3.4.22.53: calpain-2
This is an abbreviated version!
For detailed information about calpain-2, go to the full flat file.
Word Map on EC 3.4.22.53
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3.4.22.53
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calpains
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calpastatin
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mu-calpain
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calcium-dependent
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ca2+-dependent
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proteinase
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myofibrillar
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cytoskeletal
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cataract
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zymography
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longissimus
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meat
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autolysis
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calpeptin
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tender
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casein
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cathepsins
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3.4.22.17
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postmortem
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calpain-mediated
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caspase-12
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lumborum
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autolyzed
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lens-specific
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talin
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alpha-spectrin
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canps
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cataractogenesis
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warner-bratzler
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spectrin
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slaughter
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semimembranosus
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calpain-specific
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desmin
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calpain-calpastatin
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lenses
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calpain-dependent
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atrogin-1
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medicine
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calpain-induced
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fodrin
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myofibril
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ca2+-activated
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calmodulin-like
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caseinolytic
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thoracis
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ca2+-requiring
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troponin-t
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micro-calpain
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calpain-like
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proteolyzed
- 3.4.22.53
- calpains
- calpastatin
- mu-calpain
-
calcium-dependent
-
ca2+-dependent
- proteinase
- myofibrillar
- cytoskeletal
- cataract
-
zymography
- longissimus
-
meat
-
autolysis
- calpeptin
-
tender
- casein
- cathepsins
-
3.4.22.17
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postmortem
-
calpain-mediated
- caspase-12
- lumborum
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autolyzed
-
lens-specific
- talin
- alpha-spectrin
-
canps
-
cataractogenesis
-
warner-bratzler
- spectrin
-
slaughter
- semimembranosus
-
calpain-specific
- desmin
-
calpain-calpastatin
- lenses
-
calpain-dependent
-
atrogin-1
- medicine
-
calpain-induced
- fodrin
- myofibril
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ca2+-activated
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calmodulin-like
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caseinolytic
- thoracis
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ca2+-requiring
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troponin-t
- micro-calpain
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calpain-like
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proteolyzed
Reaction
broad endopeptidase specificity =
Synonyms
Cal II, calcium-activated neutral protease II, calpain 2, calpain II, calpain xCL-2 (Xenopus leavis), calpain-2, calpain-2-like, calpain2, CAPN II, CAPN2, CAPN2 g.p. (Homo sapiens), CPN2, cysteine protease, EC 3.4.22.17, EC 3.4.24.5, human calpain 2, m-calpain, milli-calpain, mitochondrial m-calpain, nCL-2, rat calpain 2
ECTree
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Source Tissue
Source Tissue on EC 3.4.22.53 - calpain-2
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calpain 2 is important for both the formation of invadopodia and invasive capacity of breast cancer cells
cell line DLD-1. In KRASWT/- cells serum starvation induces CAPN2 expression, nucleolar accumulation
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nCL-2 is localized strictly to the surface cells in the gastric epithelium and the mucus-secreting goblet cells in the duodenum
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analysis from E8.5 to 14.5 stages indicates high levels of capn2 expression in the nervous system, heart and mesodermal tissues. Up-regulation is maintained during later developmental stages in proliferating cells and in precursor cells involved in muscle (myoblasts) or bone formation (chondrocytes). At later developmental stages, elevated mRNA levels coincide with CAPN2 nuclear localization in these cell types, while differentiated cells maintain cytoplasmic expression
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pulmonary microvascular endothelial cell. Incubation of the cells with vascular endothelial growth factor results in dose- and time-dependent increases in calpain activity and protein content of calpain-2. Vascular endothelial growth factor does not change the protein contents of calpain-1 and the small subunit or of calpastatin. Inhibition of calpain activity by siRNA directed against calpain-2 and by overexpression of calpastatin prevents vascular endothelial growth factor-induced increases in actin stress fibers in endothelial cells and angiogenesis
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calpain 2 is first expressed late in embryonic development and localizes to the lens epithelium and transition zone
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nCL-2 is localized strictly to the surface cells in the gastric epithelium and the mucus-secreting goblet cells in the duodenum
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prefominantly localized in the growing hyphal and rhizoidal apices
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membrane abnormalities and altered signaling pathways observed in Duchenne muscular dystrophy lymphocytes may be due to the increased association of calpain II onto membrane and cytosol
the large catalytic subunits of calpains 2 and the small regulatory subunit common to calpains 1 and 2 are weakly expressed in the parotid gland, sublingual gland, and submandibular gland at similar levels in males and females
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calpain 2 activity is critical for the life cycle of echovirus 1 and important in the multiplication of the viral RNA genome
the large catalytic subunits of calpains 2 and the small regulatory subunit common to calpains 1 and 2 are weakly expressed in the parotid gland, sublingual gland, and submandibular gland at similar levels in males and females
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active calpain 2 is concentrated in the trailing edge of the migrating T cell
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physiological shear stress elicits Ca2+ influx-sensitive activation of m-calain in umbilical vein endothelial cells
isoform-specific hyperactivation of calpain-2, but not calpain-1 occurs at the synapse early in the pathogenesis of Alzheimer's disease potentially contributing to the deregulation of synaptic signaling in Alzheimer's disease
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longissimus dorsi lumbar, longissimus dorsi thoracic, psoas major, semimembraneous triceps brachii. Activity of m-calpain decreases more slowly in the triceps brachii muscle than in the other 4 muscvles during postmortem storage
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m-calpain localizes to phosphoinositide lipids in membranes in contact with the extracellular matrix. m-Calpain accumulates towards the rear membrane of a moving cell in an epidermal growth factor-dependent manner. Its activation is absent from forming lamellipodia
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highest activity in plexiform layers and in the photoreceptor outer segments. In dark-adapted retinas the label is distributed throughout the outer segments. In light-adapted retinas, outer segment labelling is concentrated in the connecting cilium and the inner segments are labeled
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calpains 2 is involved in atrophy development in slow type muscle. Calpains 2 is autolyzed in the early stage of skeletal muscle atrophy. This autolysis is specific to the soluble fraction for calpain 2. Calpain 2 autolysis is associated with an increased amount of calpain 2 content. Calpain autolysis is only seen in the slow soleus muscle, while the fast plantaris muscle is not affected
the large catalytic subunits of calpains 2 and the small regulatory subunit common to calpains 1 and 2 are weakly expressed in the parotid gland, sublingual gland, and submandibular gland at similar levels in males and females