Transduction of Familial Amyotrophic lateral sclerosis-related mutant PEP-1-SOD proteins into neuronal cells

Molecules and Cells

Volumn 25, Issue 1, 2008, Pages 55-63

  An, Jae Jin ^a   Lee, Yeon Pyo ^a   Kim, So Young ^a   Lee, Sun Hwa ^a   Kim, Dae Won ^a   Lee, Min Jung ^a   Jeong, Min Seop ^a   Jang, Sang Ho ^a   Kang, Jung Hoon ^b   Kwon, Hyeok Yil ^a   Kang, Tae Cheon ^a   Won, Moo Ho ^a   Cho, Sung Woo ^c   Kwon, Oh Shin ^d   Lee, Kil Soo ^a   Park, Jinseu ^a   Eum, Won Sik ^a   Choi, Soo Young ^a  

^a Hallym University   (South Korea)

^b Chongju University   (South Korea)

^c University of Ulsan College of Medicine   (South Korea)

^d Kyungpook National University   (South Korea)

Author keywords

Amyotrophic lateral sclerosis (ALS); Cu,Zn superoxide dismutase (SOD1); Heat shock protein (Hsp); Protein transduction

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE PEPTIDE FUSION PROTEIN; HEAT SHOCK PROTEIN; HYBRID PROTEIN; PARAQUAT; SUPEROXIDE DISMUTASE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL CELL; ARTICLE; CONCENTRATION RESPONSE; CYTOTOXICITY; EXPRESSION VECTOR; FAMILIAL DISEASE; GENE EXPRESSION; GENE MUTATION; GENETIC ASSOCIATION; GENETIC TRANSDUCTION; MUTANT; NERVE CELL; NEWBORN; NONHUMAN; OXIDATIVE STRESS; PATHOPHYSIOLOGY; PROTEIN EXPRESSION; PROTEIN PURIFICATION; RAT; WILD TYPE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; ASTROCYTES; CELL SURVIVAL; CELLS, CULTURED; CYSTEAMINE; HEAT-SHOCK PROTEINS; HUMANS; OXIDATIVE STRESS; PEPTIDES; RATS; RATS, WISTAR; RECOMBINANT FUSION PROTEINS; SUPEROXIDE DISMUTASE; TRANSDUCTION, GENETIC;

BACTERIA (MICROORGANISMS);

EID: 42949157227     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (48)

1. Aguirre, T., Van Den Bosch, L., Goetschalckx, K., Tilkin, P., Mathijs, G., Cassiman, J.J., and Robberecht, W. (1998). Increased sensitivity of fibroblasts from familial amyotrophic lateral sclerosis patients to oxidative stress. Ann. Neurol. 43, 452-457.
2. Andersen, P.M. (2001). Genetics of sporadic ALS. Amyotroph. Lateral Scler. Other. Mol. Neruon Disord. 2 (Suppl. 1), S37-S41.
3. Andrus, P.K., Fleck, T.J., Gurney, M.E., and Hall, E.D. (1998). Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis. J. Neurochem. 71, 2041-2048.
4. Bellmann, K., Wenz, A., Radons, J., Burkart, V., Kleemann, R., and Kolb, H. (1995). Heat shock induces resistance in rat pancreatic islet cells against nitric oxide, oxygen radicals and streptozotocin. toxicity in vitro. J. Clin. Invest. 95, 2840-2845.
5. Bradford, M. (1976). A rapid and sensitive method for the quantitation of microgram quantities utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
6. Brochelt, D.R., Guarnieri, M., Wong, P.C., Lee, M.K., Slunt, H.S., Xu, Z.S., Sisodia, S.S., Price, D.L., and Cleveland, D.W. (1995). Superoxide dismutase 1 subunits with mutations linked to familial amyotsophic lateral sclerosis do not a affect wild type subunit function. J. Biol. Chem. 270, 3234-3238.
7. Brooks, B.R., Sanjak, M., Belden, D., Juhasz-Poscine, K.; and Waclawik, A. (2000). Amyotrophic, lateral sclerosis. R.H., Brown, V., Meininger, M., Swash, eds. (London, UK), pp. 31-58.
8. Bruijn, L.I., Houseweart, M.K., K ato, S., Anderson, K.L., Anderson, S.D., Ohama, E., Reaume, A.G., Scott, R.W., and Cleveland, D.W. (1998). Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild type SOD1. Science 281, 1851-1854.
9. Choi, H.S., An, J.J., Kim, S.Y., Lee, S.H., Kim, D.W., Yoo, K.Y., Won, M.H., Kang, T.C., Kwon, H.J., Kang, J.H., et al. (2006a). PEP-1-SOD fusion protein efficiently protects against paraquat-induced dopaminergic neuron damage in a Parkinson disease mouse model. Free Radic. Biol. Med. 41, 1058-1068.
10. Choi, S.H., Kim, S.Y., An, J.J., Lee, S.H., Kim, D.W., Ryu, H.J. Lee, N.I., Yeo, S.I., Jang, S.H., Won, M.H., et al. (2006b) Human, PEP-1-ribosomal pAtein S3 protects against UV-induced skin cell death. FEBS Lett. 580, 6755-6762.
11. Cleveland, D.W. and Rothstein, J.D. (2001) From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2, 806-919.
12. Durham, H.D., Roy, J., Dong, L., and Figlewicz, D.A. (1997). Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Neuropathol. Exp. Neurol. 56, 523-530.
13. Eum W.S., Chaung, I.S., Li, M.Z., Kang, J.H., Kim, D.W., Park, J., Kwon, H.Y., and Choi, S.Y. (2004a). HIV-1 Tat mediated protein transduction of Cu,Zn-superoxide dismutase into pancreatic β cells in vitro and in vivo. Free Radic. Biol. Med. 37, 339-349.
14. Eum, W.S., Kim, D.W., Hwang, I.K., Yoo, K.Y., Kang, T.C., Jang, S.H., Choi, H.S., Choi, S.H., Kim, Y.H., Kim, S.Y., et al. (2004b). In vivo protein transduction: Biologically active intact PEP-1-superoxide dismutase fusion protein efficiently protects against ischemic insult. Free Radic. Biel. Med. 37, 1656-1669.
15. Fawell, S., Seery, J., and Daikh, Y. (1991). Tat-mediated delivery of heterologous proteins into cells. Proc. Natl. Acad. Sci. USA 91, 664-668.
16. Ferrante, R.J., Brown, S.E., Shinobu, L.A., Bowling, A.C., Baik, M.J., MacGarvey, U., Kowall, N.W., Brown, R.H., and Beal, M.F. (1997). Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J. Neurochem. 69, 2064-2074.
17. Fridovich, I. (1995). Superoxide radical and superoxide dismutase. Annu. Rev. Biochem. 64, 97-112.
18. Gabbinanelli, R., Ferri, A., Rotilio, G., and Carri, M.T. (1999). Aberrant copper chemistry as a major mediator of oxidative stress in a human cellular model of amyotrophic lateral sclerosis. J. Neurochem. 73, 1175-1180.
19. Garrido, C., Gurbuxani, S., Ravagnan, L., and Kroemer, G. (2001). Heat shock proteins: endogeneous modulators of apoptotic cell death. Biochem. Biophys. Res. Commum. 286, 433-442.
20. Gaudette, M., Hirano, M., and Siddique, T. (2000). Current status of SOD1 mutations in familial amyotrophic lateral sclerosis. Amyotroph. Lateral Scler. Other. Mol. Neruon Disord. 1, 83-89.
21. Goto, J.J., Zhu, H., Sanchez, R.J., Nersissian, A., Gralla, E.B., Valentine, J.S., and Cabelli, D.E. (2000). Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutase associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 275, 1007-1014.
22. Gurney, M.E., Pu, H., Chiu, A.Y., Dal Canto, M.G, Polchow, C. Y., Alexander, D.D., Caliendo, J., Hentati, A., Kwon, Y.W., Deng, H. X., et al. (1994). Motor neuron degeneration in mice that express a human Cu,Zn-superoxide dismutase mutantion. Science 264, 1772-1775.
23. Ha, K.T., Lee, Y.C., Cho, S.H., Kim, J.K., and Kim, C.H. (2004). Molecular characterization of membrane type and ganglioside-specific sialidase (Neu3) expressed in E. coli. Mol. Cells 17, 267-273.
24. Hough, M.A., Grossmann, J.G., Antonyuk, S.V., Strange, R.W., Doucette, P.A., Rodriguez, J.A., Whitson, L.J., Hart, P.J., Hayward, L.J., Valentine, J.S., et al. (2004). Dimer destabilization in superoxide dismutase ay results in disease-causing properties: structures of motor neuron disease mutants. Proc. Natl. Acad. Sci. USA 101, 5976-5981.
25. Johnston, J.A., Dalton, M.J., Gurney, M.E., and Kopito, R.R. (2000). Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA 97, 12571-12576.
26. Kang, J.H. and Eum, W.S. (2000). Enhanced oxidative damage by the familial amyotrophic lateral sclerosis-associated Cu, Zn-superoxide dismutase mutants. Biochim. Biophys. Acta 1524, 162-170.
27. Kim, C.H. (2003). A Salmonella typhimurium rfaE mutants recovers invasiveness for human epithelial cells when complemented by wild type rfaE (confering biosynthesis of ADP-L-glycero-D-manno-heptose-containing lipopolysaccharide). Mol. Cells 15, 226-232.
28. Kim, D.W., Eum, W.S., Jang, S.H., Kim, S.Y., Choi, H.S., Choi, S.H., An, J.J., Lee, S.H., Lee, K.S., Han, K., et al. (2005). Transduced Tat-SOD fusion protein protects against ischemic brain injury. Mol. Cells 19, 88-96.
29. Latchman, D.S. (2005). HSP27 and cell survival in neurons. Int. J. Hyperthermia. 21, 393-402.
30. Liu, H., Zhu, H., Eggers, D.K., Nersissian, A.M., Faul, K.F., Goto, J.J., Ai, J., Sanders-Loehr, J., Gralla, E.B., and Valentine, J.S. (2000). Copper(2+) binding to the surface residue cystein 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant. Biochemistry 39, 8125-8132.
31. MaCord, J.M. and Fridovich, I. (1969). Superoxide dismutase. J. Biol. Chem. 244, 6049-6055.
32. Manning-Bog, A.B., McCormack, A.L., Purisai, M.G., Bolin, L.M., and Di Monte, D.A. (2003). α-synuclein overexpression protects against paraquat-induced neuro degeneration. J. Neurosci. 23, 3095-3099.
33. Morris, M.C., Depollier, J., Mery, J., Heitz, F., and Divita, G (2001). A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nat Biotechnol. 19, 1173-1176.
34. Mulder, D.W., Kurland, L.T., Offord, K.P., and Beard, C.M. (1986). Familial adult motor neuron disease: amyotrophic lateral sclerosis. Neurology 36, 511-517.
35. Naval, M.V., Gomez-Serranillos, M.P., Carretero, M.E., and Villar, A.M. (2007). Neuroproteetive effect of a ginseng (Panax ginseng) root extract on astrocytes primary culture. J. Ethnopharmacol. 112, 262-270.
36. Oeda, T., Shimohama, S., Kitagawa, N., Kohno, R., Imura, T., Shibasaki, H., and Ishii, N. (2001). Oxidative stress causes abnormal accumulation of familial amyotrophic lateral sclerosis-related mutant SOD1 in transgenic Caenorhabditis elegans. Human Mol. Genetic. 10, 2013-2023.
37. Okado-Matsumoto, A. and Fridovich, I. (2002). Amyotrophic lateral sclerosis: a proposed mechanism. Proc. Natl. Acad. Sci. USA 99, 9010-9014.
38. Prochiantz, A (2000). Messenger proteins: homeoptoteins, TAT and others. Curr. Opin. Cell Biol. 12, 400-406.
39. Rosen, D.R., Siddigue, T., Patterson, O., Figlewicz, D.A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J.P., Deng, H. X., et al. (1993). Mutation in Cu,Zn-superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59-62.
40. Rowland, L.P. and Shneider, N.A. (2001). Amyotrophic lateral sclerosis. N. Engl. J. Med. 345, 1131-1132.
41. Seo, S.M., Lee, J.H., and Kim, Y.M. (2007). Characterization of an iron- and manganese-containing superoxide dismutase from Methyllobacillus Sp. strain SKIDSM8269. Mol. Cells 23, 370-378.
42. Stieber, A., Gonatas, J.O., and Gonatas, N.K. (2000). Aggregation of ubiquitin and a mutant ALS-linked SOD1 protein correlate with disease progressive and fragmentation of the Golgi apparatus. J. Neurol. Sci. 173, 53-62.
43. Tiwari, A. and Hayward, L.J. (2003). Familial-amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction. J. Biol. Chem. 278, 5984-5992.
44. Vives, E., Brodin, P., and Lebleu, B. (1997). A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272, 16610-16017.
45. Wadia, J.S. and Dowdy, S.F. (2002). Protein transduction technology. Curr. Opin. Biotechnol. 13, 52-56.
46. Wagstaff, M.J.D., Collaco-Moraes, Y., Smith, J., de Belleroche, J., Coffin, R.S., and Latchman, D.S. (1999). Protection of neuronal cells from apoptosis by Hsp27 delivered with a herpes simplex virus-based vector. J. Biol. Chem. 274, 5061-5069.
47. Yim, M.B., Kang, J.H., Yim, H.S., Kwak, H.S., Chock, P.B., and Stadtman, E.R. (1996). A gain-of function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: an enhancement of free radical formation due to a decrease in Km for hydrogen peroxide. Proc. Natl. Acad. Sci. USA 93, 5709-5714.
48. Yim, H.S., Kang, J.H., Chock, P.B., Stadtman, E.R., and Yim, M.B. (1997). A familial amyotrophic lateral sclerosis-associated A4V Cu,Zn-superoxide dismutase mutants has a low Km for hydrogen peroxide: Correlation between clinical severity and the Km value. J. Biol. Chem. 272, 8861-8863.