Davies et al., Kingston, Canada. In Cell, 2002
The protease region is not affected by the endogenous inhibitor, calpastatin, and may contribute to calpain-mediated pathologies when the core is released by autoproteolysis.
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