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3.4.22.52: calpain-1

This is an abbreviated version!
For detailed information about calpain-1, go to the full flat file.

Word Map on EC 3.4.22.52

Reaction

broad endopeptidase specificity =

Synonyms

Cal 1, calcium-activated neutral protease I, calpain 1, calpain 1-gamma, calpain 1A, calpain I, calpain small subunit, calpain-1, calpain-1 (micro-form), calpain-I, calpain1, CANP1, CAPN1, CAPN1 g.p. (Homo sapiens), CAPN2, CAPNS1, cysteine protease, EC 3.4.22.17, EC 3.4.24.5, m-CANP, micro-calpain, mit-CPN1, mito-mu-calpain, mu-calpain, muCANP, muI-II

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.52 calpain-1

Expression

Expression on EC 3.4.22.52 - calpain-1

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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after ageing of large cuts of beef loin in vacuum or high oxygen modified atmosphere mu-calpain activity declines below the detection limit in all ageing systems
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after cisplatin treatment, calpain activation is an early event
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although the levels of the calpain I isoform are higher in the soluble and insoluble fractions of tir- and wild type enteropathogenic Escherichia coli (E2348/69 O127:H6)-infected cells, their levels are not significantly different to the TTSS-negative control
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an increase in the activity of calpain-1 takes place at an early stage of amyotrophic lateral sclerosis
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at 24 h after status epilepticus, activity of calpain I increases in the hippocampus
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at 24 h postmortem the activity of the native mu-calpain decreases. A faster decrease in pH results in reduced level of mu-calpain activity and increased autolysis of the enzyme
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calpain 1 activity is increased 2.5fold in FA-A, FA-D2, and FA-F cells as compared to normal cells and 3.5fold in FA-C and FA-G cells compared to normal cells
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calpain 1 expression levels are high in self-renewing neuronal stem cells and decrease with differentiation
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calpain 1 protein and mRNA levels are low at early developmental time points and increase dramatically by postnatal day 30. Immunoreactivity of the 80 kDa calpain 1 increases 75% from embryonic day 18 to postnatal day 90, with the increase being most rapid between postnatal day 10 and postnatal day 20 in rat brain
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calpain activity in liver of heterozygous cystathionine beta synthase-deficient mice shows a 30% increase compared to wild type mice
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calpain activity increases in cells exposed to intermittent hypoxia 60 and 0.01 mM 1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetra(acetoxymethyl) ester prevents this effect
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calpain-1 protein and activity in mitochondria are elevated in diabetic mouse hearts
calpain-I is activated in human carotid plaques
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calpain1 mRNA is increased in the all enamel epithelia between embryonic day 18 and postnatal day 1, calpastatin mRNA expression increases in the ameloblasts from postnatal days 1 to 7
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cell infection with Ad-capn1 and significantly elevates the protein level of calpain-1
cold storage (at 4°C) induces a time dependent up-regulation of calpain 1, reflected by an increase in the autoproteolytic cleavage of calpain 1, which can be prevented by addition of EDTA or dopamine (0.025 mM) pretreatment
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compared to control cybrids, Parkonsin’s disease cybrids reveal a significant increase in calpain activity
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compared with 5-month-old mice, there is no change in calpain 1 in 16-month-old mice
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delayed calcium deregulation is not sufficient to activate calpain 1
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fatiguing jumping exercise does not change mRNA expression of calpain 1
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high glucose (33 mM) induces calpain-1 activation in cardiomyocytes. Gp91phox-NADPH oxidase contributes to calpain-1 activation in high glucose-induced cardiomyocytes
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in comparison to the sham operation group, the activity of calpain I is 1.1fold decreased in the calpain inhibitor group (N-acetyl-L-Leu-L-Leu-L-Met (1.0 mg/kg/day))
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in comparison to the sham operation group, the activity of calpain I is significantly increased (2.3fold) in the control atrial fibrillation group
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in cultured pulmonary microvascular endothelial cells, incubation with septic plasma stimulates calpain activation. Reactive oxygen species produced from NADPH oxidase stimulates calpain-1 activation
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in healthy mice, calpeptin treatment causes a significant increase in micro-calpain
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in mice with myocardial infarction, calpeptin treatment causes a significant decrease in micro-calpain level
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inner ear cell death due to apoptosis occurs in a time-dependent manner with concomitant up-regulation of calpain-I expression
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ionomycin and thapsigragin, which elevate [Ca2+], activate calpains in cells exposed to normoxia
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listeriolysin O-dependent bacterial entry into the cytoplasm is required for calpain activation and interleukin-1 alpha secretion in macrophages infected with Listeria monocytogenes
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low nutritional level diet treatment increases mRNA level of micro-calpain in skeletal muscle
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mitochondrial mu-calpain activity is increased by 160% during ischemia-reperfusion compared to time control
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MK801 added shortly after glutamate prevents calpain 1 activation
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mu-calpain activity decreases by about 37% immediately and 2 h after acute-exhaustive exercise
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mu-calpain expression levels are unchanged by laminar shear flow or disturbed shear flow stimulus
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mu-calpain is activated in neurons after ischemia
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mu-calpain is not activated immediately following sprint, endurance or eccentric exercise. mu-Calpain is not activated 24 h after a single bout of eccentric exercise
Protein Never in Mitosis Gene A Interacting-1 reduces calpain activity and slows the degradation of COX-2 in MAEC cells
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the steady-state mRNA level of calpain 1A decreases by 2-4fold at the age of 4 to 6 days compared to 1-day-old piglets. Expressions of calpain 1A is negatively correlated with birth weight and fractional rate of growth, decreased levels of calpain 1A expressions over development in neonatal pigs are associated with high protein accumulations
there are no significant differences on the expressions of calpain-1 at the levels of mRNA and protein in patients with and without stress urinary incontinence
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there is no age-dependent change in calpain 1 protein expression in control or caloric-restricted rats. Liver samples taken from control rats at 4, 9, and 24 months and from caloric-restricted rats at 24 months do not exhibit any changes in calpain 1 protein expression
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there is no age-related change in calpain 1 protein expression in human female or male kidney samples. In the human kidney, there is no age-related change in calpain 1 mRNA expression
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treatment with 12 mg/kg endotoxin increases active calpain I protein
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treatment with 50 mg/kg 7-nitroindozale shows significant suppression of the activity of mu-calpain in brain cortex (penumbra), however, it has no significant effect on the mu-calpain activity in core (striatum and overlying cortex)
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Wnt5A activates calpain-1, leading to the cleavage of filamin A
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WNT5A knockdown decreases calpain 1 expression
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