The effect of postmortem delay on the distribution of microtubule-associated proteins τ, MAP2, and MAP5 in the rat
- 10 Downloads
Breakdown or disruption of the cytoskeleton has been implicated in the neurodegenerative processes of a variety of diseases, including Alzheimer disease (AD) and stroke. Studies of such diseases in the human involve the use of postmortem brain tissue. Postmortem delay may vary considerably from a few hours to a few days, and within this period, a degree of cytoskeletal breakdown may occur. It is therefore crucial to examine alterations occurring in the cytoskeleton as a result of postmortem delay and subtract these from those caused by the disease. In this study, the distribution of τ, MAP2, and MAP5 immunohistochemistry was examined following postmortem intervals of 0–72 h in the rat cerebral cortex, corpus callosum, caudate nucleus, and hippocampus. Each microtubule-associated protein (MAP) underwent unique changes that were dependent both on postmortem interval and the brain region examined. Following long postmortem delays, some of the changes in these proteins were similar to those seen in rodent models of cerebral ischemia. These results demonstrate that MAPs are not stable during postmortem delay in the rat. Therefore, caution must be exercised when interpreting changes in MAPs in human postmortem tissue, especially in cases where ischemic injury may be involved. Examination of control tissue carefully matched for postmortem delay is therefore essential to allow meaningful interpretation of cytoskeletal abnormalities in human neurodegenerative disease.
Index Entriesτ microtubule-associated protein cytoskeleton oligodendrocyte
Unable to display preview. Download preview PDF.
- Adams J. H. and Graham D. (1989a) Vascular and hypoxic disorders, inAn Introduction to Neuropathology. Churchill Livingstone, pp. 57–82.Google Scholar
- Adams J. H. and Graham D. (1989b) Trauma, inAn Introduction to Neuropathology. Churchill Livingstone, pp. 118–136.Google Scholar
- Davis D. R., Brion J-P, Couck A-M., Gallo J-M., Hanger D., Ladhani K., Lewis C., Miller C. J., Rupniak T., Smith C., and Anderton B. H. (1995) The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures.Biochem. J. 309, 941–949.PubMedGoogle Scholar
- Dewar D. and Dawson D. (1995b) Microtubule-associated proteins in focal cerebral ischaemia.J. Neurotrauma 12, 455.Google Scholar
- Irving E. A., McCulloch J., and Dewar D. (1996) Intracortical perfusion of glutamate in vivo induces alterations of tau and MAP2 immunoreactivity in the rat.Acta Neuropath. 92, 182–196.Google Scholar
- Irving E. A., Barnett S. C., Dickinson P., McCulloch J., Dewar D., and Griffiths I. R. (1995) Increased tau immunoreactivity within oligodendrocytes following cytotoxic injury.Soc. Neurosci. Abstract 134, 9.Google Scholar
- Kitagawa K., Matsumoto M., Niinobe M., Mikoshiba K., Hata R., Ueda H., Handa N., Fukunaga R., Isaka Y., Kimura K., and Kamada T. (1989) Microtubule-associated protein 2 as a sensitive marker for cerebral ischemic damage-immunohistochemical investigation of dendritic damage.Neuroscience 31, 401–411.PubMedCrossRefGoogle Scholar
- Kosik K. S., Duffy L. K., Dowling M. M., Abraham C. R., McCluskey A., and Selkoe D. J. (1984) Microtubule-associated protein 2: monoclonal antibodies demonstrate the selective incorporation of certain epitopes into Alzheimer neurofibrillary tangles.Proc. Natl. Acad. Sci. USA 81, 7941–7945.PubMedCrossRefGoogle Scholar
- Martin S. M., Landel H. B., Lansing A. J., and Vijayan V. K. (1991) Immunocytochemical double labeling of glial fibrillary acidic protein and transferrin permits the identification of astrocytes and oligodendrocytes in the rat brain.J. Neuropathol. Exp. Neurol. 50, 161–170.PubMedCrossRefGoogle Scholar
- Ulloa L., Montejo de Garcini E., Gomez-Ramos P., Moran M. A., and Avila J. (1994) Microtubule-associated protein MAP1B showing a fetal phosphorylation pattern is present in sites of neurofibrillary degeneration in brains of Alzheimer's disease patients.Mol. Brain Res. 26, 113–122.PubMedCrossRefGoogle Scholar
- Yamada M., Wada Y., Tsukagoshi H., Otomo E-I., and Hayakawa M. (1988) A quantitative Golgi study of basal dendrites of hippocampal CA1 pyramidal cells in senile dementia of Alzhemier type.J. Neurol. Neurosurg. Psych. 51, 1088–1090.Google Scholar