39
Views
35
CrossRef citations to date
0
Altmetric
Review

Calpain inhibitors as potential treatment for stroke and other neurodegenerative diseases: recent trends and developments

&
Pages 1707-1727 | Published online: 25 Feb 2005

Bibliography

  • OTTO H-H, SCHIRMEISTER T: Cysteine proteases and their inhibitors. Chem. Rev. (1997) 97:133–171.
  • GUROFF G: A neutral, calcium-activated proteinase from the soluble fraction of rat brain. J. Biol. Chem. (1964) 239:149–155.
  • •First description of calpain.
  • MURACHI T: Calpain and calpastatin. Trends Biochem. Sci. (1983) 8:167–169.
  • OJHA M, WALLACE C: Novel Ca2±-activated neutral pro-tease from an aquatic fungus, Allomyces arbuscula. J. Bacteriol. (1988) 170:1254–1260.
  • PINTER M, FRIEDRICH P: The calcium-dependent prote-olytic system calpain-calpastatin in Drosophila mela-nogaster. Biochem. J. (1988) 253:467–473.
  • JOHNSON P: Calpains (intracellular calcium-activated cysteine proteinases): structure-activity relationships and involvement in normal and abnormal cellular me-tabolism. Int. J. Biochem. (1990) 22:811–822.
  • OJHA M: Ca(2+)-dependent protease I from Allomyces arbuscula. Biochem. Biophys. Res. Commun. (1996) 218:22–29.
  • NOMENCLATURE COMMITTEE OF THE INTERNATIONALUNION OF BIOCHEMISTRY (NC-IUB): Enzyme nomencla-ture. Recommendations 1978. Supplement 2: Corrections and Additions. Eur. j Biochem. (1981) 116:423–435.
  • SORIMACHI H, SAIDO TC, SUZUKI K: New era of calpainresearch. Discovery of tissue-specific calpains. FEBS Lett. (1994) 343:1–5.
  • SUZUKI K, OHNO S: Calcium activated neutral proteasestructure-function relationship and functional impli-cations. Cell Struct. Funct. (1990) 156:1–6.
  • OHNO S, EMORI Y, IMAJOH S, KAWASAKI H, KISARAGI M,SUZUKI K: Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein? Nature (1984) 312:566–570.
  • SAKIHAMA T, KAKIDANI H, ZENITA K et al.: A putativeCa2±-binding protein: structure of the light subunit of porcine calpain elucidated by molecular cloning and protein sequence analysis. Proc. Natl. Acad. Sci. USA (1985) 82:6075–6079.
  • LIN GD, CHATTOPADHYAY D, MAKI M et al.: Crystalstructure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regula-tion, and inhibitor binding. Nature Struct. Biol. (1997) 4:539–547.
  • WANG KKW, YUEN P-W: Calpain inhibition: an over-view of its therapeutic potential. Trends Pharm. Sci. (1994) 15:412–419.
  • AOKI K: Complete amino acid sequence of the largesubunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence. FEBS Lett. (1986) 205:313–317.
  • SAIDO T, SORIMACHI H, SUZUKI K: Calpain: new per-spectives in molecular diversity and physiological-pathological involvement. FASEB J (1994) 8:814–822.
  • CROALL DE, DEMARTINO GN: Calcium-activated neutralprotease (calpain) system: structure, function and regulation. Physiol. Rev. (1991) 71:813–847.
  • BARTUS RT: The calpain hypothesis of neurodegenera-tion: evidence for a common cytotoxic pathway. Neu-roscientist (1997) 3:314–327.
  • MURACHI T: Intracellular Ca2+ protease and its inhibi-tor protein: calpain and calpastatin. In: Calcium and Cell Function (Volume 4). Cheung WY (Ed.), Academic Press, New York (1983):377–410.
  • SIMAN R, NOSZEK JC, KEGERISE C: Calpain I activation isspecifically related to excitatory amino acid induction of hippocampal damage. J. Neurosci. (1989) 9:1579–1590.
  • MEHDI S: Cell-penetrating inhibitors of calpain. Trends Biochem. Sci. (1991) 16:150–153.
  • WANG KKW: Developing selective inhibitors of cal-pain. Trends Pharm. Sci. (1990) 11:139–142.
  • MELLONI E, PONTREMOLI S: The calpains. Trends Neuro-sci. (1989) 12:438–444.
  • SUZUKI K, SORIMACHI H, YOSHIZAWA T, KINBARA K, ISHIURA S: Calpain: novel family members, activation, and physiological function. Biol. Chem. Hoppe Seyler. (1995) 376:523–529.
  • WANG KKW, VILLALOBO A, ROUFOGALIS BD: Calmodulin-binding proteins as calpain substrates. Biochem. J. (1989) 262:693–706.
  • SHOSHAN-BARMATZ V, WEIL S, MEYER H, VARSANYI M,HEILMEYER LM: Endogenous Ca(2+)-dependent cysteine-protease cleaves specifically the ryanodine receptor/Ca2+ release channel in skeletal muscle. J. Membrane Biol. (1994) 142:281–288.
  • TAKAHASHI K: Calpain substrate specificity. In: Intra-cellular Calcium Dependent Proteolysis. Mellgren RI, Mura-chi T (Eds.), CRC Press, Boca Raton (FL) (1990):55–74.
  • MELLONI E, SALAMINO F, SPARATORE B: The calpain-calpastatin system in mammalian cells: properties and possible functions. Biochemie (1992) 74:217–223.
  • SUZUKI K, SAIDO TC, HIRAI S: Modulation of cellularsignals by calpain. Ann. NY Acad. ScL (1992) 674:218–227.
  • SEUBERT P, LYNCH G: Plasticity to pathology: brain cal-pains as modifiers of synaptic structure. In: Intracellu-lar Calcium Dependent Proteolysis. CRC Press, Boca Raton (FL) (1990):251–263.
  • SHEA TB, CRESSMAN CM, SPENCER MJ, BEERMAN ML, NIXON RA: Enhancement of neurite outgrowth follow-ing calpain inhibition is mediated by protein kinase C. Neurochem. (1995):517–527.
  • NIXON RA: Calcium-activated neutral proteinases asregulators of cellular function: implication for Alz-heimer's disease pathogenesis. Ann. NY Acad. ScL (1989) 568:198–206.
  • LYNCH G, BAUDRY M: The biochemistry of memory: anew and specific hypothesis. Science (1984) 224:1057–1063.
  • MELDRUM B, GARTHWAITE J: Excitatory amino acid neurotoxicity and neurodegenerative disease. Trends Pharmacol. ScL (1990) 11:379–387.
  • LIPTON SA, ROSENBERG PA: Excitatory amino acids as afinal common pathway for neurologic disorders. New Engl. J. Med. (1994) 330:613–622.
  • KOROSHETZ WJ, MOSKOWITZ MA: Emerging treat-ments for stroke in humans. Trends. Pharmacol ScL (1996) 17:227–233.
  • BARINAGA M: Finding new drugs to treat stroke. Science(1996) 272:664–666.
  • SIMAN R, BOZYCZKO-COYNE D, SCOTT RW: Proteolyticmechanisms of ischemic neurodegeneration. In: Cere-bro vascularDisease. Ginsberg MD, Bogousslavsky J (Eds.), Blackwell, Cambridge, MA (1998):721–734.
  • WANG KKW, NATH R, POSNER A et al.: An alpha-mercaptoacrylic acid derivative is a selective nonpep-tide cell-permeable calpain inhibitor and is neuropro-tective. Proc. Natl. Acad. Sci. USA (1996) 93:6687–6692.
  • MARKGRAF CG, VELAYO NL, JOHNSON MP et al.: Six-hour window of opportunity for calpain inhibition in focal cerebral ischaemia in rats. Stroke (1998) 29:152–158.
  • ••Z-Val-Phe-H (MDL 28170) reduced infarct volume in a ratmiddle cerebral occlusion model of ischaemia when admin-istered 0.5-6 h after ischaemia.
  • ROTHMAN SM, OLNEY JW: Glutamate and pathophysi-ology of hypoxic-ischemic brain damage. Ann. Neurol (1986) 19:105–111.
  • SIESJO BK, BENGTSSON F: Calcium fluxes, calcium an-tagonists, and calcium-related pathology in brain is-chaemia, hypoglycemia, and spreading depression: a unifying hypothesis. J. Cereb. Blood Flow Metab. (1989) 9:127–140.
  • SEUBERT P, LEE K, LYNCH G: Ischaemia triggers NMDA receptor-linked cytoskeletal proteolysis in hippocam-pus. Brain Res. (1989) 492:366–370.
  • ARAI A, VANDERKLISH P, KESSLER M, LEE K, LYNCH G: A brief period of hypoxia causes proteolysis of cyto-skeletal proteins in hippocampal slices. Brain Res. (1991) 555:276–280.
  • SIMAN R, NOSZEK JC: Excitatory amino acids activate calpain and induce structural protein breakdown in vivo. Neuron (1988) 1:279–287.
  • BRORSON JR, MANZOLILLO PA, MILLER RJ: Ca2+ entry via AMPA/KA receptors and excitotoxicity in cultured cerebellar Purkinje cells. J. NeuroscL (1994) 14:187–197.
  • MANEV H, FAVARON M, SIMAN R, GUIDOTTI A, COSTA E: Glutamate neurotoxicity is independent of calpain I inhibition in primary cultures of cerebellar granule cells. J. Neurochem. (1991) 57:1288–1295.
  • DISTASI AM, GALLO V, CECCARINI M, PETRUCCI TC: Neu-ronal fodrin proteolysis occurs independently of exci-tatory amino acid-induced neurotoxicity. Neuron (1991) 6:445–454.
  • LEEK, FRANKS, VANDERKLISH P, ARAI A, LYNCH G: Inhi-bition of proteolysis protects hippocampal neurons from ischemia. Proc. Natl. Acad. ScL USA (1991) 88:7233–7237.
  • RAMI A, KRIEGLSTEIN J: Protective effects of calpain in-hibitors against neuronal damage caused by cytotoxic hypoxia in vitro and ischemia in vivo. Brain Res. (1993) 609:67–70.
  • HONG S-C, GOTO Y, LANZINO G, SALEAU S, KASSEL NF, LEE KS: Neuroprotection with a calpain inhibitor in a model of focal cerebral ischemia. Stroke (1994) 25:663–669.
  • ••Z-Val-Phe-H (MDL 28170) reduced infarct volume in a ratmiddle cerebral occlusion model of ischaemia.
  • BARTUS RT, BAKER KL, HEISER AD et al.: Postischemic administration of AK275, a calpain inhibitor, provides substantial protection against focal ischemic brain damage. J. Cereb. Blood Flow Metab. (1994) 14:537–544.
  • •Z-Leu-Abu-CONHEt (AK275) perfused directly to the corti-cal surface decreased infarct volume in a rat MCAO model.
  • BARTUS RT, HAYVVARD NJ, ELLIOTT PJ et al.: Calpain in- hibitor AK295 protects neurons from focal brain dam-age. Stroke (1994) 25:2265–2270.
  • •Z-Leu-Abu-CONH(CH2)3morpholine (AK295) continuously infused through the internal carotid artery decreased infarct volume in a rat MCAO model.
  • MATZELLE JT, BARTUS RT, HOGAN EL, BANIK NL: New in-hibitors of calpain prevent degradation of cytoskeletal and myelin proteins in spinal cord in vitro. J. Neurosci. Res. (1998) 51:218–222.
  • KRANTZ A: Some thoughts on enzyme inhibition and the quiescent affinity label concept. In: Advances in Me-dicinal Chemistry, Vol.]. Maryanoff BE, Maryanoff CA (Eds.), JAI Press, Greenwich, Conn. (1992):235–261.
  • AOYAGI T, TAKEUCHI T, MATSUZAKI A et. al.: Leupetins, new protease inhibitors from Actinomycetes. J. Antibi-otics (1969) 22:283–286.
  • TSUJINAKA T, KAJIWARA Y, KAMBAYASHI J, SAKON M,HIGUCHI N, TANAKA T: Synthesis of a new cell pene-trating calpain inhibitor (calpeptia Biochem. Biophys. Res. Commun. (1988) 153:1201–1208.
  • MEHDI S, ANGELASTRO MR, WISEMAN JS, BEY P: Inhibi-tion of the proteolysis of rat erythrocyte membrane proteins by a synthetic inhibitor of calpain. Biochem. Biophys. Res. Commun. (1988) 157:1117–1123.
  • IQBAL M, MESSINA PA, FREED B et al.: Subsite require-ments for peptide aldehyde inhibitors of human cal-pain I. Bioorg. Med. Chem. Lett. (1997) 7:539–544.
  • •Potencies of 70 peptide aldehydes were determined.
  • SASAKI T, KISHI M, SAITO M et al.: Inhibitory effect of di-and tripeptidyl aldehydes on calpains and cathepsins. J. Enzyme Inhib. (1990) 3:195–201.
  • CHATTERJEE S, GU Z-Q, DUNN D et al.: El-Amino acid containing high-affinity inhibitors of recombinant hu-man calpain I. J. Med. Chem. (1998) 41:2663–2666.
  • CHATTERJEE S, IQBAL M, KAUER JC et al.: Xanthene de-rived potent nonpeptidic inhibitors of recombinant human calpain I. Bioorg. Med. Chem. Lett. (1996) 6:1619–1622.
  • CHATTERJEE S, IQBAL M, MALLYA SK et al.: Explorationof the importance of the P2-P3 -NHCO-moiety in a po-tent di- or tripeptide inhibitor of calpain I: insights into the development of nonpeptidic inhibitors of cal-pain I. Bioorg. Med. Chem. (1998) 6:509–522.
  • CHATTERJEE S, SENADHI S, BOZYCZKO-COYNE D, SI-MAN R, MALLAMO JP: Nonpeptidic inhibitors of human calpain I. Bioorg. Med. Chem. Lett. (1997) 7:287–290.
  • HARRIS AL, GREGORY JS, MAYCOCK AL et al.: Characteri-zation of a continuous fluorogenic assay for calpain I. Kinetic evaluation of peptide aldehydes, halomethyl ketones and (acyloxy)methyl ketones as inhibitors of the enzyme. Bioorg. Med. Chem. Lett. (1995) 5:393–398.
  • MEYER SL, BOZYCZKO-COYNE D, MALLYA SK et al Bio- logically active monomeric and heterodimeric recom-binant human calpain I produced using the baculovirus expression system. Biochem. J. (1996) 314:511–519.
  • •Human calpain I was expressed in the baculovirus expres-sion system.
  • ANDO R, MORINAKA Y, TOKUYAMA H, ISAKA M, NAKA-MURA E: A new class of proteinase inhibitor. Cyclopropenone-containing inhibitor of papain. J. Am. Chem. Soc. (1993) 115:1175.
  • MEHDI S: Synthetic and naturally occurring protease inhibitors containing an electrophilic carbonyl group. Bioorg. Chem. (1993) 21:249–259.
  • TAO M, BIHOVSKY R, WELLS GJ, MALLAMO JP: Novel peptidyl phosphorus derivatives as inhibitors of hu-man calpain I. J. Med. Chem. (1998). (In Press).
  • TAO M, BIHOVSKY R, KAUER JC: Inhibition of calpain by peptidyl heterocycles. Bioorg. Med. Chem. Lett. (1996) 6:3009–3012.
  • SHAW E: Cysteinyl proteases and their selective inacti-vation. Adv. Enzymol. (1990) V63:271–347.
  • PEET NP, BURKHART JP, ANGELASTRO MR et al: Synthe-sis of peptidyl fluoromethyl ketones and peptidyl a-keto esters as inhibitors of porcine pancreatic elastase, human neutrophil elastase, and rat and hu-man neutrophil cathepsin G. J. Med. Chem. (1990) 33:394–407.
  • ANGELASTRO MR, MEHDI S, BURKHART JP, PEET NP, BEY P: a-Diketone and a-keto ester derivatives of N-protected amino acids and peptides as novel inhibi-tors of cysteine and serine proteinases. J. Med. Chem. (1990) 33:11–13.
  • ••Moderately potent a-ketoester, and 1,2-diketone inhibitorsof calpain were described.
  • OCAIN TD, RICH DH: a-Keto amide inhibitors of amino-peptidases. J. Med. Chem. (1992) 35:451–456.
  • WASSERMAN HH, ENNIS DS, POWER PL, ROSS MJ: Syn-thesis and evaluation of peptidyl vicinal tricarbonyl monohydrates as inhibitors of hydrolytic enzymes. J. Org. Chem. (1993) 58:4785–4787.
  • LI Z, PATIL GS, GOLUBSKI ZE et al.: Peptide a-keto am-ide, and a-keto acid inhibitors of calpains and other cysteine proteases. J. Med. Chem. (1993) 36:3472–3480.
  • ••Potent a-ketoamide and a-ketoacid calpain inhibitors aswell as less potent a-ketoesters were described.
  • LI Z, ORTEGA-VILAIN AC, PATIL GS et al.: Novel peptidyl a-keto amide inhibitors of calpains and other cysteine proteases. J. Med. Chem. (1996) 39:4089–4098.
  • HARBESON SL, ABELLEIRA SM, AKIYAMA A et al.: Stereo-specific synthesis of peptidyl a-keto amides as inhibi-tors of calpain. J. Med. Chem. (1994) 37:2918–2929.
  • HANADA K, TAMAI M, YAMAGISHI M, OHMURA S, SA-WADA J, TANAKA I: Isolation and characterization of E-64, a new thiol protease inhibitor. Agric. Biol. Chem. (1978) 42:523–528.
  • PARKES C, KEMBHAVI AA, BARRETT AJ: Calpain inhibi-tion by peptide epoxides. Biochem. J. (1985) 230:509–516.
  • INUZUKA T, TAMUAR A, SATO S et al.: Suppressive effect of E-64c on ischemic degradation of cerebral proteins following occlusion of the middle cerebral artery in rats. Brain Res. (1990) 526:177–179.
  • SATOYOSHI E: Therapeutic trials on progressive mus-cular dystrophy. Intern. Med. (1992) 31:841–846.
  • FUKUSHIMA K, ARAI M, KOHNO Y, SUWA T, SATOH T: An epoxysuccinic acid derivative floxistatiOinduced he-patic injury in rats and hamsters. Toxicol. Appl. Pharma-col. (1990) 105:1–12.
  • CRAWFORD C, MASON RW, WIKSTROM P, SHAW E: The design of peptidyldiazomethane inhibitors to distin-guish between the cysteine proteinases calpain II, cathepsin Land cathepsin B. Biochem. J. (1988) 253:751–758.
  • SASAKI T, KIKUCHI T, FUKUI I, MURACHI T: Inactivation of calpain I and calpain II by specificity-oriented tripeptidyl chloromethyl ketones. J. Biochem. (1986) 99:173–179.
  • ANGLIKER H, ANAGLI J, SHAW, E.: Inactivation of cal-pain by peptidyl fluoromethyl ketones. J. Med. Chem. (1992) 35:216–220.
  • CHATTERJEE S, ATOR MA, BOZYCZKO-COYNE D et al: Synthesis and biological activity of a series of potent fluoromethyl ketone inactivators of human calpain I. J. Med. Chem. (1997) 40:3820–3828.
  • ESSER RE, WATTS LM, ANGELO RA et al.: The effects of fluoromethyl ketone inhibitors of cathepsin B on adju-vant induced arthritis. J. Rheumatol. (1993) 20:1176–1183.
  • DOLLE RE, SINGH J, WHIPPLE D et al.: Aspartyl a-ffdi-phenylphosphinyfioxylmethyl ketones as novel in-hibitors of interleukin-10 converting enzyme. Utility of the diphenylphosphinic acid leaving group for in-hibition of cysteine proteases. J. Med. Chem. (1995) 38:220–222.
  • PLIURA DH, BONAVENTURA BJ, SMITH RA, COLES PJ, KRANTZ A: Comparative behaviour of calpain and cathepsin B toward peptidyl acyloxymethyl ketones, sulphonium methyl ketones and other potential in-hibitors of cysteine proteinases. Biochem. j (1992) 288:759–762.
  • PALMER JT, RASNICK D, KLAUS JL, BROMME D: Vinyl sul-fones as mechanism-based cysteine protease inhibi-tors. J. Med. Chem. (1995) 38:3193–3196.
  • POSNER A, RASER KJ, HAJIMOHAMMADREZA I, YUEN P, WANG KKW: Aurintricarboxylic acid is an inhibitor of µ- and m-calpain. Biochem. Mol Biol. Int. (1995) 36:291–299.
  • PURI R, MATSUDA R, UMEYAMA H, BRADFORD HN, COL- MAN RW: Modulation of thrombin-induced platelet ag-gregation by inhibition of calpain by a synthetic peptide derived from the thiol-protease inhibitory se-quence on kininogens and S-(3-nitro-2-pyridinesulfenyfi-cysteine. Eur. J. Biochem. (1993) 214:233–241.
  • ALVAREZ ME, HOUCK DR, WHITE CB eta].:Isolation and structure elucidation of two new calpain inhibitors from Streptomyces griseus. J. Antibiotics. (1994) 47:1195–1201.
  • OLNEY JW, LABRUYERE J, WANG G, WOZNIAK DF, PRICE MT, SESMA MA: NMDA antagonist neurotoxicity: mechanism and prevention. Science (1991) 254 :1515–1518.
  • HUNTER AJ, GREEN AR, CROSS AJ: Animal models of acute ischaemic stroke: can they predict clinically suc-cessful neuroprotective drugs? Trends Pharm. Sci. (1995) 16:123128.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.