Vai ai contenuti. | Spostati sulla navigazione | Spostati sulla ricerca | Vai al menu | Contatti | Accessibilità

| Crea un account

Zanetti, Filippo (2010) Intact hearts: a new tool for elucidating the antioxidant role of the prion protein. [Tesi di dottorato]

Full text disponibile come:

[img]
Anteprima
Documento PDF
3065Kb

Abstract (inglese)

The elusive function of the cellular prion protein (PrPC) hampers the understanding of the molecular mechanism at the basis of prion diseases, and the development of suitable therapeutic protocols. Use of cell model systems, and genetically modified animals, have nevertheless suggested a number of potential roles for the protein, ranging from protecting against oxidative stress to cell differentiation. Because we now know that muscle is involved in PrPC pathophysiology, we have considered intact heart paradigms for the in situ study of the cell-protecting function of PrPC.
Isolated muscle organs retain the cell native environment and are also more suitable to experimental designs than whole animals. Accordingly, by taking advantage of mice expressing different PrPC amounts (wild type (WT), knock-out (KO) and overexpressors (OE)), the protection of PrPC against cell oxidative injuries was investigated in isolated hearts subjected to ischemia/reperfusion and perfusion protocols that involve oxidative stress. In line with the putative capability of PrPC to antagonize oxidative injury and cell death mechanisms, our prediction was that hearts from PrPC-KO adult mice manifest an overt phenotype after ischemic challenge, resulting in exacerbation of heart oxidative damage. Conversely, PrPC-OE mice should demonstrate a higher resistance over reactive oxygen species (ROS) production.
We found that PrPC-OE hearts were more protected from the damage induced by post-ischemic reperfusion than WT and PrPC-KO hearts, as indicated by reduced cell death and decreased oxidation of myofibrillar protein and accumulation of ROS. We then reasoned that, if indeed PrPC acts as an antioxidant, absence of PrPC should increase the effect of ischemic preconditioning (IPC), in contrast to the less evident protection in hearts from PrPC-OE mice. Our data on hearts subjected to IPC nicely fitted with this prediction, given that IPC led to a strong decrease of damage in PrPC-KO hearts, an intermediate protection in WT hearts, and no significant effect in PrPC-OE hearts. We also applied protocols of non-ischemic oxidative injury, by subjecting isolated hearts to perfusion with hydrogen peroxide. Such treatment was associated with a significantly larger myocardial cell loss and myofibrillar oxidative damage PrPC-KO hearts, compared to hearts from WT and PrPC-OE mice.
We then investigated the possible modulation by PrPC of proteins involved in the oxidative stress response. We performed enzymatic activity assays on catalase (CAT) and mitochondrial and cytosolic superoxide dismutase (SOD): we found a decrease in CAT activity in PrPC-KO hearts with respect to PrPC-expressing counterparts, whereas no major variation in the activity/expression of SOD was registered among the different PrPC-genotypes. In addition, we found increased levels of both total and mitochondrial p66Shc, a protein involved in oxidative stress-mediated apoptosis, in hearts lacking PrPC. This unprecedented and intriguing finding demands further investigations in the future.
This data thus supports both the value of the in situ muscle paradigm for studying the physiologic function of PrPC, and the role of PrPC against oxidative insults and cell damage.

Abstract (italiano)

L’esatto ruolo che la proteina prionica cellulare (PrPC) svolge nella fisiologia della cellula è ancora incerto, e questo impedisce la comprensione dei meccanismi che stanno alla base delle malattie da prione e lo sviluppo di opportune strategie terapeutiche. Studi condotti su modelli cellulare e animali geneticamente modificati, tuttavia, hanno suggerito che PrPC possa svolgere un ruolo protettivo nei confronti dello stress ossidativo e di segnali di morte cellulare. PrPC è particolarmente abbondante nel sistema nervoso centrale, ma è espressa a livelli elevati anche nei tessuti muscolari. Inoltre, recenti evidenze hanno correlato la proteina alla fisiopatologia muscolare. Per questo motivo, abbiamo orientato la nostra ricerca sull’utilizzo di cuori isolati e perfusi, un paradigma sperimentale innovativo per lo studio in situ delle funzioni protettive della PrPC.
Rispetto alle cellule in coltura, i cuori isolati hanno il vantaggio di mantenere l’ambiente cellulare di origine e sono inoltre modelli più adatti dell’animale intero per le manipolazioni sperimentali. Di conseguenza, servendoci di topi wild-type (WT) e geneticamente modificati, esprimenti differenti quantità di PrPC (knock-out (KO) e sovra-esprimenti (OE) la proteina), abbiamo verificato la putativa funzione antiossidante di PrPC servendoci di cuori isolati sottoposti a protocolli di ischemia/riperfusione (I/R), o di perfusione, che implicano lo stress ossidativo. La nostra previsione, in linea con la putativa capacità di PrPC di contrastare l’insulto ossidativo ed i meccanismi di morte cellulare, era che i cuori espiantati da topi PrPC-KO e da topi PrPC-OE, e sottoposti a protocolli di I/R, manifestassero, rispettivamente, una maggiore e minore sensibilità al danno rispetto alla controparte WT.
Quello che abbiamo rilevato è che i cuori PrPC-OE sono più resistenti al danno indotto dalla riperfusione post-ischemica rispetto a cuori WT e PrPC-KO, come indicato dalla riduzione di morte cellulare, ossidazione di proteine miofibrillari ed accumulo di specie reattive dell’ossigeno (ROS). Abbiamo quindi ipotizzato che, se realmente PrPC agisse come un agente anti-ossidante, l’assenza della proteina avrebbe potuto aumentare la protezione conferita dall’utilizzo di un protocollo di pre-condizionamento ischemico (IPC), il cui meccanismo si basa sulla produzione di piccole quantità di ROS. Questa ipotesi si è dimostrata corretta, dato che il protocollo di IPC svolge un forte ruolo protettivo nei cuori PrPC-KO, uno intermedio nei WT, e nessun effetto nei cuori PrPC-OE. Abbiamo inoltre applicato protocolli basati su un tipo di danno ossidativo non ischemico, perfondendo i cuori isolati con perossido di idrogeno. Tale trattamento produce una maggiore morte cellulare ed una maggiore ossidazione delle proteine miofibrillari nei cuori PrPC-KO, paragonati a quelli WT e PrPC-OE.
Abbiamo infine ipotizzato un possibile ruolo di PrPC nella modulazione dell’attività/espressione di proteine coinvolte nella risposta agli stimoli ossidativi. A tal fine, abbiamo testato l’attività, in cuori non perfusi, di alcuni enzimi scavenger di ROS, tra cui catalasi (CAT) e superossido dismutasi (SOD) mitocondriale e citosolica. Mentre abbiamo osservato una riduzione significativa dell’attività di CAT nei cuori PrPC-KO rispetto a quelli esprimenti PrPC, l’espressione e l’attività delle SOD non sono risultate differenti nei tre genotipi di PrPC. Da sottolineare, infine, che è stato dimostrato un aumento dell’espressione di p66Shc, una proteina coinvolta nella mediazione di segnali pro-apoptotici, nei cuori privi PrPC. Tale osservazione, assolutamente inedita, meriterà ulteriori approfondimenti futuri.
I nostri risultati supportano dunque sia il valore del nuovo modello sperimentale in situ per lo studio della funzione fisiologica di PrPC, sia il coinvolgimento della proteina nelle difese contro lo stress ossidativo ed il danno cellulare.

Statistiche Download - Aggiungi a RefWorks
Tipo di EPrint:Tesi di dottorato
Relatore:Sorgato, Maria Catia
Correlatore:Bertoli, Alessandro
Dottorato (corsi e scuole):Ciclo 22 > Scuole per il 22simo ciclo > BIOCHIMICA E BIOTECNOLOGIE > BIOCHIMICA E BIOFISICA
Data di deposito della tesi:NON SPECIFICATO
Anno di Pubblicazione:29 Gennaio 2010
Parole chiave (italiano / inglese):Prion protein, heart, oxidative stress, ischemia, perfusion
Settori scientifico-disciplinari MIUR:Area 05 - Scienze biologiche > BIO/10 Biochimica
Struttura di riferimento:Centri > Centro Interdipartimentale di servizi A. Vallisneri
Dipartimenti > pre 2012 Dipartimento di Chimica Biologica
Codice ID:2736
Depositato il:20 Set 2010 10:33
Simple Metadata
Full Metadata
EndNote Format

Bibliografia

I riferimenti della bibliografia possono essere cercati con Cerca la citazione di AIRE, copiando il titolo dell'articolo (o del libro) e la rivista (se presente) nei campi appositi di "Cerca la Citazione di AIRE".
Le url contenute in alcuni riferimenti sono raggiungibili cliccando sul link alla fine della citazione (Vai!) e tramite Google (Ricerca con Google). Il risultato dipende dalla formattazione della citazione.

• Aebi H. Catalase in vitro. Methods Enzymol. 1984;105:121-6. Cerca con Google

• Aguzzi A, Baumann F, Bremer J. The prion's elusive reason for being. Annu Rev Neurosci. 2008;31:439-77. Cerca con Google

• Aguzzi A, Calella AM. Prions: protein aggregation and infectious diseases. Physiol Rev. 2009 Oct;89(4):1105-52. Cerca con Google

• Allen DG, Orchard CH. Myocardial contractile function during ischemia and hypoxia. Circ Res. 1987 Feb;60(2):153-68. Cerca con Google

• Allen KL, Busza AL, Proctor E, Williams SR, Van Bruggen N, Gadian DG, Crockard HA. Restoration of energy metabolism and resolution of oedema following profound ischaemia. Acta Neurochir Suppl (Wien). 1990;51:171-3. Cerca con Google

• Alper T, Does the agent of scrapie replicate without nucleic acid? Nature. 1967 May 20;214(5090):764-6. Cerca con Google

• Andoh T, Lee SY, Chiueh CC. Preconditioning regulation of bcl-2 and p66shc by human NOS1 enhances tolerance to oxidative stress. Faseb J. 2000;14:2144–2146. Cerca con Google

• Andréoletti O, Simon S, Lacroux C, Morel N, Tabouret G, Chabert A, Lugan S, Corbière F, Ferré P, Foucras G, Laude H, Eychenne F, Grassi J, Schelcher F. PrPSc accumulation in myocytes from sheep incubating natural scrapie. Nat Med. 2004 Jun;10(6):591-3. Cerca con Google

• Angers RC, Browning SR, Seward TS, Sigurdson CJ, Miller MW, Hoover EA, Telling GC. Prions in skeletal muscles of deer with chronic wasting disease. Science. 2006 Feb 24;311(5764):1117. Cerca con Google

• Ashwath ML, Dearmond SJ, Culclasure T, Prion-associated dilated cardiomyopathy. Arch Intern Med. 2005 Feb 14;165(3):338-40. Cerca con Google

• Barbato R, Menabo R, Dainese P, Carafoli E, Schiaffino S, Di Lisa F. Binding of cytosolic proteins to myofibrils in ischemic rat hearts, Circ. Res. 78 (1996) 821–828. Cerca con Google

• Basler K, Oesch B, Scott M, Westaway D, Walchli M, Groth DF, McKinley MP, Prusiner SB, Weissmann C. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell. 1986 Aug 1;46(3):417-28. Cerca con Google

• Beckman JS, Koppenol WH. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am J Physiol. 1996 Nov;271(5 Pt 1):C1424-37. Cerca con Google

• Bellinger-Kawahara C, Diener TO, McKinley MP, Groth DF, Smith DR, Prusiner SB. Purified scrapie prions resist inactivation by procedures that hydrolyze, modify, or shear nucleic acids. Virology. 1987 Sep;160(1):271-4. Cerca con Google

• Bergmeyer HU, Bernt E. in: H.U. Bergmeyer (Ed.), Lactate Dehydrogenase. Weinheim, 1974, pp. 607–612 Cerca con Google

• Bianchin MM, Walz R, Brentani RR, Martins VR. Dilated cardiomyopathy and Creutzfeldt-Jakob disease: evidence for a role of cellular prion protein in the heart? Arch Intern Med. 2005 Jul 25;165(14):1663-4. Cerca con Google

• Bosque PJ, Ryou C, Telling G, Peretz D, Legname G, DeArmond SJ, Prusiner SB. Prions in skeletal muscle. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3812-7. Cerca con Google

• Bounhar Y, Zhang Y, Goodyer CG, LeBlanc A. Prion protein protects human neurons against Bax-mediated apoptosis. J Biol Chem. 2001 Oct 19;276(42):39145-9. Cerca con Google

• Braasch W, Gudbjarnason S, Puri PS, Ravens KG, Bing RJ. Early changes in energy metabolism in the myocardium following acute coronary artery occlusion in anesthetized dogs. Circ Res. 1968 Sep;23(3):429-38. Cerca con Google

• Brandner S, Raeber A, Sailer A, Blättler T, Fischer M, Weissmann C, Aguzzi A. Normal host prion protein (PrPC) is required for scrapie spread within the central nervous system. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):13148-51. Cerca con Google

• Brini M, Miuzzo M, Pierobon N, Negro A, Sorgato MC. The prion protein and its paralogue Doppel affect calcium signaling in Chinese hamster ovary cells. Mol Biol Cell. 2005 Jun;16(6):2799-808. Cerca con Google

• Brown DR, Besinger A. Prion protein expression and superoxide dismutase activity. Biochem J. 1998 Sep 1;334 ( Pt 2):423-9. Cerca con Google

• Brown DR, Qin K, Herms JW, Madlung A, Manson J, Strome R, Fraser PE, Kruck T, von Bohlen A, Schulz-Schaeffer W, Giese A, Westaway D, Kretzschmar H. The cellular prion protein binds copper in vivo. Nature. 1997a; Dec 18-25;390(6661):684-7. Cerca con Google

• Brown DR, Sassoon J. Copper-dependent functions for the prion protein. Mol Biotechnol. 2002 Oct;22(2):165-78. Cerca con Google

• Brown DR, Schmidt B, Groschup MH, Kretzschmar HA. Prion protein expression in muscle cells and toxicity of a prion protein fragment. Eur J Cell Biol. 1998 Jan;75(1):29-37. Cerca con Google

• Brown DR, Schmidt B, Kretzschmar HA, Effects of oxidative stress on prion protein expression in Pc12 cells. Int. J. Dev. Neurosci. 1997b, 146:104-12. Cerca con Google

• Brown DR, Schulz-Schaeffer WJ, Schmidt B, Kretzschmar HA, Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 1997c, 146: 104-12 Cerca con Google

• Brown DR, Wong BS, Hafiz F, Clive C, Haswell SJ, Jones IM. Normal prion protein has an activity like that of superoxide dismutase. Biochem J. 1999 Nov 15;344 Pt 1:1-5. Cerca con Google

• Büeler H, Fischer M, Lang Y, Bluethmann H, Lipp HP, DeArmond SJ, Prusiner SB, Aguet M, Weissmann C. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature. 1992; 356, 577-82. Cerca con Google

• Canton M, Neverova I, Menabò R, Van Eyk J, Di Lisa F. Evidence of myofibrillar protein oxidation induced by postischemic reperfusion in isolated rat hearts. Am J Physiol Heart Circ Physiol. 2004 Mar;286(3):H870-7. Cerca con Google

• Canton M, Skyschally A, Menabò R, Boengler K, Gres P, Schulz R, Haude M, Erbel R, Di Lisa F, Heusch G. Oxidative modification of tropomyosin and myocardial dysfunction following coronary microembolization. Eur Heart J. 2006 Apr;27(7):875-81. Cerca con Google

• Carpi A, Menabò R, Kaludercic N, Pelicci P, Di Lisa F, Giorgio M. The cardioprotective effects elicited by p66(Shc) ablation demonstrate the crucial role of mitochondrial ROS formation in ischemia/reperfusion injury. Biochim Biophys Acta. 2009 Jul;1787(7):774-80. Cerca con Google

• Caughey B, Brown K, Raymond GJ, Katzenstein GE, Thresher W. Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red J Virol. 1994 Apr;68(4):2135-41. Erratum in: J Virol 1994 Jun;68(6):4107. Cerca con Google

• Caughey B, Race R, Chesebro B. Comparative sequence analysis, in vitro expression and biosynthesis of mouse PrP. Prog Clin Biol Res. 1989;317:619-36. Cerca con Google

• Caughey B, Raymond GJ. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J Biol Chem. 1991 Sep 25;266(27):18217-23. Cerca con Google

• Cereghetti GM, Schweiger A, Glockshuber R, Van Doorslaer S. Electron paramagnetic resonance evidence for binding of Cu(2+) to the C-terminal domain of the murine prion protein. Biophys J. 2001 Jul;81(1):516-25. Cerca con Google

• Cesselli D, Jakoniuk I, Barlucchi L, Beltrami AP, Hintze TH, Nadal-Ginard B, Kajstura J, Leri A, Anversa P. Oxidative stress-mediated cardiac cell death is a major determinant of ventricular dysfunction and failure in dog dilated cardiomyopathy. Circ Res. 2001 Aug 3;89(3):279-86. Cerca con Google

• Chen S, Mangé A, Dong L, Lehmann S, Schachner M. Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival. Mol Cell Neurosci. 2003 Feb;22(2):227-33. Cerca con Google

• Chiesa R, Pestronk A, Schmidt RE, Tourtellotte WG, Ghetti B, Piccardo P, Harris DA. Primary myopathy and accumulation of PrPSc-like like molecules in peripheral tissues of transgenic mice ex pressing a prion protein insertional mutation. Neurobiol Dis. 2001 Apr;8(2):279-88. Cerca con Google

• Chrétien F, Dorandeu A, Adle-Biassette H, Ereau T, Wingertsmann L, Brion F, Gray F. A process of programmed cell death as a mechanisms of neuronal death in prion diseases. Clin Exp Pathol. 1999;47(3-4):181-91. Cerca con Google

• Cohen FE, Pan KM, Huang Z, Baldwin M, Fletterick RJ, Prusiner SB. Structural clues to prion replication. Science. 1994 Apr 22;264(5158):530-1. Cerca con Google

• Cohen FE. Protein misfolding and prion diseases. J Mol Biol. 1999 Oct 22;293(2):313-20. Cerca con Google

• Coitinho AS, Freitas AR, Lopes MH, Hajj GN, Roesler R, Walz R, Rossato JI, Cammarota M, Izquierdo I, Martins VR, Brentani RR. The interaction between prion protein and laminin modulates memory consolidation. Eur J Neurosci. 2006 Dec;24(11):3255-64. Cerca con Google

• Collinge J, Owen F, Poulter M, Leach M, Crow TJ, Rossor MN, Hardy J, Mullan MJ, Janota I, Lantos PL. Prion dementia without characteristic pathology. Lancet. 1990 Jul 7;336(8706):7-9. Cerca con Google

• Collins SR, Douglass A, Vale RD, Weissman JS. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2004 Oct;2(10):e321. Cerca con Google

• Cosentino F, Francia P, Camici GG, Pelicci PG, Lüscher TF, Volpe M. Final common molecular pathways of aging and cardiovascular disease: role of the p66Shc protein. Arterioscler Thromb Vasc Biol. 2008 Apr;28(4):622-8. Cerca con Google

• del Monte F, Lebeche D, Guerrero JL, Tsuji T, Doye AA, Gwathmey JK, Hajjar RJ. Abrogation of ventricular arrhythmias in a model of ischemia and reperfusion by targeting myocardial calcium cycling. Proc Natl Acad Sci U S A. 2004 Apr 13;101(15):5622-7. Cerca con Google

• Demaison L, Moreau D, Martine L, Chaudron I, Grynberg A. Myocardial ischemia and in vitro mitochondrial metabolic efficiency. Mol Cell Biochem. 1999 Apr;194(1-2):291-300. Cerca con Google

• Di Lisa F, Menabò R, Canton M, Barile M, Bernardi P. Opening of the mitochondrial permeability transition pore causes depletion of mitochondrial and cytosolic NAD+ and is a causative event in the death of myocytes in postischemic reperfusion of the heart. J Biol Chem. 2001 Jan 26;276(4):2571-5. Cerca con Google

• Diarra-Mehrpour M, Arrabal S, Jalil A, Pinson X, Gaudin C, Piétu G, Pitaval A, Ripoche H, Eloit M, Dormont D, Chouaib S. Prion protein prevents human breast carcinoma cell line from tumor necrosis factor alpha-induced cell death. Cancer Res. 2004 Jan 15;64(2):719-27. Cerca con Google

• Dorandeu A, Wingertsmann L, Chrétien F, Delisle MB, Vital C, Parchi P, Montagna P, Lugaresi E, Ironside JW, Budka H, Gambetti P, Gray F. Neuronal apoptosis in fatal familial insomnia. Brain Pathol. 1998 Jul;8(3):531-7. Cerca con Google

• Downey JM, Cohen MV, Ytrehus K, Liu Y. Cellular mechanisms in ischemic preconditioning: the role of adenosine and protein kinase C. Ann N Y Acad Sci. 1994 Jun 17;723:82-98. Cerca con Google

• Dröge W. Free radicals in the physiological control of cell function. Physiol Rev. 2002 Jan;82(1):47-95. Cerca con Google

• Ettaiche M, Pichot R, Vincent JP, Chabry J. In vivo cytotoxicity of the prion protein fragment 106-126. J Biol Chem. 2000 Nov 24;275(47):36487-90. Cerca con Google

• Evans MD, Dizdaroglu M, Cooke MS. Oxidative DNA damage and disease: induction, repair and significance. Mutat Res. 2004 Sep;567(1):1-61. Cerca con Google

• Forloni G, Angeretti N, Chiesa R, Monzani E, Salmona M, Bugiani O, Tagliavini F. Neurotoxicity of a prion protein fragment. Nature. 1993 Apr 8;362(6420):543-6. Cerca con Google

• Fornai F, Ferrucci M, Gesi M, Bandettini di Poggio A, Giorgi FS, Biagioni F, Paparelli A. A hypothesis on prion disorders: are infectious, inherited, and sporadic causes so distinct? Brain Res Bull. 2006 Mar 31;69(2):95-100. Cerca con Google

• Fujio Y, Nguyen T, Wencker D, Kitsis RN, Walsh K. Akt promotes survival of cardiomyocytes in vitro and protects against ischemia-reperfusion injury in mouse heart. Circulation. 2000 Feb 15;101(6):660-7. Cerca con Google

• Garcia-Dorado D, Agulló L, Sartorio CL, Ruiz-Meana M. Myocardial protection against reperfusion injury: the cGMP pathway. Thromb Haemost. 2009 Apr;101(4):635-42. Cerca con Google

• Gauczynski S, Peyrin JM, Haïk S, Leucht C, Hundt C, Rieger R, Krasemann S, Deslys JP, Dormont D, Lasmézas CI, Weiss S. The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein. EMBO J. 2001 Nov 1;20(21):5863-75. Cerca con Google

• Giorgio M, Migliaccio E, Orsini F, Paolucci D, Moroni M, Contursi C, Pelliccia G, Luzi L, Minucci S, Marcaccio M, Pinton P, Rizzuto R, Bernardi P, Paolucci F, Pelicci PG. Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell. 2005 Jul 29;122(2):221-33. Cerca con Google

• Glatzel M, Abela E, Maissen M, Aguzzi A. Extraneural pathologic prion protein in sporadic Creutzfeldt-Jakob disease. N Engl J Med. 2003 Nov 6;349(19):1812-20. Cerca con Google

• Graner E, Mercadante AF, Zanata SM, Forlenza OV, Cabral AL, Veiga SS, Juliano MA, Roesler R, Walz R, Minetti A, Izquierdo I, Martins VR, Brentani RR Cellular prion protein binds laminin and mediates neuritogenesis. Brain Res Mol Brain Res. 2000b Mar 10;76(1):85-92. Cerca con Google

• Graner E, Mercadante AF, Zanata SM, Forlenza OV, Cabral AL, Veiga SS, Juliano MA, Roesler R, Walz R, Minetti A, Izquierdo I, Martins VR, Brentani RR. Cellular prion protein binds laminin and mediates neuritogenesis. Brain Res Mol Brain Res. 2000a Mar 10;76(1):85-92. Cerca con Google

• Graner E, Mercadante AF, Zanata SM, Martins VR, Jay DG, Brentani RR. Laminin-induced PC-12 cell differentiation is inhibited following laser inactivation of cellular prion protein. FEBS Lett. 2000b Oct 6;482(3):257-60. Cerca con Google

• Griffith, J.S. Self-replication and scrapie. Nature. 1967 215(105):1043-4. Cerca con Google

• Hajj GN, Lopes MH, Mercadante AF, Veiga SS, da Silveira RB, Santos TG, Ribeiro KC, Juliano MA, Jacchieri SG, Zanata SM, Martins VR. Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins. J Cell Sci. 2007 Jun 1;120(Pt 11):1915-26. Cerca con Google

• Hampton MB, Orrenius S. Redox regulation of apoptotic cell death. Biofactors. 1998;8(1-2):1-5. Cerca con Google

• Hansen SM, Berezin V, Bock E. Signaling mechanisms of neurite outgrowth induced by the cell adhesion molecules NCAM and N-cadherin. Cell Mol Life Sci. 2008 Nov;65(23):3809-21. Cerca con Google

• Hausenloy DJ, Yellon DM. Survival kinases in ischemic preconditioning and postconditioning. Cardiovasc Res. 2006 May 1;70(2):240-53. Cerca con Google

• Hearse DJ. Free radicals and the heart. Bratisl Lek Listy. 1991 Mar-Apr;92(3-4):115-8. Cerca con Google

• Hearse DJ. Ischemia at the crossroads? Cardiovasc Drugs Ther. 1988 May;2(1):9-15. Cerca con Google

• Hearse DJ. Myocardial protection during ischemia and reperfusion. Mol Cell Biochem. 1998 Sep;186(1-2):177-84. Cerca con Google

• Hill AF, Joiner S, Linehan J, Desbruslais M, Lantos PL, Collinge J. Species-barrier-independent prion replication in apparently resistant species. Proc Natl Acad Sci U S A. 2000 Aug 29;97(18):10248-53. Cerca con Google

• Huang S, Liang J, Zheng M, Li X, Wang M, Wang P, Vanegas D, Wu D, Chakraborty B, Hays AP, Chen K, Chen SG, Booth S, Cohen M, Gambetti P, Kong Q. Inducible overexpression of wild-type prion protein in the muscles leads to a primary myopathy in transgenic mice. Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6800-5. Cerca con Google

• Hundt C, Peyrin JM, Haïk S, Gauczynski S, Leucht C, Rieger R, Riley ML, Deslys JP, Dormont D, Lasmézas CI, Weiss S. Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor. EMBO J. 2001 Nov 1;20(21):5876-86. Cerca con Google

• Hutter G, Heppner FL, Aguzzi A. No superoxide dismutase activity of cellular prion protein in vivo. Biol Chem. 2003 Sep;384(9):1279-85. Cerca con Google

• Ishikawa T, Akerboom TPM, Sies H. Target Organ Toxicity. CRC Press Inc., Boca Raton FL, 1986; 129–143. Cerca con Google

• Jennings RB. Treatment of acute myocardial ischemia. West J Med. 1987 Jul;147(1):62-4. Cerca con Google

• Jones DP, Thor H, Andersson B, Orrenius S. Detoxification reactions in isolated hepatocytes. Role of glutathione peroxidase, catalase, and formaldehyde dehydrogenase in reactions relating to N-demethylation by the cytochrome P-450 system. J Biol Chem. 1978 Sep 10;253(17):6031-7. Cerca con Google

• Jones S, Batchelor M, Bhelt D, Clarke AR, Collinge J, Jackson GS. Recombinant prion protein does not possess SOD-1 activity. Biochem J. 2005 Dec 1;392(Pt 2):309-12. Cerca con Google

• Kabouridis PS. Lipid rafts in T cell receptor signaling. Mol Membr Biol. 2006 Jan-Feb;23(1):49-57. Cerca con Google

• Kanaani J, Prusiner SB, Diacovo J, Baekkeskov S, Legname G. Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro. J Neurochem. 2005 Dec;95(5):1373-86. Cerca con Google

• Kang YJ, Chen Y, Epstein PN. Suppression of doxorubicin cardiotoxicity by overexpression of catalase in the heart of transgenic mice. J Biol Chem. 1996 May 24;271(21):12610-6. Cerca con Google

• Kim BH, Lee HG, Choi JK, Kim JI, Choi EK, Carp RI, Kim YS. The cellular prion protein (PrPC) prevents apoptotic neuronal cell death and mitochondrial dysfunction induced by serum deprivation. Brain Res Mol Brain Res. 2004 Apr 29;124(1):40-50. Cerca con Google

• Klamt F, Dal-Pizzol F, Conte da Frota ML JR, Walz R, Andrades ME, da Silva EG, Brentani RR, Izquierdo I, Fonseca Moreira JC. Imbalance of antioxidant defense in mice lacking cellular prion protein. Free Radic Biol Med. 2001 May 15;30(10):1137-44. Cerca con Google

• Knight RS, Will RG. Prion diseases. J Neurol Neurosurg Psychiatry. 2004 Mar;75 Suppl 1:i36-42. Cerca con Google

• Kovacs GC, Linleck-Pozza E, Chimelli L, Araujo AQ, Gabbai AA, Strobel T, Glatzel M, Aguzzi A, Budke H, Creutzfeld-Jacob and inclusion body myositis: abundant disease-associated prion protein in muscle. Ann Neurol. 2004 Jan;55(1):121-5. Cerca con Google

• Kramer ML, Kratzin HD, Schmidt B, Römer A, Windl O, Liemann S, Hornemann S, Kretzschmar H. Prion protein binds copper within the physiological concentration range. J Biol Chem. 2001 May 18;276(20):16711-9. Cerca con Google

• Langendorff, O. Untersuchungen am uber lebenden Sangetier Herzen. Pflüegers Archiv. 1985; 61 : 291-322. Cerca con Google

• Lasmézas CI, Deslys JP, Robain O, Jaegly A, Beringue V, Peyrin JM, Fournier JG, Hauw JJ, Rossier J, Dormont D. Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein.Science. 1997 Jan 17;275(5298):402-5. Cerca con Google

• Lee JA, Allen DG. Mechanism of acute ischemic contractile failure of heart. Role of intracellular calcium. J Clin Invest. 1991 Aug;88(2):361-7. Cerca con Google

• Lefer AM, Weyrich AS, Buerke M. Role of selectins, a new family of adhesion molecules, in ischaemia-reperfusion injury. Cardiovasc Res. 1994 Mar;28(3):289-94. Cerca con Google

• Lemasters JJ, Thurman RG. The many facets of reperfusion injury. Gastroenterology. 1995 Apr;108(4):1317-20. Cerca con Google

• Levraut J, Iwase H, Shao ZH, Vanden Hoek TL, Schumacker PT. Cell death during ischemia: relationship to mitochondrial depolarization and ROS generation. Am J Physiol Heart Circ Physiol. 2003 Feb;284(2):H549-58. Cerca con Google

• Li Y, Mei GY, Jiang HY, Wang GR, Tian C, Chen C, Wang X, Wang KX, Han J, Dong XP. The construction and identification of the PRNP vectors with ubiquitin or the lysosome-targeting signal. Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi. 2008 Dec;22(6):419-21. Cerca con Google

• Linden R, Martins VR, Prado MA, Cammarota M, Izquierdo I, Brentani RR, Physiology of the prion protein. Physiol Rev. 2008 Apr;88(2):673-728. Cerca con Google

• Liu H, Cala PM, Anderson SE. Ischemic preconditioning: effects on pH, Na and Ca in newborn rabbit hearts during Ischemia/Reperfusion. J Mol Cell Cardiol. 1998 Mar;30(3):685-97. Cerca con Google

• Lopes MH, Hajj GN, Muras AG, Mancini GL, Castro RM, Ribeiro KC, Brentani RR, Linden R, Martins VR. Interaction of cellular prion and stress-inducible protein 1 promotes neuritogenesis and neuroprotection by distinct signaling pathways. J Neurosci. 2005 Dec 7;25(49):11330-9. Cerca con Google

• Málaga-Trillo E, Sempou E. PrPs: Proteins with a purpose: Lessons from the zebrafish. Prion. 2009 Jul;3(3):129-33. Cerca con Google

• Mallucci G, Collinge J. Update on Creutzfeldt-Jakob disease. Curr Opin Neurol. 2004 Dec;17(6):641-7. Cerca con Google

• Mallucci GR, Ratte S, Asante EA, Linehan J, Gowland I, Jefferys JG, Collinge J. Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J. 2002 Feb 1;21(3):202-10 Cerca con Google

• Mangé A, Béranger F, Peoc'h K, Onodera T, Frobert Y, Lehmann S. Alpha- and beta- cleavages of the amino-terminus of the cellular prion protein. Biol Cell. 2004 Mar;96(2):125-32. Cerca con Google

• Manson JC, Clarke AR, Hooper ML, Aitchison L, McConnell I, Hope J. 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol. 1994 Apr-Jun;8(2-3):121-7. Cerca con Google

• Marber M. Viewpoint: stunning and longterm perfusion-contraction matching are clinically indistinguishable components of clinical hibernation and separation, even if practical, is unlikely to matter. Basic Res Cardiol. 1997;92 Suppl 2:26-9. Cerca con Google

• Marciano PG, Brettschneider J, Manduchi E, Davis JE, Eastman S, Raghupathi R, Saatman KE, Speed TP, Stoeckert CJ Jr, Eberwine JH, McIntosh TK. Neuron-specific mRNA complexity responses during hippocampal apoptosis after traumatic brain injury. J Neurosci. 2004 Mar 24;24(12):2866-76. Cerca con Google

• Maroko PR, Carpenter CB, Chiariello M, Fishbein MC, Radvany P, Knostman JD, Hale SL. Reduction by cobra venom factor of myocardial necrosis after coronary artery occlusion. J Clin Invest. 1978 Mar;61(3):661-70. Cerca con Google

• Massimino ML, Ballarin C, Bertoli A, Casonato S, Genovesi S, Negro A, Sorgato MC. Human Doppel and prion protein share common membrane microdomains and internalization pathways. Int J Biochem Cell Biol. 2004 Oct;36(10):2016-31. Cerca con Google

• Massimino ML, Ferrari J, Sorgato MC, Bertoli A. Heterogeneous PrPC metabolism in skeletal muscle cells. FEBS Lett. 2006 Feb 6;580(3):878-84. Cerca con Google

• McCord JM, Fridovich I. The utility of superoxide dismutase in studying free radical reactions. I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen. J Biol Chem. 1969 Nov 25;244(22):6056-63. Cerca con Google

• McKerracher L, Chamoux M, Arregui CO. Role of laminin and integrin interactions in growth cone guidance. Mol Neurobiol. 1996 Apr;12(2):95-116. Cerca con Google

• McLennan NF, Brennan PM, McNeill A, Davies I, Fotheringham A, Rennison KA, Ritchie D, Brannan F, Head MW, Ironside JW, Williams A, Bell JE. Prion protein accumulation and neuroprotection in hypoxic brain damage. Am J Pathol. 2004 Jul;165(1):227-35. Cerca con Google

• McMahon HE, Mangé A, Nishida N, Créminon C, Casanova D, Lehmann S. Cleavage of the amino terminus of the prion protein by reactive oxygen species. J Biol Chem. 2001 Jan 19;276(3):2286-91. Cerca con Google

• Medori R, Montagna P, Tritschler HJ, LeBlanc A, Cortelli P, Tinuper P, Lugaresi E, Gambetti P. Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178. Neurology. 1992 Mar;42(3 Pt 1):669-70. Cerca con Google

• Miao W, Luo Z, Kitsis RN, Walsh K. Intracoronary, adenovirus-mediated Akt gene transfer in heart limits infarct size following ischemia-reperfusion injury in vivo. J Mol Cell Cardiol. 2000 Dec;32(12):2397-402. Cerca con Google

• Miele G, Alejo Blanco AR, Baybutt H, Horvat S, Manson J, Clinton M. Embryonic activation and developmental expression of the murine prion protein gene. Gene Expr. 2003;11(1):1-12. Cerca con Google

• Migliaccio E, Giorgio M, Mele S, Pelicci G, Reboldi P, Pandolfi PP, Lanfrancone L, Pelicci PG. The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature. 1999;402:309 –313. Cerca con Google

• Migliaccio E, Mele S, Salcini AE, Pelicci G, Lai KM, Superti-Furga G, Pawson T, Di Fiore PP, Lanfrancone L, Pelicci PG. Opposite effects of the p52shc/p46shc and p66Shc splicing isoforms on the EGF receptor-MAP kinase-fos signalling pathway. EMBO J. 1997 Feb 17;16(4):706-16. Cerca con Google

• Milhavet O, Lehmann S. Oxidative stress and the prion protein in transmissible spongiform encephalopathies. Brain Res Brain Res Rev. 2002 Feb;38(3):328-39. Cerca con Google

• Mitteregger G, Vosko M, Krebs B, Xiang W, Kohlmannsperger V, Nölting S, Hamann GF, Kretzschmar HA. The role of the octarepeat region in neuroprotective function of the cellular prion protein.Brain Pathol. 2007 Apr;17(2):174-83. Cerca con Google

• Monnet C, Gavard J, Mège RM, Sobel A. Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells. FEBS Lett. 2004 Oct 8;576(1-2):114-8. Cerca con Google

• Moore RC, Lee IY, Silverman GL, Harrison PM, Strome R, Heinrich C, Karunaratne A, Pasternak SH, Chishti MA, Liang Y, Mastrangelo P, Wang K, Smit AF, Katamine S, Carlson GA, Cohen FE, Prusiner SB, Melton DW, Tremblay P, Hood LE, Westaway D. Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J Mol Biol. 1999 Oct 1;292(4):797-817. Cerca con Google

• Moore RC, Mastrangelo P, Bouzamondo E, Heinrich C, Legname G, Prusiner SB, Hood L, Westaway D, DeArmond SJ, Tremblay P. Doppel-induced cerebellar degeneration in transgenic mice. Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15288-93. Cerca con Google

• Mouillet-Richard, S., Ermonval, M., Chebassier, C., Laplanche, J.L., Lehmann, S., Launay, J.M., Kellermann, O. Signal transduction through prion protein. Science, 2000 289, 1925-1928. Cerca con Google

• Murry CE, Jennings RB, Reimer KA. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation. 1986 Nov;74(5):1124-36. Cerca con Google

• Napoli C, Martin-Padura I, de Nigris F, Giorgio M, Mansueto G, Somma P, Condorelli M, Sica G, De Rosa G, Pelicci P. Deletion of the p66Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet. Proc Natl Acad Sci U S A. 2003;100:2112–2116. Cerca con Google

• Nazor KE, Seward T, Telling GC. Motor behaviour and neuropathological deficits in mice deficient form normal prion protein expression. Biochim Biophys Acta. 2007 Jun;1772(6):645-53. Cerca con Google

• Nico PB, Lobão-Soares B, Landemberger MC, Marques W Jr, Tasca CI, de Mello CF, Walz R, Carlotti CG Jr, Brentani RR, Sakamoto AC, Bianchin MM. Impaired exercise capacity, but unaltered mitochondrial respiration in skeletal or cardiac muscle of mice lacking cellular prion protein. Neurosci Lett. 2005 Nov 4;388(1):21-6. Cerca con Google

• Obreztchikova M, Elouardighi H, Ho M, Wilson BA, Gertsberg Z, Steinberg SF. Distinct signaling functions for Shc isoforms in the heart. J Biol Chem. 2006 Jul 21;281(29):20197-204. Cerca con Google

• Okado-Matsumoto A, Fridovich I. Assay of superoxide dismutase: cautions relevant to the use of cytochrome c, a sulfonated tetrazolium, and cyanide. Anal Biochem. 2001 Nov 15;298(2):337-42. Cerca con Google

• Oudot A, Martin C, Busseuil D, Vergely C, Demaison L, Rochette L. NADPH oxidases are in part responsible for increased cardiovascular superoxide production during aging. Free Radic Biol Med. 2006 Jun 15;40(12):2214-22. Cerca con Google

• Pain T, Yang XM, Critz SD, Yue Y, Nakano A, Liu GS, Heusch G, Cohen MV, Downey JM. Opening of mitochondrial K(ATP) channels triggers the preconditioned state by generating free radicals. Circ Res. 2000 Sep 15;87(6):460-6. Cerca con Google

• Pan KM, Baldwin M, Nguyen, Gasset M, Serban A, Groth D, Mehlhorn I, Huang Z, Fletterick RJ, Cohen FE, Conversion of alpha-helices into beta sheet features in the formation of scrapie prion protein. Proc. Natl. Acad. Sci. USA 1993, 90: 10962-6. Cerca con Google

• Pan T, Wong BS, Liu T, Li R, Petersen RB, Sy MS. Cell-surface prion protein interacts with glycosaminoglycans. Biochem J. 2002 Nov 15;368(Pt 1):81-90. Cerca con Google

• Parkin ET, Watt NT, Turner AJ, Hooper NM. .Dual mechanisms for shedding of the cellular prion protein. Biol Chem. 2004 Mar 19;279(12):11170-8. Cerca con Google

• Paterson AW, Curtis JC, Macleod NK. Complex I specific increase in superoxide formation and respiration rate by PrP-null mouse brain mitochondria. J Neurochem. 2008 Apr;105(1):177-91. Cerca con Google

• Pauly PC, Harris DA Copper stimulates endocytosis of the prion protein. J Biol Chem. 1998 Dec 11;273(50):33107-10 Cerca con Google

• Peden AH, Ritchie DL, Head MW, Ironside JW. Detection and localization of PrPSc in the skeletal muscle of patients with variant, iatrogenic, and sporadic forms of Creutzfeldt-Jakob disease. Am J Pathol. 2006 Mar;168(3):927-35. Cerca con Google

• Peters PJ, Mironov A Jr, Peretz D, van Donselaar E, Leclerc E, Erpel S, DeArmond SJ, Burton DR, Williamson RA, Vey M, Prusiner SB. Trafficking of prion proteins through a caveolae-mediated endosomal pathway. J Cell Biol. 2003 Aug 18;162(4):703-17. Cerca con Google

• Peterson DB, Holian J, Garrison WM. Radiation chemistry of the alpha-amino acids. Gamma radiolysis of solid cysteine. J Phys Chem. 1969 May;73(5):1568-72. Cerca con Google

• Prince RC, Gunson DE. Prions are copper-binding proteins. Trends Biochem Sci. 1998 Jun;23(6):197-8. Cerca con Google

• Prusiner SB. Prions. Proc. Natl. Acad. Sci. 1998, 95, 13363-13383. Cerca con Google

• Prusiner SB. Prions: novel infectious pathogens. Adv Virus Res. 1984;29:1-56. Cerca con Google

• Race R, Chesebro B. Scrapie infectivity found in resistant species. Nature. 1998 Apr 23;392(6678):770. Cerca con Google

• Radovanovic I, Braun N, Giger OT, Mertz K, Miele G, Prinz M, Navarro B, Aguzzi A. Truncated prion protein and Doppel are myelinotoxic in the absence of oligodendrocytic PrPC. J Neurosci. 2005 May 11;25(19):4879-88. Cerca con Google

• Reimer KA, Jennings RB. The “wavefront phenomenon” of myocardial ischemic cell death. II. Trensmural progressin of necrosis within the framework of ischemic deb size (myocardium at risk) and collateral flow. Lab Invest. 1979 Jun;40(6):633-44. Cerca con Google

• Rieger R, Edenhofer F, Lasmezas CI, Weiss S. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat Med. 1997 Dec;3(12):1383-8. Cerca con Google

• Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K. NMR structure of the mouse prion protein domain PrP(121-321). Nature. 1996 Jul 11;382(6587):180-2. Cerca con Google

• Rodgers MA, Sokol HA, Garrison WM. The radiation-induced “hydrolysis” of the peptide boned. J Am Chem Soc. 1968 Jan 31;90(3):795-6. Cerca con Google

• Rossi D, Cozzio A, Flechsig E, Klein MA, Rülicke T, Aguzzi A, Weissmann C. Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. EMBO J. 2001 Feb 15;20(4):694-702. Cerca con Google

• Safar J, Roller PP, Gajduesek DC, Gibbs CJ Jr., Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity. Protein Sci. 1993, 2: 2206-16. Cerca con Google

• Samaia HB, Brentani RR. Can loss-of-function prion-related diseases exist? Mol Psychiatry. 1998 May;3(3):196-7. Cerca con Google

• Santuccione A, Sytnyk V, Leshchyns’ka I, Schachner M. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59Fyn and to enhance neurite outgrowth. J Cell Biol. 2005 Apr 25;169(2):341-54. Cerca con Google

• Sarkozi E, Askanas V, Engel WK. Abnormal accumulation of prion protein mRNA in muscle fibres of patients with sporadic inclusion-body myositis and hereditary inclusion-body myopathy. Am J Pathol. 1994 Dec;145(6):1280-4. Cerca con Google

• Schluter KD, Schwartz P, Siegmund B, Piper HM. Prevention of the oxygen paradox in hypoxic-reoxygenated hearts. Am J Physiol. 1991 Aug;261(2 Pt 2):H416-23. Cerca con Google

• Schmitt-Ulms G, Legname G, Baldwin MA, Ball HL, Bradon N, Bosque PJ, Crossin KL, Edelman GM, DeArmond SJ, Cohen FE, Prusiner SB. Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein. J Mol Biol. 2001 Dec 14;314(5):1209-25. Cerca con Google

• Schneider B, Mutel V, Pietri M, Ermoval M, Mouillet-Richard S, Kellermann O. NADPH oxidase and extracellular regulated kinases1/2 are targets of prions protein signalling in neuronal and nonneuronal cells. Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13326-31. Cerca con Google

• Schulz R. Intracellular targets of matrix metalloproteinase-2 in cardiac disease: rationale and therapeutic approaches. Annu Rev Pharmacol Toxicol. 2007;47:211-42. Cerca con Google

• Shmerling D, Hegyi I, Fischer M, Blättler T, Brandner S, Götz J, Rülicke T, Flechsig E, Cozzio A, von Mering C, Hangartner C, Aguzzi A, Weissmann C. Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell. 1998 Apr 17;93(2):203-14. Cerca con Google

• Shyu WC, Lin SZ, Chiang MF, Ding DC, Li KW, Chen SF, Yang HI, Li H. Overexpression of PrPC by Adenovirus-mediated gene targeting reduces ischemic injury in a stroke rat model. J Neurosci. 2005 Sep 28;25(39):8967-77. Cerca con Google

• Simons K, Ikonen E. Functional rafts in cell membranes. Nature. 1997 Jun 5;387(6633):569-72. Cerca con Google

• Sommerschild HT, Kirkebøen KA. Preconditioning endogenous defence mechanisms of the heart. Acta Anaesthesiol Scand. 2002 Feb;46(2):123-37. Cerca con Google

• Sorgato MC, Bertoli A. From cell protection to death: may Ca2+ signals explain the chameleonic attributes of the mammalian prion protein? Biochem Biophys Res Commun. 2009 Feb 6;379(2):171-4. Cerca con Google

• Sorgato MC, Peggion C, Bertoli A. Is, indeed, the prion protein a Harlequin servant of "many" masters? Prion. 2009 Oct;3(4):202-5. Cerca con Google

• Sparkes RS, Simon M, Cohn VH, Fournier RE, Lem J, Klisak I, Heinzmann C, Blatt C, Lucero M, Mohandas T. Assignment of the human and mouse prion protein genes to homologous chromosomes. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7358-62. Cerca con Google

• Spudich A, Frigg R, Kilic E, Kilic U, Oesch B, Raeber A, Bassetti CL, Hermann DM. Aggravation of ischemic brain injury by prion protein deficiency: role of ERK-1/-2 and STAT-1. Neurobiol Dis. 2005 Nov;20(2):442-9. Cerca con Google

• Steele AD, Lindquist S, Aguzzi A. The prion protein knockout mouse: a phenotype under challenge. Prion. 2007 Apr;1(2):83-93. Cerca con Google

• Steele AD, Zhou Z, Jackson WS, Zhu C, Auluck P, Moskowitz MA, Chesselet MF, Lindquist S. Context dependent neuroprotective properties of prion protein (PrP).Prion. 2009 Oct 16;3(4). Cerca con Google

• Stuermer CA, Langhorst MF, Wiechers MF, Legler DF, Von Hanwehr SH, Guse AH, Plattner H. PrPc capping in T cells promotes its association with the lipid raft proteins reggie-1 and reggie-2 and leads to signal transduction. FASEB J. 2004 Nov;18(14):1731-3. Cerca con Google

• Taylor DR, Hooper NM. The prion protein and lipid rafts. Mol Membr Biol. 2006 Jan-Feb;23(1):89-99. Cerca con Google

• Thomzig A, Schulz-Schaeffer W, Kratzel C, Mai J, Beekes M. Preclinical deposition of pathological prion protein PrPSc in muscles of hamsters orally exposed to scrapie. J Clin Invest. 2004 May;113(10):1465-72. Cerca con Google

• Ukeda H, Maeda S, Ishii T, Sawamura M. Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3'--1--(phenylamino)-carbonyl--3, 4-tetrazolium]-bis(4-methoxy-6-nitro)benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase. Anal Biochem. 1997 Sep 5;251(2):206-9. Cerca con Google

• Uptain SM, Lindquist S. Prions as protein-based genetic elements. Annu Rev Microbiol. 2002;56:703-41. Cerca con Google

• Valko M, Morris H, Cronin MT. Metals, toxicity and oxidative stress. Curr Med Chem. 2005;12(10):1161-208. Cerca con Google

• Vanden Hoek TL, Becker LB, Shao Z, Li C, Schumacker PT. Reactive oxygen species released from mitochondria during brief hypoxia induce preconditioning in cardiomyocytes. J Biol Chem. 1998 Jul 17;273(29):18092-8. Cerca con Google

• Vanden Hoek TL, Shao Z, Li C, Schumacker PT, Backer LB. Mitochondrial electron transport can become a significant source of oxidative injury in cardiomyocytes. J Mol Cell Cardiol. 1997 Sep;29(9):2441-50. Cerca con Google

• Vey M, Pilkuhn S, Wille H, Nixon R, DeArmond SJ, Smart EJ, Anderson RG, Taraboulos A, Prusiner SB. Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14945-9. Cerca con Google

• Vincent B, Paitel E, Saftig P, Frobert Y, Hartmann D, De Strooper B, Grassi J, Lopez-Perez E, Checler F. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J Biol Chem. 2001 Oct 12;276(41):37743-6. Cerca con Google

• Waggoner DJ, Drisaldi B, Bartnikas TB, Casareno RL, Prohaska JR, Gitlin JD, Harris DA. Brain copper content and cuproenzyme activity do not vary with prion protein expression level. J Biol Chem. 2000 Mar 17;275(11):7455-8. Cerca con Google

• Watt NT, Taylor DR, Gillott A, Thomas DA, Perera WS, Hooper NM. Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress. J Biol Chem. 2005 Oct 28;280(43):35914-21. Cerca con Google

• Weise J, Crome O, Sandau R, Schulz-Schaeffer W, Bähr M, Zerr I. Upregulation of cellular prion protein (PrPC) after focal cerebral ischemia and influence of lesion severity. Neurosci Lett. 2004 Nov 30;372(1-2):146-50. Cerca con Google

• Weise J, Doeppner TR, Müller T, Wrede A, Schulz-Schaeffer W, Zerr I, Witte OW, Bähr M. Overexpression of cellular prion protein alters postischemic Erk1/2 phosphorylation but not Akt phosphorylation and protects against focal cerebral ischemia. Restor Neurol Neurosci. 2008;26(1):57-64. Cerca con Google

• Weise J, Sandau R, Schwarting S, Crome O, Wrede A, Schulz-Schaeffer W, Zerr I, Bähr M. Deletion of cellular prion protein results in reduced Akt activation, enhanced postischemic caspase-3 activation, and exacerbation of ischemic brain injury. Stroke. 2006 May;37(5):1296-300. Cerca con Google

• Weissmann C, Flechsig E. PrP knock-out and PrP transgenic mice in prion research. Br Med Bull. 2003;66:43-60. Cerca con Google

• Weissmann C. Molecular genetics of transmissible spongiform encephalopathies. J Biol Chem. 1999 Jan 1;274(1):3-6. Cerca con Google

• White AR, Collins SJ, Maher F, Jobling MF, Stewart LR, Thyer JM, Beyreuther K, Masters CL, Cappai R. Prion protein-deficient neurons reveal lower glutathione reductase activity and increased susceptibility to hydrogen peroxide toxicity. Am J Pathol. 1999 Nov;155(5):1723-30. Cerca con Google

• Wong BS, Brown DR, Pan T, Whiteman M, Liu T, Bu X, Li R, Gambetti P, Olesik J, Rubenstein R, Sy MS. Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities. J Neurochem. 2001 Nov;79(3):689-98. Cerca con Google

• Zaccagnini G, Martelli F, Fasanaro P, Magenta A, Gaetano C, Di Carlo A, Biglioli P, Giorgio M, Martin-Padura I, Pelicci PG, Capogrossi MC. p66ShcA modulates tissue response to hindlimb ischemia. Circulation. 2004;109:2917–2923. Cerca con Google

• Zanata SM, Lopes MH, Mercadante AF, Hajj GN, Chiarini LB, Nomizo R, Freitas AR, Cabral AL, Lee KS, Juliano MA, de Oliveira E, Jachieri SG, Burlingame A, Huang L, Linden R, Brentani RR, Martins VR. Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection. EMBO J. 2002 Jul 1;21(13):3307-16. Cerca con Google

• Zanusso G, Vattemi G, Ferrari S, Tabaton M, Pecini E, Cavallaro T, Tomelleri G, Filosto M, Tonin P, Nardelli E, Rizzuto N, Monaco S. Increased expression of the normal cellular isoform of prion protein in inclusion-body myositis, inflammatory myopathies and denervation atrophy. Brain Pathol. 2001 Apr;11(2):182-9. Cerca con Google

• Zhang CC, Steele AD, Lindquist S, Lodish HF. Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal. Proc Natl Acad Sci U S A. 2006 Feb 14;103(7):2184-9. Cerca con Google

• Zielonka J, Vasquez-Vivar J, Kalyanaraman B. Detection of 2-hydroxyethidium in cellular systems: a unique marker product of superoxide and hydroethidine. Nat Protoc. 2008;3(1):8-21. Cerca con Google

Download statistics

Solo per lo Staff dell Archivio: Modifica questo record