Abstract
Oxidative stress is suggested as a significant causative factor forpathogenesis of neuronal degeneration on spinal cord of human ALS. Wemeasured some enzymic activities implicating neuronal degenerationprocess, such as cytochrome c oxidase (CO), superoxidedismutase (SOD), and transglutaminase (TG) in spinalcord of an animal model of ALS, motor neuron degeneration(Mnd) mouse, a mutant that exhibits progressivedegeneration of lower spinal neurons during developmental growth, andcompared them with age-matched control C57BL/6 mice. CO activity inMnd spinal cord decreased during early postnatal period, whileSOD activity reduced in later stage. In Mnd tissue, TG activityin lumbar cord was increasing during early stage, but tended to declinein later period gradually. These biochemical alterations became evidentprior to the appearance of clinical motor dysfunction which wereobserved in later stages of development in Mnd spinal cord.
Similar content being viewed by others
REFERENCES
Caroscio, J. T., Mulvibill, M. M., Sterling, R., and Abrams, B., 1987. Amyotrophic lateral sclerosis: its natural history, Neurol. Clin. 5:1-8.
Gsell, W., Conrad, R., Hicketheir, M., Sofic, E., Fralich, L., Wichart, I., Jellinger, K., Mall, G., Rausmayer, G., Beckman, H., and Riederer, P., 1995. Decreased catalase activity but unchanged superoxide dismutase activity in brains of patients with dementia of Alzheimer type. J. Neurochem. 64:1216-1223.
Przedborski, S., Jackson-Lewis, V., Kostic, V., Carlson, E., Epstein, C. J., and Cadet, J. L., 1992. Superoxide sidmutase, catalase, and glutathion peroxidase activities in copper/zinc-superoxide dismutase transgenic mice, J. Neurochem. 62:384-387.
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, Jr., Deng, H-X., Rahmani, Z., Krizus, A., McKenna-Ysek, D., Cayabyab, A., Gaston, S. M., Berger, R., Tanzi, R., Halperin, J. J., Herzfeld, B., Van der Bergh, R., Hung, W., Bird, T., Deng, G., Mulder, D. W., Smyth, C., Laing, N. G., Soriano, E., Pericak-Vance Haines, J., Rouleau, G. A., Gusella, J. S., Horocitz, H. R., and Brown, R. H. Jr., 1993. Mutation in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis, Nature 362:59-62.
Gurney, M. E., Pu, H., Chiu, A. Y., DalCanto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Heitati, A., Kwon, Y. W., Deng, H-X., Chen, W., Zhai, P., Suftt, R. L., and Siddique, T., 1994. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation, Science 264:1772-1775.
Richter, C., Park, J-W., and Ames, B. M., 1988. Neuronal oxidative damage to mitochondrial and nuclear DNA is extensive, Proc. Nat. Acad. Sci. USA. 85:6465-6467.
Fujita, K., Yamauchi, K., Shibayama, K., Ando, M., Honda, M., and Nagata, Y., 1996. Decreased cytochrome c oxidase activity but unchanged superoxide dismutase and glutathione peroxidase activities in the spinal cord of patients with amyotrophic lateral sclerosis, J. Neurosci. Res. 45:276-281.
Greenkerg, C. S., Birchbichler, P. J., and Rice, G. H., 1991. Transglutaminase: multifunctional cross-linking enzymes that stabilize tissues, FEBS Lett., 5:3071-3077.
Ando, M., Kunii, S., Tatematsu, T., and Nagata, Y., 1993. Rapid and transient alterations in transglutaminase activity in rat superior cervical ganglion following denervation or axotomy, Neurosci. Res. 17:47-52.
Fujita, K., Ando, M., Yamauchi, M., Nagata, Y., and Honda, M., 1995. Alteration of transglutaminase activity in rat and human spinal cord after neuronal degeneration, Neurochem. Res. 20:1195-1201.
Messer, A., Strominger, N. L., and Mazurkiewicz, J. E., 1987. Histopathology of the late-onset motor neuron degeneration (Mnd) mutant in the mouse, J. Neurogenet. 4:201-213.
Pardo, C. A., Rabin, R. A., Palmer, D. W., and Price, D. L., 1994. Accumulation of the adenosine triphosphate synthase subunit in the Mnd mutant mouse, a model for neuronal ceroid lipofuscinosis, Am. J. Pathol., 144:829-835.
Messer, A., Plummer, J., Maskin, P., Coffin, J. M., and Frankel, W. N., 1992. Mapping of the motor neuron degeneration (Mnd) gene, a mouse model of amyotrophic lateral sclerosis (ALS), Genemics 18:797-802.
Callahan, L. M., Esther, P. S., Nylen, E. L., Messer, A., and Mazurkiewicz, J. E., 1991. Neurofilament distribution isolated in the Mnd (motor neuron degeneration) mouse, J. Neuropathol. Exp. Neurol. 50:491-504.
Wharton, D. C., and Tzagoloff, A., 1976. Cytochrome oxidase from beef heart mitochondria, Methods Enzymol. 10:245-250.
Misra, N. P., and Fridovich, I., 1972. The role of superoxide anion in the autooxidation of epinephrine and a simple assay for superoxide dismutase, J. Biol. Chem. 249:3170-3175.
Lorand, L., Campbell-Wikes, L. K., and Cooperstein, L., 1972. A filter paper assay for transamidating enzymes using radioactive amine substrates, Analy. Biochem. 50:623-631.
Bradford, M. M., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72:242-252.
Klüver, H., and Barrera, E., 1954. On the use of azapolphin derivatives (pathalocyanines) in staining nervous tissue, J. Physiol., 37:631-633.
Almeida, A., Allen, K. L., Bates, T. E., and Clark, J. B., 1995. Effect of reperfusion following cerebral ischemia on the activity of mitochondrial respiratory chain in the gerbil brain, J. Neurochem. 65:1698-1703.
Bowling, A. C., Mutisya, E. M., Walker, L. C., Price, D. L., Cork, L. C., and Beal, M. F., 1993. Age-dependent impairment of mitochondrial function in primate brain, J. Neurochem. 60:1964-1967.
Mugge, H. P., Elwell, J. H., Peterson, T. E., and Harrison, D. G., 1991. Release of intact endothelium-derived relaxing factor depends on endothelial SOD activity, Am. J. Physiol. 260:C219-C222.
Battaglioli, G., Martin, D. L., Plummer, J., and Messer, A., 1993. Synaptosomal glutamate uptake declines progressively in the spinal cord of a mutant mouse with motor neuron disease, J. Neurochem. 60:1567-1569.
Fesus, L., Thomazy, V., and Falus, A., 1988. Reaching for function of tissue transglutaminase; its possible involvement in biochemical pathway of programmed cell death, Adv. Exp. Biol. 231:119-139.
Folk, J. E. 1980. Transglutaminase, Ann. Rev. Biochem. 49:517-531.
Holmes, F. E., and Haynes, L. W., 1996. Superactivation of transglutaminase type 2 without change in enzyme level occurs during progressive neurodegeneration in the mnd mouse mutant, Neurosci. Lett. 213:185-188.
Dudek, S. M., and Johnson, G. V. W., 1993. Transglutaminase catalyses the formation of sodium dodecyl sulfate-insoluble Alz 50-reactive polymers of tissue, J. Neurochem. 61:1159-1162.
Miller, C. C. J., and Anderton, B. H., 1986. Transglutaminase and the neuronal cytoskeleton in Alzheimer's disease, J. Neurochem. 46:1912-1922.
Katoh, S., Nakagawa, Y., Yano, Y., Kohno, H., and Ohkubo, Y., 1996. Transglutaminase induced by epidermal growth factor negatively regulates the growth signal in primary cultures hepatocytes, Biochem. J. 313:305-309.
Fujita, K., Yamauchi, M., Matsui, T., Titani, K., Takahashi, H., Kato, T., Isomura, G., Ando, M., and Nagata, Y., 1998. Increase of glial fibrillary acidic protein fragments in the spinal cord of motor neuron degeneration mutant mouse, Brain Res., in press.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Fujita, K., Shibayama, K., Yamauchi, M. et al. Alteration of Enzymatic Activities Implicating Neuronal Degeneration in the Spinal Cord of the Motor Neuron Degeneration Mouse During Postnatal Development. Neurochem Res 23, 557–562 (1998). https://doi.org/10.1023/A:1022442904179
Issue Date:
DOI: https://doi.org/10.1023/A:1022442904179