Proteolysis of tau by calpain

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

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Phosphorylation affects the ability of tau protein to promote microtubule assembly.

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Accumulation of abnormally phosphorylated τ precedes the formation of neurofibrillary tangles in Alzheimer's disease

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Microtubule-Associated Proteins: Their Potential Role In Determining Neuronal Morphology

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Microtubule-Associated Proteins

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Phosphorylation determines two distinct species of tau in the central nervous system

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Structure of the Bovine Tau Gene: Alternatively Spliced Transcripts Generate a Protein Family

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Calcium‐activated neutral protease and its endogenous inhibitor Activation at the cell membrane and biological function

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Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain

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Separation and characterization of microtubule proteins from calf brain

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Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

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Roles of tau protein in health and disease

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Role of tau protein in both physiological and pathological conditions

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Cysteine Proteases and Their Inhibitors

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Cutting to the chase: calpain proteases in cell motility

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Calpain-Mediated Signaling Mechanisms in Neuronal Injury and Neurodegeneration

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The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine

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Calcium signaling in neurodegeneration

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GSK3: a possible link between beta amyloid peptide and tau protein

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Immunolocalization of calpain I-mediated spectrin degradation to vulnerable neurons in the ischemic gerbil brain

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Tau phosphorylation and aggregation in Alzheimer's disease pathology

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Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B

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Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain.

Litersky, J. M., & Johnson, G. V. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45982-0 · Cited by 201

Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: cause or effect?

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It’s all about tau

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Degradation of Microtubule‐Associated Protein 2 and Brain Spectrin by Calpain: A Comparative Study

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Activation of m-Calpain (Calpain II) by Epidermal Growth Factor Is Limited by Protein Kinase A Phosphorylation of m-Calpain

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Proteins released from degenerating neurons are surrogate markers for acute brain damage

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Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease

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Distinct Mechanistic Roles of Calpain and Caspase Activation in Neurodegeneration as Revealed in Mice Overexpressing Their Specific Inhibitors

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Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356

Litersky, J. M., Johnson, G. V. W., Jakes, R., Goedert, M., Lee, M., & Seubert, P. A. (1996) · Biochemical Journal · doi:10.1042/bj3160655 · Cited by 150

Aluminum-Induced Structural Alterations of the Precursor of the Non-Aβ Component of Alzheimer's Disease Amyloid

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Rapid Calpain I Activation and Cytoskeletal Protein Degradation Following Traumatic Spinal Cord Injury: Attenuation with Riluzole Pretreatment

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Microtubule-Associated Protein 2 Levels Decrease in Hippocampus Following Traumatic Brain Injury

Taft, W. C., Yang, K., Dixon, C. E., & Hayes, R. L. (1992) · Journal of Neurotrauma · doi:10.1089/neu.1992.9.281 · Cited by 141

Proteolytic processing of tau

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Microtubular Proteolysis in Focal Cerebral Ischemia

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Role of calpains in the injury-induced dysfunction and degeneration of the mammalian axon

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Relevance of Phosphorylation and Truncation of Tau to the Etiopathogenesis of Alzheimer’s Disease

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'Oxidation Inhibits Substrate Proteolysis by Calpain I but Not Autolysis

Guttmann, R. P., Elce, J. S., Bell, P. D., Isbell, J. C., & Johnson, G. V. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.3.2005 · Cited by 119

Tau Phosphorylation by GSK3 in Different Conditions

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Calpain‐Induced Proteolysis of Normal Human Tau and Tau Associated with Paired Helical Filaments

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Truncation and activation of GSK-3β by calpain I: a molecular mechanism links to tau hyperphosphorylation in Alzheimer's disease

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Differential vulnerability of microtubule components in cerebral ischemia

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Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment

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Oxidative Stress Inhibits Calpain Activity in Situ

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Hypothermia Attenuates the Loss of Hippocampal Microtubule-Associated Protein 2 (MAP2) following Traumatic Brain Injury

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Calpain activation in neurodegenerative diseases: confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2

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O-GlcNAc cycling: Implications for neurodegenerative disorders

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Calpains: Intact and active?

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Transglutaminase Catalyzes the Formation of Sodium Dodecyl Sulfate‐Insoluble, Alz‐50‐Reactive Polymers of τ

Dudek, S. M., & Johnson, G. V. W. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03636.x · Cited by 92

Calpains (intracellular calcium-activated cysteine proteinases): Structure-activity relationships and involvement in normal and abnormal cellular metabolism

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Casein kinase II preferentially phosphorylates human tau isoforms containing an amino-terminal insert. Identification of threonine 39 as the primary phosphate acceptor.

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Phosphorylation Modulates Calpain‐Mediated Proteolysis and Calmodulin Binding of the 200‐kDa and 160‐kDa Neurofilament Proteins

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In vitro polymerization of oxidized tau into filaments

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Modulation of the phosphorylation state of tau in situ: the roles of calcium and cyclic AMP

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Polymerization of Microtubule-associated Protein Tau under Near-physiological Conditions

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TOC1: Characterization of a Selective Oligomeric Tau Antibody

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Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF‐tau

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Chronic traumatic encephalopathy-integration of canonical traumatic brain injury secondary injury mechanisms with tau pathology

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Tau phosphorylation and proteolysis: Insights and perspectives

Johnson, G. V. W. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s326 · Cited by 69

Calpain-mediated proteolysis of microtubule associated proteins MAP1B and MAP2 in developing brain

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Glutamate receptor antagonists inhibit calpain-mediated cytoskeletal proteolysis in focal cerebral ischemia

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Axonal degeneration in multiple sclerosis: can we predict and prevent permanent disability?

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Cytoskeletal Disruption Following Contusion Injury to the Rat Spinal Cord

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Altered levels and distribution of microtubule‐associated proteins before disease onset in a mouse model of amyotrophic lateral sclerosis

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Intracellular and Extracellular Roles for Tau in Neurodegenerative Disease

Hanger, D. P., Lau, D. H. W., Phillips, E. C., Bondulich, M. K., Guo, T., Woodward, B. W., Pooler, A. M., & Noble, W. J. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132054 · Cited by 66

Calpain Dysregulation in Alzheimer’s Disease

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Insulin therapy modulates mitochondrial dynamics and biogenesis, autophagy and tau protein phosphorylation in the brain of type 1 diabetic rats

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Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target

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Asparagine endopeptidase is an innovative therapeutic target for neurodegenerative diseases

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Steele‐Richardson‐Olszewski syndrome in a patient with a single C212Y mutation in the parkin protein

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Postmortem changes in the levels and localization of microtubule‐associated proteins (tau, MAP2 and MAP1B) in the rat and human hippocampus

Schwab, C., Bondada, V., Sparks, D. L., Cahan, L. D., & Geddes, J. W. (1994) · Hippocampus · doi:10.1002/hipo.450040212 · Cited by 60

Tau cleavage and tau aggregation in neurodegenerative disease

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Tau Phosphorylation, Aggregation, and Cell Toxicity

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Dual Vulnerability of Tau to Calpains and Caspase-3 Proteolysis Under Neurotoxic and Neurodegenerative Conditions

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The regulatory role of calmodulin in the proteolysis of individual neurofilament proteins by calpain

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Calpain and N-methyl-d-aspartate (NMDA)-induced excitotoxicity in rat retinas

Chiu, K., Lam, T. T., Li, W. W. Y., Caprioli, J., & Kwong, J. M. K. (2005) · Brain Research · doi:10.1016/j.brainres.2005.04.016 · Cited by 56

Calpain-mediated tau fragmentation is altered in Alzheimer’s disease progression

Chen, H.-H., Liu, P., Auger, P., Lee, S.-H., Adolfsson, O., Rey-Bellet, L., Lafrance-Vanasse, J., Friedman, B. A., Pihlgren, M., Muhs, A., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-35130-y · Cited by 51

Proteasome inhibition and Tau proteolysis: an unexpected regulation

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Differential Phosphorylation of τ by Cyclic AMP‐Dependent Protein Kinase and Ca2+/Calmodulin‐Dependent Protein Kinase II: Metabolic and Functional Consequences

Johnson, G. V. W. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10094.x · Cited by 55

Presence of calpain‐induced proteolysis in retinal degeneration and dysfunction in a rat model of acute ocular hypertension

Oka, T., Tamada, Y., Nakajima, E., Shearer, T. R., & Azuma, M. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20827 · Cited by 53

Calpain‐mediated proteolysis of microtubule‐associated protein 2 (MAP‐2) is inhibited by phosphorylation by cAMP‐dependent protein kinase, but not by Ca2+/calmodulin‐dependent protein kinase II

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Probable Participation of 14-3-3 in Tau Protein Oligomerization and Aggregation

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Phosphorylation, calpain proteolysis and tubulin binding of recombinant human tau isoforms

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Calcium-activated proteolysis of intracellular domains in the cell adhesion molecules NCAM and N-cadherin

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Very low levels of methylmercury induce cell death of cultured rat cerebellar neurons via calpain activation

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Tau Protein Is Hyperphosphorylated in a Site‐Specific Manner in Apoptotic Neuronal PC12 Cells

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Phosphorylation of Tau Alters Its Association with the Plasma Membrane

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VASE-encoded peptide modifies NCAM- and L1-mediated neurite outgrowth

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Proteolysis of neuronal cytoskeletal proteins by calpain contributes to rat retinal cell death induced by hypoxia

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Progressive supranuclear palsy and tau hyperphosphorylation in a patient with a C212Y parkin mutation

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Inhibitory effect of a brain derived peptide preparation on the Ca++-dependent protease, calpain

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A dose-dependent increase of Tau immunostaining is produced by glutamate toxicity in primary neuronal cultures

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Alzheimer's disease-associated presenilin 1 in neuronal cells: Evidence for localization to the endoplasmic reticulum-Golgi intermediate compartment

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Metal-catalyzed oxidation of bovine neurofilaments in vitro

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Tissue Transglutaminase Is an In Situ Substrate of Calpain: Regulation of Activity

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Anti-tau oligomers passive vaccination for the treatment of Alzheimer disease

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Activation of calpain‐1 in myelin and microglia in the white matter of the aged rhesus monkey

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Parkin deletion causes cerebral and systemic amyloidosis in human mutated tau over-expressing mice

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Microtubule‐Dissociating Drugs and A23187 Reveal Differences in the Inhibition of Synaptosomal Transmitter Release by Botulinum Neurotoxins Types A and B

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Proteasome or calpain inhibition does not alter cellular tau levels in neuroblastoma cells or primary neurons

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Perikaryal accumulation and proteolysis of neurofilament proteins in the post-mortem rat brain

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Stem Cells as Potential Targets of Polyphenols in Multiple Sclerosis and Alzheimer’s Disease

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Identification and characterization of PEBP as a calpain substrate

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Proteolysis of Microtubule‐Associated Protein 2 and Tubulin by Cathepsin D

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Neighbored phosphorylation sites as PHF-tau specific markers in Alzheimer’s disease

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LabCaS: Labeling calpain substrate cleavage sites from amino acid sequence using conditional random fields

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Amyloid-like properties of a synthetic peptide corresponding to the carboxy terminus of β-amyloid protein precursor

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Brain G-protein proteolysis by calpain: enhancement by lithium

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Ethanol enhances tau accumulation in neuroblastoma cells that inducibly express tau

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Effect of Calpain on The Degradation of Tau in Rat Brain Co rtex Extracts

Fang, Z. (2003) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS

Degradation of Microtubule‐Associated Protein 2 and Brain Spectrin by Calpain: A Comparative Study

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Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules

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Calpain processing of brain microtubules from the Atlantic Cod, Gadus morhua

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Proteolytic degradation of tau via calpain may be involved in tau-induced neurodegeneration

Reinecke, J. B., & Steinhilb, M. L. (2007)