Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
casein + H2O
hydrolyzed casein
-
-
-
-
?
N-succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
peptide + H2O
hydrolyzed peptide
additional information
?
-
-
the enzyme undergoes N-terminal autolysis in a Ca2+-dependent manner
-
-
?
cactus + H2O
?
an IkappaB homologue, Cactus and calpain A physically interact, calpain A generates a C-terminaltruncated Cactus fragment devoid of Toll-responsive sequences, cleavage analysis in vivo, overview
-
-
?
cactus + H2O
?
an IkappaB homologue, GFP-tagged substrate, calpain A generates a C-terminaltruncated Cactus fragment devoid of Toll-responsive sequences
-
-
?
peptide + H2O
hydrolyzed peptide
calpain is involved in the dynamic changes in the embryonic cytoskeleton, especially actin-related structures, during early embryogenesis prior to cellularization
-
-
?
peptide + H2O
hydrolyzed peptide
calpain is involved in the dynamic changes in the embryonic cytoskeleton, especially actin-related structures, during early embryogenesis prior to cellularization
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Acute Lung Injury
Calpain inhibition ameliorates scald burn-induced acute lung injury in rats.
Alzheimer Disease
Calcium-activated neutral proteinase (calpain) system in aging and Alzheimer's disease.
Alzheimer Disease
Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration.
Amyotrophic Lateral Sclerosis
A role for calpain-dependent cleavage of TDP-43 in amyotrophic lateral sclerosis pathology.
Anemia
Comparative action of calpain on erythrocyte Ca2(+)-pumping ATPase in sickle cell anaemia, essential hypertension and kwashiorkor.
Anemia, Sickle Cell
Comparative action of calpain on erythrocyte Ca2(+)-pumping ATPase in sickle cell anaemia, essential hypertension and kwashiorkor.
Arthritis
Immunohistochemical demonstration of calcium-dependent cysteine proteinase (calpain) in collagen-induced arthritis in mice.
Arthritis, Rheumatoid
Amelioration of experimental arthritis by a calpain-inhibitory compound: regulation of cytokine production by E-64-d in vivo and in vitro.
Arthritis, Rheumatoid
Domain reactivity of autoantibodies to calpastatin in patients with systemic rheumatic diseases.
Arthritis, Rheumatoid
Overexpression of a minimal domain of calpastatin suppresses IL-6 production and Th17 development via reduced NF-?B and increased STAT5 signals.
Arthritis, Rheumatoid
The calpain inhibitor calpeptin prevents bleomycin-induced pulmonary fibrosis in mice.
Autoimmune Diseases
Overexpression of a minimal domain of calpastatin suppresses IL-6 production and Th17 development via reduced NF-?B and increased STAT5 signals.
Blister
Calpain activation in plasma membrane bleb formation during tert-butyl hydroperoxide-induced rat hepatocyte injury.
Brain Ischemia
Calpain activation induced by glucose deprivation is mediated by oxidative stress and contributes to neuronal damage.
Demyelinating Diseases
Calpain activity and expression are increased in splenic inflammatory cells associated with experimental allergic encephalomyelitis.
Demyelinating Diseases
Calpain, a mediator of myelin breakdown in demyelinating diseases.
Demyelinating Diseases
Pathogenesis of myelin breakdown in demyelinating diseases: role of proteolytic enzymes.
Encephalomyelitis, Autoimmune, Experimental
A putative mechanism of demyelination in multiple sclerosis by a proteolytic enzyme, calpain.
Encephalomyelitis, Autoimmune, Experimental
Upregulation of calpain activity and expression in experimental allergic encephalomyelitis: a putative role for calpain in demyelination.
Essential Hypertension
Comparative action of calpain on erythrocyte Ca2(+)-pumping ATPase in sickle cell anaemia, essential hypertension and kwashiorkor.
Glioma
Calcium-activated neutral proteinase (calpain) activity in C6 cell line: compartmentation of mu and m calpain.
Hyperalgesia
Neurotropin(®) inhibits calpain activity upregulated by specific alternation of rhythm in temperature in the mesencephalon of rats.
Infarction, Middle Cerebral Artery
[Functional roles of constitutively active calcineurin in delayed neuronal death after brain ischemia].
Kwashiorkor
Comparative action of calpain on erythrocyte Ca2(+)-pumping ATPase in sickle cell anaemia, essential hypertension and kwashiorkor.
Melanoma, Experimental
Involvement of calpain in melanogenesis of mouse B16 melanoma cells.
Multiple Sclerosis
Microglial functions and proteases.
Muscular Dystrophies
Proteasome expression in the skeletal muscles of patients with muscular dystrophy.
Neoplasms
Calpain-dependent proteolysis of NF2 protein: involvement in schwannomas and meningiomas.
Nervous System Diseases
Prolonged calpain-mediated spectrin breakdown occurs regionally following experimental brain injury in the rat.
Parkinsonian Disorders
Calpain as a potential therapeutic target in Parkinson's disease.
Parkinsonian Disorders
Extranigral neurodegeneration in Parkinson's disease.
Prostatic Neoplasms
Calpain activation through galectin-3 inhibition sensitizes prostate cancer cells to cisplatin treatment.
Reperfusion Injury
Calpain inhibition decreases endothelin-1 levels and pulmonary hypertension after cardiopulmonary bypass with deep hypothermic circulatory arrest.
Reperfusion Injury
[Demonstration of secondary free radicals and the role of calpain in functional changes associated with the myocardial ischemia-reperfusion sequence]
Spinal Cord Injuries
Calpain activation and apoptosis in motor neurons of cultured adult mouse spinal cord.
Spinal Cord Injuries
Calpain activity and translational expression increased in spinal cord injury.
Spinal Cord Injuries
Calpain in the pathophysiology of spinal cord injury: neuroprotection with calpain inhibitors.
Spinal Cord Injuries
Cell death in spinal cord injury (SCI) requires de novo protein synthesis. Calpain inhibitor E-64-d provides neuroprotection in SCI lesion and penumbra.
Spinal Cord Injuries
E-64-d prevents both calpain upregulation and apoptosis in the lesion and penumbra following spinal cord injury in rats.
Spinal Cord Injuries
Higher calpastatin levels correlate with resistance to calpain-mediated proteolysis and neuronal apoptosis in juvenile rats after spinal cord injury.
Spinal Cord Injuries
Inhibition of calpain-mediated apoptosis by E-64 d-reduced immediate early gene (IEG) expression and reactive astrogliosis in the lesion and penumbra following spinal cord injury in rats.
Spinal Cord Injuries
Relatively low levels of calpain expression in juvenile rat correlate with less neuronal apoptosis after spinal cord injury.
Tauopathies
Inhibition of Calpain Protects Against Tauopathy in Transgenic P301S Tau Mice.
Uremia
Calpain is activated in experimental uremia: is calpain a mediator of uremia-induced myocardial injury?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
-
brenda
expression during early embryogenesis
brenda
CalpA protein is apically enriched in the submembranous cytoplasm of the embryo syncytium
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
calpain is first detected near the anterior pole and in posterior region of the embryo just after fertilization. The anterior calpain disappears during the cleavage cycles. On the other hand, the posterior calpain moved to the posterior pole when polar buds are formed, and condenses just below the pole cells. At cleavage cycles 8 and 9, when nuclei reach the egg surface, calpain is localized between the nuclei at the surface beneath the precleavage furrows. Calpain condenses specifically at the edge of and between actin caps that underlie the plasma membrane immediately above each nucleus
brenda
-
-
-
brenda
-
calpain is first detected near the anterior pole and in posterior region of the embryo just after fertilization. The anterior calpain disappears during the cleavage cycles. On the other hand, the posterior calpain moved to the posterior pole when polar buds are formed, and condenses just below the pole cells. At cleavage cycles 8 and 9, when nuclei reach the egg surface, calpain is localized between the nuclei at the surface beneath the precleavage furrows. Calpain condenses specifically at the edge of and between actin caps that underlie the plasma membrane immediately above each nucleus
-
brenda
-
brenda
-
-
-
brenda
-
brenda
-
-
-
brenda
-
brenda
-
-
-
brenda
additional information
the expression of the protein is more restricted than that of the corresponding transcripts, which are widely distributed in the central nervous system, digestive tract, and other tissues
brenda
additional information
-
the expression of the protein is more restricted than that of the corresponding transcripts, which are widely distributed in the central nervous system, digestive tract, and other tissues
brenda
additional information
cactus regulates calpain A localization, calpain A redistribution to the cytoplasm requires full-length cactus, overview
brenda
additional information
-
cactus regulates calpain A localization, calpain A redistribution to the cytoplasm requires full-length cactus, overview
brenda
additional information
-
the expression of the protein is more restricted than that of the corresponding transcripts, which are widely distributed in the central nervous system, digestive tract, and other tissues
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
-
calpainA knockdowns increase Cactus levels, shifting the dorsal gradient and dorsal-ventral patterning. Decapentaplegic protein signals increase Cactus levels through calpain A inhibition, thereby interfering with Dorsal gene activation
physiological function
-
calpain A alters the size and position of Dorsal target gene expression domains, Cactus is regulated by calpain A, calpain A is regulated by Decapentaplegic signaling
physiological function
calpain A regulates regulate NFkappaB function by different mechanisms, it decreases IkappaB homologue cactus levels in vivo and regulates cactus function in the immune system. The enzyme interacts physically with cactus, recognizing a Cactus pool that is not bound to Dorsal, a fly NFkappaB/Rel homologue. The enzyme targets free cactus, which is incorporated into and modulates Toll-responsive complexes in the embryo and immune system. Effect of calpain A on the embryonic DV axis. Cactus regulates calpain A activity and localization
physiological function
a significant percentage of embryos from hypomorphic or knockdown calpain A mothers are lethal and do not complete embryogenesis. Lethality is increased as maternal calpain A function is reduced. Impaired Calpain A function results in loss of mitotic synchrony and ultimately halted embryonic development. Calpain A is required for the metaphase-to-anaphase transition, loss leads to presence of defective microtubules and chromosomal architecture at the mitotic spindle during metaphase and anaphase and perturbed levels of Cyclin B
additional information
cactus protein levels affect the cellular localization of the enzyme, overview. Wild-type syncytial blastoderm embryo show endogenous calpain A beneath the plasma membrane, while in loss-of-function cact mutants calpain A is diffuse in the cytoplasm. In a gain-of-function cact mutant, calpain A distribution is patchy during interphase and remains so during mitosis. Cactus regulates calpain A activity and localization
additional information
-
cactus protein levels affect the cellular localization of the enzyme, overview. Wild-type syncytial blastoderm embryo show endogenous calpain A beneath the plasma membrane, while in loss-of-function cact mutants calpain A is diffuse in the cytoplasm. In a gain-of-function cact mutant, calpain A distribution is patchy during interphase and remains so during mitosis. Cactus regulates calpain A activity and localization
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Adams, M.D.; Celniker, S.E.; Holt, R.A.; Evans, C.A.; Gocayne, J.D.; et al.
The genome sequence of Drosophila melanogaster
Science
287
2185-2195
2000
Drosophila melanogaster (Q11002), Drosophila melanogaster Berkeley (Q11002)
brenda
Theopold, U.; Pinter, M.; Daffre, S.; Tryselius, Y.; Friedrich, P.; Nassel, D.R.; Hultmark, D.
CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells
Mol. Cell. Biol.
15
824-834
1995
Drosophila melanogaster (Q11002), Drosophila melanogaster, Drosophila melanogaster Canton-S (Q11002)
brenda
Emori, Y.; Saigo, K.
Calpain localization changes in coordination with actib-related cytoskeletal changes during early embryonic development of Drosophila
J. Biol. Chem.
269
25137-25142
1994
Drosophila melanogaster (Q11002), Drosophila melanogaster, Drosophila melanogaster Canton-S (Q11002)
brenda
Stapleton, M.; Carlson, J.W.; Brokstein, P.; Yu, C.; et al.
A Drosophila full-length cDNA resource
Genome Biol.
3
research0080.1-0080.8
2002
Drosophila melanogaster (Q11002), Drosophila melanogaster Berkeley (Q11002)
-
brenda
Jekely, G.; Friedrich, P.
Characterization of two recombinant Drosophila calpains. CALPA and a novel homolog, CALPB
J. Biol. Chem.
274
23893-23900
1999
Drosophila melanogaster
brenda
Fontenele, M.; Carneiro, K.; Agrellos, R.; Oliveira, D.; Oliveira-Silva, A.; Vieira, V.; Negreiros, E.; Machado, E.; Araujo H.
The Ca2+-dependent protease calpain A regulates cactus/I kappaB levels during Drosophila development in response to maternal Dpp signals
Mech. Dev.
126
737-751
2009
Drosophila melanogaster
brenda
Fontenele, M.; Lim, B.; Oliveira, D.; Buffolo, M.; Perlman, D.H.; Schupbach, T.; Araujo, H.
Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis
Mol. Biol. Cell
24
2966-2980
2013
Drosophila melanogaster (Q11002), Drosophila melanogaster
brenda
Vieira, V.; Cardoso, M.; Araujo, H.
Calpain A controls mitotic synchrony in the Drosophila blastoderm embryo
Mech. Dev.
144
141-149
2017
Drosophila melanogaster (Q11002)
brenda