Calpain-Mediated Signaling Mechanisms in Neuronal Injury and Neurodegeneration
Tóm tắt
Từ khóa
Tài liệu tham khảo
Camins A (2006) Involvement of calpain activation in neurodegenerative processes. CNS Drug Rev 12:135–148
Ray SK (2006) Currently evaluated calpain and caspase inhibitors for neuroprotection in experimental brain ischemia. Curr Med Chem 13:3425–3440
Saez ME (2006) The therapeutic potential of the calpain family: new aspects. Drug Discov Today 11:917–923
Wu HY (2007) Calpain–calcineurin signaling in the pathogenesis of calcium-dependent disorder. Acta Med Okayama 61:123–137
Blanchard H (1997) Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes. Nat Struct Biol 4:532–538
Bevers MB (2008) Mechanistic role of calpains in postischemic neurodegeneration. J Cereb Blood Flow Metab 28:655–673
Chan SL (1999) Caspase and calpain substrates: roles in synaptic plasticity and cell death. J Neurosci Res 58:167–190
Hyrc K (1997) Ionized intracellular calcium concentration predicts excitotoxic neuronal death: observations with low-affinity fluorescent calcium indicators. J Neurosci 17:6669–6677
Goll DE (1992) Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? Bioessays 14:549–556
Arthur JS (2000) Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol Cell Biol 20:4474–4481
Dutt P (2006) m-Calpain is required for preimplantation embryonic development in mice. BMC Dev Biol 6:3
Pontremoli S (1992) Modulation of inhibitory efficiency of rat skeletal muscle calpastatin by phosphorylation. Biochem Biophys Res Commun 187:751–759
DeMartino GN (1988) Proteolysis of the protein inhibitor of calcium-dependent proteases produces lower molecular weight fragments that retain inhibitory activity. Arch Biochem Biophys 262:189–198
Czogalla A (2005) Spectrin and calpain: a ‘target’ and a ‘sniper’ in the pathology of neuronal cells. Cell Mol Life Sci 62:1913–1924
Nixon RA (1986) Fodrin degradation by calcium-activated neutral proteinase (CANP) in retinal ganglion cell neurons and optic glia: preferential localization of CANP activities in neurons. J Neurosci 6:1264–1271
Siman R (1984) Brain fodrin: substrate for calpain I, an endogenous calcium-activated protease. Proc Natl Acad Sci U S A 81:3572–3576
Seubert P (1987) Calmodulin stimulates the degradation of brain spectrin by calpain. Synapse 1:20–24
Cuerrier D (2005) Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: the importance of primed side interactions. J Biol Chem 280:40632–40641
Olney JW (1969) Brain lesions, obesity, and other disturbances in mice treated with monosodium glutamate. Science 164:719–721
Siman R (1988) Excitatory amino acids activate calpain I and induce structural protein breakdown in vivo. Neuron 1:279–287
Hong SC (1994) Neuroprotection with a calpain inhibitor in a model of focal cerebral ischemia. Stroke 25:663–669
Bevers MB (2007) Mechanistic role of calpains in postischemic neurodegeneration. J Cereb Blood Flow Metab 28(4):655–673
Newcomb-Fernandez JK (2001) Concurrent assessment of calpain and caspase-3 activation after oxygen–glucose deprivation in primary septo-hippocampal cultures. J Cereb Blood Flow Metab 21:1281–1294
McGinnis KM (1999) Procaspase-3 and poly(ADP)ribose polymerase (PARP) are calpain substrates. Biochem Biophys Res Commun 263:94–99
Malagelada C (2005) Contribution of caspase-mediated apoptosis to the cell death caused by oxygen–glucose deprivation in cortical cell cultures. Neurobiol Dis 20:27–37
Yamashima T (1998) Inhibition of ischaemic hippocampal neuronal death in primates with cathepsin B inhibitor CA-074: a novel strategy for neuroprotection based on ‘calpain–cathepsin hypothesis’. Eur J Neurosci 10:1723–1733
Yamashima T (2003) Sustained calpain activation associated with lysosomal rupture executes necrosis of the postischemic CA1 neurons in primates. Hippocampus 13:791–800
Chaitanya GV (2008) Activation of calpain, cathepsin-b and caspase-3 during transient focal cerebral ischemia in rat model. Neurochem Res. doi: 10.1007/s11064-007-9567-7
Tsubokawa T (2006) Cathepsin and calpain inhibitor E64d attenuates matrix metvalloproteinase-9 activity after focal cerebral ischemia in rats. Stroke 37:1888–1894
Tsubokawa T (2006) Neurovascular and neuronal protection by E64d after focal cerebral ischemia in rats. J Neurosci Res 84:832–840
Pottorf WJ 2nd (2006) Glutamate-induced protease-mediated loss of plasma membrane Ca2+ pump activity in rat hippocampal neurons. J Neurochem 98:1646–1656
Bano D (2005) Cleavage of the plasma membrane Na+/Ca2+ exchanger in excitotoxicity. Cell 120:275–285
De Jongh KS (1994) Differential proteolysis of the full-length form of the L-type calcium channel alpha 1 subunit by calpain. J Neurochem 63:1558–1564
Hell JW (1996) N-methyl-D-aspartate receptor-induced proteolytic conversion of postsynaptic class C L-type calcium channels in hippocampal neurons. Proc Natl Acad Sci U S A 93:3362–3367
Rardon DP (1990) Digestion of cardiac and skeletal muscle junctional sarcoplasmic reticulum vesicles with calpain II. Effects on the Ca2+ release channel. Circ Res 67:84–96
French JP (2006) Ischemia–reperfusion-induced calpain activation and SERCA2a degradation are attenuated by exercise training and calpain inhibition. Am J Physiol Heart Circ Physiol 290:H128–H136
Parsons JT (1999) Global ischemia-induced inhibition of the coupling ratio of calcium uptake and ATP hydrolysis by rat whole brain microsomal Mg(2+)/Ca(2+) ATPase. Brain Res 834:32–41
Magnusson A (1993) Calcium-induced degradation of the inositol (1,4,5)-trisphosphate receptor/Ca(2+)-channel. FEBS Lett 323:229–232
Pattni K (2003) Calpain cleavage of the B isoform of Ins(1,4,5)P3 3-kinase separates the catalytic domain from the membrane anchoring domain. Biochem J 375:643–651
Gascon S (2008) Excitotoxicity and focal cerebral ischemia induce truncation of the NR2A and NR2B subunits of the NMDA receptor and cleavage of the scaffolding protein PSD-95. Mol Psychiatry 13:99–114
Guttmann RP (2001) Specific proteolysis of the NR2 subunit at multiple sites by calpain. J Neurochem 78:1083–1093
Guttmann RP (2002) Proteolysis of the N-methyl-d-aspartate receptor by calpain in situ. J Pharmacol Exp Ther 302:1023–1030
Simpkins KL (2003) Selective activation induced cleavage of the NR2B subunit by calpain. J Neurosci 23:11322–11331
Bi R (1998) Phosphorylation regulates calpain-mediated truncation of glutamate ionotropic receptors. Brain Res 797:154–158
Bi X (2000) Calpain-mediated truncation of glutamate ionotropic receptors. Methods for studying the effects of calpain activation in brain tissue. Methods Mol Biol 144:203–217
Bi X (1998) Calpain-mediated proteolysis of GluR1 subunits in organotypic hippocampal cultures following kainic acid treatment. Brain Res 781:355–357
Wu HY (2005) Regulation of N-methyl-D-aspartate receptors by calpain in cortical neurons. J Biol Chem 280:21588–21593
Xu W (2007) Calpain-mediated mGluR1alpha truncation: a key step in excitotoxicity. Neuron 53:399–412
Tremper-Wells B (2005) Nuclear calpain regulates Ca2+-dependent signaling via proteolysis of nuclear Ca2+/calmodulin-dependent protein kinase type IV in cultured neurons. J Biol Chem 280:2165–2175
Sharkey J (1994) Immunophilins mediate the neuroprotective effects of FK506 in focal cerebral ischaemia. Nature 371:336–339
Uchino H (2002) Differential neuroprotection by cyclosporin A and FK506 following ischemia corresponds with differing abilities to inhibit calcineurin and the mitochondrial permeability transition. Neurobiol Dis 10:219–233
Shioda N (2007) Constitutively active calcineurin mediates delayed neuronal death through Fas-ligand expression via activation of NFAT and FKHR transcriptional activities in mouse brain ischemia. J Neurochem 102:1506–1517
Shioda N (2006) Generation of constitutively active calcineurin by calpain contributes to delayed neuronal death following mouse brain ischemia. J Neurochem 98:310–320
Neumar RW (1998) Calpain mediates eukaryotic initiation factor 4G degradation during global brain ischemia. J Cereb Blood Flow Metab 18:876–881
Petegnief V (2008) Nitric oxide mediates NMDA-induced persistent inhibition of protein synthesis through dephosphorylation of eukaryotic initiation factor 4E-binding protein 1 and eukaryotic initiation factor 4G proteolysis. Biochem J 411(3):667–677
Mao X (2002) Neuronal kappa B-binding factors consist of Sp1-related proteins. Functional implications for autoregulation of N-methyl-D-aspartate receptor-1 expression. J Biol Chem 277:44911–44919
Mao X (2007) Glutamate receptor activation evokes calpain-mediated degradation of Sp3 and Sp4, the prominent Sp-family transcription factors in neurons. J Neurochem 100:1300–1314
Gascon S (2005) Transcription of the NR1 subunit of the N-methyl-D-aspartate receptor is down-regulated by excitotoxic stimulation and cerebral ischemia. J Biol Chem 280:35018–35027
Hou ST (2006) Calpain-cleaved collapsin response mediator protein-3 induces neuronal death after glutamate toxicity and cerebral ischemia. J Neurosci 26:2241–2249
Jiang SX (2007) Calpain cleavage of collapsin response mediator proteins in ischemic mouse brain. Eur J Neurosci 26:801–809
Bretin S (2006) Calpain product of WT-CRMP2 reduces the amount of surface NR2B NMDA receptor subunit. J Neurochem 98:1252–1265
Rashidian J (2005) Multiple cyclin-dependent kinases signals are critical mediators of ischemia/hypoxic neuronal death in vitro and in vivo. Proc Natl Acad Sci U S A 102:14080–14085
Wen Y (2007) Cdk5 is involved in NFT-like tauopathy induced by transient cerebral ischemia in female rats. Biochim Biophys Acta 1772:473–483
Grundke-Iqbal I (1986) Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc Natl Acad Sci U S A 83:4913–4917
Haass C (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nat Rev Mol Cell Biol 8:101–112
Vincent B (2008) Regulation of betaAPP and PrPc cleavage by alpha-secretase: mechanistic and therapeutic perspectives. Curr Alzheimer Res 5:202–211
Lue LF (1999) Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer’s disease. Am J Pathol 155:853–862
Naslund J (2000) Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline. JAMA 283:1571–1577
De Felice FG (2007) Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 282:11590–11601
Demuro A (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280:17294–17300
Kelly BL (2006) Beta-amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons. J Biol Chem 281:28079–28089
Nixon RA (1994) Calcium-activated neutral proteinase (calpain) system in aging and Alzheimer’s disease. Ann N Y Acad Sci 747:77–91
Saito K (1993) Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc Natl Acad Sci U S A 90:2628–2632
Veeranna (2004) Calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons: relevance to Alzheimer’s disease. Am J Pathol 165:795–805
Chen M (2004) Stimulation of beta-amyloid precursor protein alpha-processing by phorbol ester involves calcium and calpain activation. Biochem Biophys Res Commun 316:332–340
Li QX (1995) Proteolytic processing of Alzheimer’s disease beta A4 amyloid precursor protein in human platelets. J Biol Chem 270:14140–14147
Siman R (1990) Proteolytic processing of beta-amyloid precursor by calpain I. J Neurosci 10:2400–2411
Chen M (2005) Mu-calpain is functionally required for alpha-processing of Alzheimer’s beta-amyloid precursor protein. Biochem Biophys Res Commun 330:714–721
Kelly BL (2005) Beta-amyloid-induced dynamin 1 depletion in hippocampal neurons. A potential mechanism for early cognitive decline in Alzheimer disease. J Biol Chem 280:31746–31753
Oddo S (2003) Triple-transgenic model of Alzheimer’s disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron 39:409–421
Yao PJ (2005) Preserved synaptic vesicle recycling in hippocampal neurons in a mouse Alzheimer’s disease model. Biochem Biophys Res Commun 330:34–38
Barco A (2002) Expression of constitutively active CREB protein facilitates the late phase of long-term potentiation by enhancing synaptic capture. Cell 108:689–703
Liang Z (2007) Down-regulation of cAMP-dependent protein kinase by over-activated calpain in Alzheimer disease brain. J Neurochem 103:2462–2470
Shiraha H (2002) Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain. Mol Cell Biol 22:2716–2727
Lakshmikuttyamma A (2004) In vitro proteolytic degradation of bovine brain calcineurin by m-calpain. Neurochem Res 29:1913–1921
Wang KK (1989) Characterization of the fragmented forms of calcineurin produced by calpain I. Biochem Cell Biol 67:703–711
Liu F (2005) Truncation and activation of calcineurin A by calpain I in Alzheimer disease brain. J Biol Chem 280:37755–37762
Delobel P (2003) Stable-tau overexpression in human neuroblastoma cells: an open door for explaining neuronal death in tauopathies. Ann N Y Acad Sci 1010:623–634
Zheng YL (2005) A Cdk5 inhibitory peptide reduces tau hyperphosphorylation and apoptosis in neurons. Embo J 24:209–220
Kishimoto A (1989) Limited proteolysis of protein kinase C subspecies by calcium-dependent neutral protease (calpain). J Biol Chem 264:4088–4092
Yoshimura Y (1996) Purification and characterization of active fragment of Ca2+/calmodulin-dependent protein kinase II from the post-synaptic density in the rat forebrain. J Biochem 119:268–273
Shea TB (1996) Calcium influx into human neuroblastoma cells induces ALZ-50 immunoreactivity: involvement of calpain-mediated hydrolysis of protein kinase C. J Neurochem 66:1539–1549
Lucas JJ (2001) Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. Embo J 20:27–39
Goni-Oliver P (2007) N-terminal cleavage of GSK-3 by calpain: a new form of GSK-3 regulation. J Biol Chem 282:22406–22413
Forde JE (2007) Glycogen synthase kinase 3: a key regulator of cellular fate. Cell Mol Life Sci 64:1930–1944
Abe K (2007) NMDA-receptor activation induces calpain-mediated beta-catenin cleavages for triggering gene expression. Neuron 53:387–397
Chong ZZ (2005) Stress in the brain: novel cellular mechanisms of injury linked to Alzheimer’s disease. Brain Res Brain Res Rev 49:1–21
Monaco EA 3rd (2004) Recent evidence regarding a role for Cdk5 dysregulation in Alzheimer’s disease. Curr Alzheimer Res 1:33–38
Tsai LH (1994) p35 is a neural-specific regulatory subunit of cyclin-dependent kinase 5. Nature 371:419–423
Jamsa A (2006) Glutamate treatment and p25 transfection increase Cdk5 mediated tau phosphorylation in SH-SY5Y cells. Biochem Biophys Res Commun 345:324–331
Patrick GN (1999) Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature 402:615–622
Alvarez A (1999) Inhibition of tau phosphorylating protein kinase cdk5 prevents beta-amyloid-induced neuronal death. FEBS Lett 459:421–426
Lopes JP (2007) Role of cyclin-dependent kinase 5 in the neurodegenerative process triggered by amyloid-beta and prion peptides: implications for Alzheimer’s disease and prion-related encephalopathies. Cell Mol Neurobiol 27:943–957
Saito T (2007) p25/cyclin-dependent kinase 5 promotes the progression of cell death in nucleus of endoplasmic reticulum-stressed neurons. J Neurochem 102:133–140
Becker EB (2004) Cell cycle regulation of neuronal apoptosis in development and disease. Prog Neurobiol 72:1–25
Weishaupt JH (2003) Inhibition of CDK5 is protective in necrotic and apoptotic paradigms of neuronal cell death and prevents mitochondrial dysfunction. Mol Cell Neurosci 24:489–502
Wittmann CW (2001) Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles. Science 293:711–714
Yoshiyama Y (2003) Reduction of detyrosinated microtubules and Golgi fragmentation are linked to tau-induced degeneration in astrocytes. J Neurosci 23:10662–10671
Park SY (2005) The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration. J Neurosci 25:5365–5375
Amadoro G (2006) NMDA receptor mediates tau-induced neurotoxicity by calpain and ERK/MAPK activation. Proc Natl Acad Sci U S A 103:2892–2897
Farrer MJ (2006) Genetics of Parkinson disease: paradigm shifts and future prospects. Nat Rev Genet 7:306–318
Hirsch EC (1992) Why are nigral catecholaminergic neurons more vulnerable than other cells in Parkinson’s disease? Ann Neurol 32(Suppl):S88–S93
Iacopino AM (1990) Specific reduction of calcium-binding protein (28-kilodalton calbindin-D) gene expression in aging and neurodegenerative diseases. Proc Natl Acad Sci U S A 87:4078–4082
Mouatt-Prigent A (1994) Does the calcium binding protein calretinin protect dopaminergic neurons against degeneration in Parkinson’s disease? Brain Res 668:62–70
Mouatt-Prigent A (1996) Increased m-calpain expression in the mesencephalon of patients with Parkinson’s disease but not in other neurodegenerative disorders involving the mesencephalon: a role in nerve cell death? Neuroscience 73:979–987
Kiuchi K (1991) Limited proteolysis of tyrosine hydroxylase by Ca(2+)-activated neutral protease (calpain). Biochemistry 30:10416–10419
Barzilai A (2000) The molecular mechanism of dopamine-induced apoptosis: identification and characterization of genes that mediate dopamine toxicity. J Neural Transm Suppl 59–76
Tabrizi SJ (2000) Expression of mutant alpha-synuclein causes increased susceptibility to dopamine toxicity. Hum Mol Genet 9:2683–2689
Tehranian R (2006) Alpha-synuclein inhibits aromatic amino acid decarboxylase activity in dopaminergic cells. J Neurochem 99:1188–1196
Mouatt-Prigent A (2000) Calpastatin immunoreactivity in the monkey and human brain of control subjects and patients with Parkinson’s disease. J Comp Neurol 419:175–192
Langston JW (1983) Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 219:979–980
Chiba K (1984) Metabolism of the neurotoxic tertiary amine, MPTP, by brain monoamine oxidase. Biochem Biophys Res Commun 120:574–578
Wu DC (2003) NADPH oxidase mediates oxidative stress in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine model of Parkinson’s disease. Proc Natl Acad Sci U S A 100:6145–650
Chen TS (1995) MPP+ selectively affects calcium homeostasis in mesencephalic cell cultures from embryonal C57/Bl6 mice. J Neural Transm Gen Sect 100:153–163
Crocker SJ (2003) Inhibition of calpains prevents neuronal and behavioral deficits in an MPTP mouse model of Parkinson’s disease. J Neurosci 23:4081–4091
Radke JM (1998) Atypical antipsychotic drugs selectively increase neurotensin efflux in dopamine terminal regions. Proc Natl Acad Sci U S A 95:11462–11464
Martorana A (2001) Dopamine denervation induces neurotensin immunoreactivity in GABA-parvalbumin striatal neurons. Synapse 41:360–362
Schimpff RM (2001) Increased plasma neurotensin concentrations in patients with Parkinson’s disease. J Neurol Neurosurg Psychiatry 70:784–786
Liou AK (2005) BimEL up-regulation potentiates AIF translocation and cell death in response to MPTP. Faseb J 19:1350–1352
Cao G (2007) Critical role of calpain I in mitochondrial release of apoptosis-inducing factor in ischemic neuronal injury. J Neurosci 27:9278–9293
Mishizen-Eberz AJ (2003) Distinct cleavage patterns of normal and pathologic forms of alpha-synuclein by calpain I in vitro. J Neurochem 86:836–47
Mishizen-Eberz AJ (2005) Cleavage of alpha-synuclein by calpain: potential role in degradation of fibrillized and nitrated species of alpha-synuclein. Biochemistry 44:7818–7829
Li W (2005) Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson’s disease-linked mutations. Proc Natl Acad Sci U S A 102:2162–2167
Dufty BM (2007) Calpain-cleavage of alpha-synuclein: connecting proteolytic processing to disease-linked aggregation. Am J Pathol 170:1725–1738
Tofaris GK (2006) Pathological changes in dopaminergic nerve cells of the substantia nigra and olfactory bulb in mice transgenic for truncated human alpha-synuclein(1–120): implications for Lewy body disorders. J Neurosci 26:3942–3950
Shimura H (2000) Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet 25:302–305
Zhang Y (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc Natl Acad Sci U S A 97:13354–13359
Kim SJ (2003) Parkin cleaves intracellular alpha-synuclein inclusions via the activation of calpain. J Biol Chem 278:41890–41899
Chen MJ (2006) Early induction of calpains in rotenone-mediated neuronal apoptosis. Neurosci Lett 397:69–73
Kruman II (2004) Cell cycle activation linked to neuronal cell death initiated by DNA damage. Neuron 41:549–561
Sedarous M (2003) Calpains mediate p53 activation and neuronal death evoked by DNA damage. J Biol Chem 278:26031–26038
Kubbutat MH (1997) Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol Cell Biol 17:460–468
Samantaray S (2007) The parkinsonian neurotoxin rotenone activates calpain and caspase-3 leading to motoneuron degeneration in spinal cord of Lewis rats. Neuroscience 146:741–755
Samantaray S (2006) Calpain activation in apoptosis of motoneurons in cell culture models of experimental parkinsonism. Ann N Y Acad Sci 1074:349–356
Cohen G (1974) The generation of hydrogen peroxide, superoxide radical, and hydroxyl radical by 6-hydroxydopamine, dialuric acid, and related cytotoxic agents. J Biol Chem 249:2447–2452
Saito Y (2007) Molecular mechanisms of 6-hydroxydopamine-induced cytotoxicity in PC12 cells: involvement of hydrogen peroxide-dependent and -independent action. Free Radic Biol Med 42:675–685
Hirai S (1991) Degradation of transcription factors, c-Jun and c-Fos, by calpain. FEBS Lett 287:57–61
Xia XG (2001) Gene transfer of the JNK interacting protein-1 protects dopaminergic neurons in the MPTP model of Parkinson’s disease. Proc Natl Acad Sci U S A 98:10433–10438
Qu D (2007) Role of Cdk5-mediated phosphorylation of Prx2 in MPTP toxicity and Parkinson’s disease. Neuron 55:37–52
Smith PD (2006) Calpain-regulated p35/cdk5 plays a central role in dopaminergic neuron death through modulation of the transcription factor myocyte enhancer factor 2. J Neurosci 26:440–447
Avraham E (2007) Phosphorylation of Parkin by the cyclin-dependent kinase 5 at the linker region modulates its ubiquitin-ligase activity and aggregation. J Biol Chem 282:12842–12850
Alvira D (2007) Activation of the calpain/cdk5/p25 pathway in the girus cinguli in Parkinson’s disease. Parkinsonism Relat Disord 14(4):309–313
Alvira D (2006) Inhibition of the cdk5/p25 fragment formation may explain the antiapoptotic effects of melatonin in an experimental model of Parkinson’s disease. J Pineal Res 40:251–258
(1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington’s disease chromosomes. The Huntington’s Disease Collaborative Research Group. Cell 72:971–983
Ferrante RJ (1985) Selective sparing of a class of striatal neurons in Huntington’s disease. Science 230:561–563
Cudkowicz M (1990) Degeneration of pyramidal projection neurons in Huntington’s disease cortex. Ann Neurol 27:200–204
Brouillet E (1998) Partial inhibition of brain succinate dehydrogenase by 3-nitropropionic acid is sufficient to initiate striatal degeneration in rat. J Neurochem 70:794–805
Brouillet E (1995) Chronic mitochondrial energy impairment produces selective striatal degeneration and abnormal choreiform movements in primates. Proc Natl Acad Sci U S A 92:7105–7109
Panov AV (2002) Early mitochondrial calcium defects in Huntington’s disease are a direct effect of polyglutamines. Nat Neurosci 5:731–736
Panov AV (2005) Ca2+-induced permeability transition in human lymphoblastoid cell mitochondria from normal and Huntington’s disease individuals. Mol Cell Biochem 269:143–152
Hodgson JG (1999) A YAC mouse model for Huntington’s disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration. Neuron 23:181–192
Li H (2000) Amino-terminal fragments of mutant huntingtin show selective accumulation in striatal neurons and synaptic toxicity. Nat Genet 25:385–389
Chen N (1999) Subtype-specific enhancement of NMDA receptor currents by mutant huntingtin. J Neurochem 72:1890–1898
Zeron MM (2002) Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington’s disease. Neuron 33:849–860
Fernandes HB (2007) Mitochondrial sensitivity and altered calcium handling underlie enhanced NMDA-induced apoptosis in YAC128 model of Huntington’s disease. J Neurosci 27:13614–13623
Brustovetsky N (2003) Increased susceptibility of striatal mitochondria to calcium-induced permeability transition. J Neurosci 23:4858–4867
Brustovetsky N (2005) Age-dependent changes in the calcium sensitivity of striatal mitochondria in mouse models of Huntington’s disease. J Neurochem 93:1361–1370
Galas MC (2004) Death of cortical and striatal neurons induced by mitochondrial defect involves differential molecular mechanisms. Neurobiol Dis 15:152–159
Jacquard C (2006) Brain mitochondrial defects amplify intracellular [Ca2+] rise and neurodegeneration but not Ca2+ entry during NMDA receptor activation. Faseb J 20:1021–1023
DiFiglia M (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277:1990–1993
Sapp E (1997) Huntingtin localization in brains of normal and Huntington’s disease patients. Ann Neurol 42:604–612
Davies SW (1997) Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90:537–548
Scherzinger E (1997) Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 90:549–58
Goldberg YP (1996) Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nat Genet 13:442–449
Wellington CL (1998) Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J Biol Chem 273:9158–9167
Kim YJ (2001) Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington’s disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc Natl Acad Sci U S A 98:12784–12789
Sun B (2002) Polyglutamine repeat length-dependent proteolysis of huntingtin. Neurobiol Dis 11:111–122
Goffredo D (2002) Calcium-dependent cleavage of endogenous wild-type huntingtin in primary cortical neurons. J Biol Chem 277:39594–39598
Hackam AS (1998) The influence of huntingtin protein size on nuclear localization and cellular toxicity. J Cell Biol 141:1097–1105
Bizat N (2003) Calpain is a major cell death effector in selective striatal degeneration induced in vivo by 3-nitropropionate: implications for Huntington’s disease. J Neurosci 23:5020–5030
Gafni J (2004) Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus. J Biol Chem 279:20211–20220
Bizat N (2003) In vivo calpain/caspase cross-talk during 3-nitropropionic acid-induced striatal degeneration: implication of a calpain-mediated cleavage of active caspase-3. J Biol Chem 278:43245–43253
Bizat N (2005) Neuroprotective effect of zVAD against the neurotoxin 3-nitropropionic acid involves inhibition of calpain. Neuropharmacology 49:695–702
Crespo-Biel N (2007) 3-Nitropropionic acid activates calpain/cdk5 pathway in rat striatum. Neurosci Lett 421:77–81
Luo S (2005) Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: implications for mutant huntingtin toxicity. J Cell Biol 169:647–656
Anne SL (2007) Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced by DNA damage and regulates wild-type and mutant huntingtin toxicity in neurons. J Neurosci 27:7318–7328
Ofosu-Appiah W (1991) Characterization of in vivo-activated T cell clones from peripheral blood of multiple sclerosis patients. Clin Immunol Immunopathol 58:46–55
Compston A (2004) The pathogenesis and basis for treatment in multiple sclerosis. Clin Neurol Neurosurg 106:246–248
Hohlfeld R (2004) Autoimmune concepts of multiple sclerosis as a basis for selective immunotherapy: from pipe dreams to (therapeutic) pipelines. Proc Natl Acad Sci U S A 101(Suppl 2):14599–14606
Inuzuka T (1987) Neutral protease in cerebrospinal fluid from patients with multiple sclerosis and other neurological diseases. Acta Neurol Scand 76:18–23
Shields DC (1999) Pathophysiological role of calpain in experimental demyelination. J Neurosci Res 55:533–541
Clementi E (1994) Intracellular Ca2+ stores of T lymphocytes: changes induced by in vitro and in vivo activation. Eur J Immunol 24:1365–1371
Deshpande RV (1993) Differential distribution of calpain in human lymphoid cells. Neurochem Res 18:767–773
Deshpande RV (1995) Calpain expression in lymphoid cells. Increased mRNA and protein levels after cell activation. J Biol Chem 270:2497–2505
Deshpande RV (1995) Calpain secreted by activated human lymphoid cells degrades myelin. J Neurosci Res 42:259–265
Shields DC (1998) Upregulation of calpain activity and expression in experimental allergic encephalomyelitis: a putative role for calpain in demyelination. Brain Res 794:68–74
Shields DC (1998) Increased calpain expression in experimental demyelinating optic neuritis: an immunocytochemical study. Brain Res 784:299–304
Schaecher K (2002) Calpain expression and infiltration of activated T cells in experimental allergic encephalomyelitis over time: increased calpain activity begins with onset of disease. J Neuroimmunol 129:1–9
Guyton MK (2005) Upregulation of calpain correlates with increased neurodegeneration in acute experimental auto-immune encephalomyelitis. J Neurosci Res 81:53–61
Diaz-Sanchez M (2006) Protein co-expression with axonal injury in multiple sclerosis plaques. Acta Neuropathol 111:289–299
Shields DC (1999) A putative mechanism of demyelination in multiple sclerosis by a proteolytic enzyme, calpain. Proc Natl Acad Sci U S A 96:11486–11491
Benveniste EN (1995) TNF-alpha- and IFN-gamma-mediated signal transduction pathways: effects on glial cell gene expression and function. Faseb J 9:1577–1584
Smith ME (1998) Effects of phorbol myristate acetate (PMA) on functions of macrophages and microglia in vitro. Neurochem Res 23:427–434
Benjamins JA (2003) Protection of mature oligodendrocytes by inhibitors of caspases and calpains. Neurochem Res 28:143–152
Jurewicz A (2005) Tumour necrosis factor-induced death of adult human oligodendrocytes is mediated by apoptosis inducing factor. Brain 128:2675–2688
Das A (2006) Calpeptin provides functional neuroprotection to rat retinal ganglion cells following Ca2+ influx. Brain Res 1084:146–157
Hassen GW (2006) A novel calpain inhibitor for the treatment of acute experimental autoimmune encephalomyelitis. J Neuroimmunol 180:135–146
Imam SA (2007) Increased calpain correlates with Th1 cytokine profile in PBMCs from MS patients. J Neuroimmunol 190:139–145
Wopfner F (1999) Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein. J Mol Biol 289:1163–1178
Zanusso G (1998) Prion protein expression in different species: analysis with a panel of new mAbs. Proc Natl Acad Sci U S A 95:8812–8816
Chen SG (1995) Truncated forms of the human prion protein in normal brain and in prion diseases. J Biol Chem 270:19173–19180
Ma J (2002) Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298:1781–1785
Wang X (2005) Calpain and other cytosolic proteases can contribute to the degradation of retro-translocated prion protein in the cytosol. J Biol Chem 280:317–325
Watt NT (2005) Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress. J Biol Chem 280:35914–35921
Kristensson K (1993) Scrapie prions alter receptor-mediated calcium responses in cultured cells. Neurology 43:2335–2341
Xiao YF (2000) Mechanism of suppression of cardiac L-type Ca(2+) currents by the phospholipase A(2) inhibitor mepacrine. Eur J Pharmacol 399:107–116
O’Donovan CN (2001) Prion protein fragment PrP-(106–126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells. J Biol Chem 276:43516–43523
Yadavalli R (2004) Calpain-dependent endoproteolytic cleavage of PrPSc modulates scrapie prion propagation. J Biol Chem 279:21948–21956
Gray BC (2006) Increased expression of glial fibrillary acidic protein fragments and mu-calpain activation within the hippocampus of prion-infected mice. Biochem Soc Trans 34:51–54
Du S (1999) Calcium influx and activation of calpain I mediate acute reactive gliosis in injured spinal cord. Exp Neurol 157:96–105
Lee YB (2000) Rapid increase in immunoreactivity to GFAP in astrocytes in vitro induced by acidic pH is mediated by calcium influx and calpain I. Brain Res 864:220–229
Riemenschneider M (2003) Phospho-tau/total tau ratio in cerebrospinal fluid discriminates Creutzfeldt–Jakob disease from other dementias. Mol Psychiatry 8:343–347
Cleveland DW (1999) From Charcot to SOD1: mechanisms of selective motor neuron death in ALS. Neuron 24:515–520
Ludolph AC (2000) The role of excitotoxicity in ALS—what is the evidence? J Neurol 247 Suppl 1:17–16
Ludolph AC (1998) Amyotrophic lateral sclerosis and glutamate. Restor Neurol Neurosci 13:59–67
Alexianu ME (1994) The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis. Ann Neurol 36:846–858
Siklos L (1998) Intracellular calcium parallels motoneuron degeneration in SOD-1 mutant mice. J Neuropathol Exp Neurol 57:571–587
Beers DR (2001) Parvalbumin overexpression alters immune-mediated increases in intracellular calcium, and delays disease onset in a transgenic model of familial amyotrophic lateral sclerosis. J Neurochem 79:499–509
Malik MN (1986) Purification and degradation of purified neurofilament proteins by the brain calcium-activated neutral proteases. Life Sci 39:1335–1343
Pant HC (1988) Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain. Biochem J 256:665–668
Johnson GV (1991) The regulatory role of calmodulin in the proteolysis of individual neurofilament proteins by calpain. Neurochem Res 16:869–873
Strong MJ (2001) Phosphorylation state of the native high-molecular-weight neurofilament subunit protein from cervical spinal cord in sporadic amyotrophic lateral sclerosis. J Neurochem 76:1315–1325
Bajaj NP (1999) Cyclin dependent kinase-5 (CDK-5) phosphorylates neurofilament heavy (NF-H) chain to generate epitopes for antibodies that label neurofilament accumulations in amyotrophic lateral sclerosis (ALS) and is present in affected motor neurones in ALS. Prog Neuropsychopharmacol Biol Psychiatry 23:833–850
Nguyen MD (2001) Deregulation of Cdk5 in a mouse model of ALS: toxicity alleviated by perikaryal neurofilament inclusions. Neuron 30:135–147
Couillard-Despres S (1998) Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase. Proc Natl Acad Sci U S A 95:9626–9630
Takahashi S (2004) Mutant superoxide dismutase 1 causes motor neuron degeneration independent of cyclin-dependent kinase 5 activation by p35 or p25. J Neurochem 88:1295–1304
Wootz H (2006) XIAP decreases caspase-12 cleavage and calpain activity in spinal cord of ALS transgenic mice. Exp Cell Res 312:1890–1898
Cardali S (2006) Detection of alphaII-spectrin and breakdown products in humans after severe traumatic brain injury. J Neurosurg Sci 50:25–31
Lewis SB (2007) Alpha-II spectrin breakdown products in aneurysmal subarachnoid hemorrhage: a novel biomarker of proteolytic injury. J Neurosurg 107:792–796
Siman R (2005) Novel surrogate markers for acute brain damage: cerebrospinal fluid levels corrrelate with severity of ischemic neurodegeneration in the rat. J Cereb Blood Flow Metab 25:1433–1444
Polster BM (2005) Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria. J Biol Chem 280:6447–6454
Reimertz C (2001) Ca(2+)-induced inhibition of apoptosis in human SH-SY5Y neuroblastoma cells: degradation of apoptotic protease activating factor-1 (APAF-1). J Neurochem 78:1256–1266
Choi WS (2001) Cleavage of Bax is mediated by caspase-dependent or -independent calpain activation in dopaminergic neuronal cells: protective role of Bcl-2. J Neurochem 77:1531–1541
Wood DE (1998) Bax cleavage is mediated by calpain during drug-induced apoptosis. Oncogene 17:1069–1078
Nakagawa T (2000) Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 150:887–894
Takano J (2005) Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice. J Biol Chem 280:16175–16184
Kim MJ (2002) Calpain-dependent cleavage of cain/cabin1 activates calcineurin to mediate calcium-triggered cell death. Proc Natl Acad Sci U S A 99:9870–9875
Covault J (1991) Calcium-activated proteolysis of intracellular domains in the cell adhesion molecules NCAM and N-cadherin. Brain Res Mol Brain Res 11:11–16
Hajimohammadreza I (1997) Neuronal nitric oxide synthase and calmodulin-dependent protein kinase IIalpha undergo neurotoxin-induced proteolysis. J Neurochem 69:1006–1013
Tallant EA (1988) Activation of a calmodulin-dependent phosphatase by a Ca2+-dependent protease. Biochemistry 27:2205–2211
Blomgren K (2001) Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia: a mechanism of “pathological apoptosis”? J Biol Chem 276:10191–10198
Chua BT (2000) Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. J Biol Chem 275:5131–5135
Ruiz-Vela A (1999) Implication of calpain in caspase activation during B cell clonal deletion. Embo J 18:4988–4998
Volbracht C (2005) The critical role of calpain versus caspase activation in excitotoxic injury induced by nitric oxide. J Neurochem 93:1280–1292
Nakagawa T (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403:98–103
Krajewska M (2004) Early processing of Bid and caspase-6, -8, -10, -14 in the canine brain during cardiac arrest and resuscitation. Exp Neurol 189:261–279
Ohno H (2007) Ischemia promotes calpain-mediated degradation of p120-catenin in SH-SY5Y cells. Biochem Biophys Res Commun 353:547–552
Zakharov VV (2001) Site-specific calcium-dependent proteolysis of neuronal protein GAP-43. Neurosci Res 39:447–453
Zakharov VV (2007) M-calpain-mediated cleavage of GAP-43 near Ser41 is negatively regulated by protein kinase C, calmodulin and calpain-inhibiting fragment GAP-43–3. J Neurochem 101:1539–1551
Yuen EY (2007) Calpain regulation of AMPA receptor channels in cortical pyramidal neurons. J Physiol 580:241–254
Lee SY (1990) Purification and properties of D-myo-inositol 1,4,5-trisphosphate 3-kinase from rat brain. Susceptibility to calpain. J Biol Chem 265:9434–9440
Yoshihara Y (1990) Purification of a novel type of calcium-activated neutral protease from rat brain. Possible involvement in production of the neuropeptide kyotorphin from calpastatin fragments. J Biol Chem 265:5809–5815
Yoshihara Y (1988) Calcium-activated neutral protease (CANP), a putative processing enzyme of the neuropeptide, kyotorphin, in the brain. Biochem Biophys Res Commun 155:546–553
Sato C (1986) Rapid proteolysis of brain MAP-1 related cytoskeleton-associated 350 kd protein by purified calpain. Cell Struct Funct 11:253–257
Inuzuka T (1990) Changes in the concentrations of cerebral proteins following occlusion of the middle cerebral artery in rats. Stroke 21:917–922
Posmantur RM (1996) Cytoskeletal derangements of cortical neuronal processes three hours after traumatic brain injury in rats: an immunofluorescence study. J Neuropathol Exp Neurol 55:68–80
Dong YN (2004) Interactions of postsynaptic density-95 and the NMDA receptor 2 subunit control calpain-mediated cleavage of the NMDA receptor. J Neurosci 24:11035–11045
Banno Y (1995) Endogenous cleavage of phospholipase C-beta 3 by agonist-induced activation of calpain in human platelets. J Biol Chem 270:4318–4324
Low MG (1984) Multiple forms of phosphoinositide-specific phospholipase C of different relative molecular masses in animal tissues. Evidence for modification of the platelet enzyme by Ca2+-dependent proteinase. Biochem J 221:813–820
Park D (1993) Removal of the carboxyl-terminal region of phospholipase C-beta 1 by calpain abolishes activation by G alpha q. J Biol Chem 268:3710–3714
Boland B (2003) beta-Amyloid (1–40)-induced apoptosis of cultured cortical neurones involves calpain-mediated cleavage of poly-ADP-ribose polymerase. Neurobiol Aging 24:179–186
Mikawa K (1990) Studies on proteolysis of protein kinase C with calpain I and II. Kobe J Med Sci 36:55–69
Sessoms JS (1992) Ca(2+)-induced persistent protein kinase C activation in rat hippocampal homogenates. Second Messengers Phosphoprot 14:109–126
Ziemka-Nalecz M (2003) Decrease of PKC precedes other cellular signs of calpain activation in area CA1 of the hippocampus after transient cerebral ischemia. Neurochem Int 42:205–214
Lu X (2000) Calpain-mediated degradation of PSD-95 in developing and adult rat brain. Neurosci Lett 286:149–153
Jourdi H (2005) Effects of positive AMPA receptor modulators on calpain-mediated spectrin degradation in cultured hippocampal slices. Neurochem Int 46:31–40
Xie HQ (1998) Calcineurin inhibition prevents calpain-mediated proteolysis of tau in differentiated PC12 cells. J Neurosci Res 53:153–164