Identification of monocyte chemoattractant protein-1 in senile plaques and reactive microglia of Alzheimer's disease
Corresponding Author
KOKO ISHIZUKA MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Department of Neuropsychiatry, Kumamoto University School of Medicine, Honjo 1-1-1, Kumamoto 860, Japan.Search for more papers by this authorTAKEMI KIMURA MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Search for more papers by this authorRURIKO IGATA-YI MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Search for more papers by this authorSHOICHI KATSURAGI MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Search for more papers by this authorJUNICHI TAKAMATSU MD
National Kikuchi Hospital, Kumamoto, Japan
Search for more papers by this authorTAIHEI MIYAKAWA MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Search for more papers by this authorCorresponding Author
KOKO ISHIZUKA MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Department of Neuropsychiatry, Kumamoto University School of Medicine, Honjo 1-1-1, Kumamoto 860, Japan.Search for more papers by this authorTAKEMI KIMURA MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Search for more papers by this authorRURIKO IGATA-YI MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Search for more papers by this authorSHOICHI KATSURAGI MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Search for more papers by this authorJUNICHI TAKAMATSU MD
National Kikuchi Hospital, Kumamoto, Japan
Search for more papers by this authorTAIHEI MIYAKAWA MD
Department of Neuropsychiatry, Kumamoto University School of Medicine
Search for more papers by this authorWe thank Dr Motohiro Takeya for his editorial advice and Mr Toshiyuki Hisano for his excellent technical assistance.
Abstract
Abstract It has been shown that human monocytes express monocyte chemoattractant protein-1 (MCP-1), an inflammatry factor, in response to non-fibrillar β-amyloid protein. Reactive microglia and inflammatory factors were reported to be present in β-amyloid deposits (senile plaques) in Alzheimer's disease, suggesting the presence of MCP-1 in senile plaques. To address this issue, we examined MCP-1-immunoreactivity in senile plaques using a mouse monoclonal anti-MCP-1 antibody. Monocyte chemoattractant protein-1 was found immunohistochemically in mature senile plaques and reactive microglia but not in immature senile plaques of brain tissues from five patients with Alzheimer's disease. These findings suggest that MCP-1-related inflammatory events induced by reactive microglia contribute to the maturation of senile plaques.
REFERENCES
- 1 Hardy J., Allsop D. Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 1991; 12: 383–388.
- 2 Khachaturian ZS. Diagnosis of Alzheimer's disease. Arch. Neurol. 1985; 42: 1097–1105.
- 3 Sisodia SS., Koo EH., Beyreuther K., Unterbeck A., Price DL. Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing. Science 1990; 248: 492–495.
- 4 Shoji M. Golde TE. Ghiso J. et al. Production of the Alzheimer amyloid β protein by normal proteolytic processing. Science 1992; 258: 126–129.
- 5 Haass C., Koo EH., Mellon A., Hung AY., Selkoe DJ. Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments. Nature 1992; 357: 500–503.
- 6 Estus S. Golde TE. Kunishita T. et al. Potentially amyloidogenic, carboxyl-terminal derivatives of the amyloid protein precursor. Science 1992; 255: 726–728.
- 7 Golde TE., Estus S., Younkin LH., Selkoe DJ., Younkin SG. Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 1992; 255: 728–730.
- 8 Caporaso GL., Gandy SE., Buxbaum JD., Greengard P. Chloroquine inhibits intracellular degradation but not secretion of Alzheimer β/A4 amyloid precursor protein. Proc. Natl Acad. Sci. USA 1992; 89: 2252–2256.
- 9 Haass C. Schlossmacher MG. Hung AT. et al. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 1992; 359: 322–325.
- 10 McGeer PL., Rogers J., McGeer EG. Neuroimmune mechanisms in Alzheimer disease pathogenesis. Alzheimer Dis. Discord. 1994; 8: 149–158.
- 11 Vandenabeele P., Fiers W. Is amyloidogenesis during Alzheimer's disease due to an IL-1/IL-6-mediated ‘acute phase response’ in the brain? Immunol Today 1991; 12: 217–219.
- 12 Aisen PS., Davis KL. Inflammatory mechanisms in Alzheimer's disease: Implications for therapy. Am. J. Psychiatry 1994; 151: 1105–1113.
- 13 Griffin WS. Stanley LC. Ling C. et al. Brain interleukin 1 and S-100 immunoreactivity are elevated in Down syndrome and Alzheimer disease. Proc. Natl Acad. Sci. USA 1989; 86: 7611–7615.
- 14 Andersen K., Launer LJ., Ott A., Hoes AW., Bretler MM., Hofman A. Do nonsteroidal anti-inflammatory drugs decrease the risk for Alzheimer's disease? The Rotterdam Study. Neurology 1995; 45: 1441–1445.
- 15 Rich JB., Rasmusson DX., Folstein MF., Carson KA., Kawas, C. Brandt, J. Nonsteroidal anti-inflammatory drugs in Alzheimer's disease. Neurology 1995; 45: 51–55.
- 16 Leonard EJ., Yoshimura T. Human monocyte chemoattractant protein-1 (MCP-1). Immunol. Today 1990; 11: 97–101.
- 17 Euentes ME. Durham SK. Swerdel MR. et al. Controlled recruitment of monocytes and macrophages to specific organs through transgenic expression of monocyte chemoattractant protein-1. J. Immunol. 1995; 155: 5769–5776.
- 18 Hurwitz AA., Lyman WD., Berman JW. Tumor necrosis factor alpha and transforming growth factor beta upregulate astrocyte expression of monocyte chemoattractant protein-1. J. Neuroimmunol. 1995; 57: 193–198.
- 19 Meda L. Bernasconi S. Bonaiuto C. et al. β-amyloid (25–35) peptide and IFN-γ synergistically induce the production of the chemotactic cytokine MCP-1/JE in monocytes and microglial cells. J. Immunol. 1996; 157: 1213–1218.
- 20 Hulkower K. Brosnan CF. Aquino DA. et al. Expression of CSF-1, c-fms, and MCP-1 in the central nervous system of rats with experimental allergic encephalomyelitis. J. Immunol. 1993; 150: 2525–2533.
- 21 Ransohoff RM. Hamilton TA. Tani M. et al. Astrocyte expression of mRNA encoding cytokines IP-10 and JE/MCP-1 in experimental autoimmune encephalomyelitis. FASEB J. 1993; 7: 592–600.
- 22 American Psychiatric Association. Diagnostic and Statistical Manual of Mental Disorders, 3rd edn revised. American Psychiatric Association, Washington , DC , 1987.
- 23 Yamaguchi H., Haga C., Hirai S., Nakazato Y., Kosaka K. Distinctive, rapid and easy labeling of diffuse plaques in the Alzheimer brains by a new methenamine silver stain. Acta Neuropathol. 1990; 79: 569–572.
- 24 Delaere P., Duyckaerts C., He Y., Piette F., Hauw JJ. Subtypes and differential laminar distributions of β A4 deposits in Alzheimer's disease: Relationship with the intellectual status of 26 cases. Acta Neuropahol. 1991; 81: 328–335.
- 25 Sparks DL., Liu H., Scheff SW., Coyne CM., Hunsaker JC III. Temporal sequence of plaque formation in the cerebral cortex of non-demented individuals. J. Neuropathol. Exp. Neurol. 1993; 52: 135–142.
- 26 Berg L., McKeel DW. Jr, Miller JP., Baty J., Morris JC. Neuropathological indexes of Alzheimer's disease in demented and non-demented persons aged 80 years and older. Arch. Neurol. 1993; 50: 349–358.
- 27 Crystal HA. Dickson DW. Sliwinski MJ. et al. Pathological markers associated with normal aging and dementia in the elderly. Ann. Neurol. 1993; 34: 566–573.
- 28 Yankner BA., Duffy LK., Kirschner DA. Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides. Science 1990; 250: 279–282.
- 29 Pike CJ., Walencewicz AJ., Glabe CG., Cotman CW. In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 1991; 563: 311–314.
- 30 Pike CJ., Burdick D., Walencewicz AJ., Glabe CG., Cotman CW. Neurodegeneration induced by β-amyloid peptides in vitro. The role of peptide assembly state. J. Neurosci. 1993; 13: 1676–1687.
- 31 Selkoe DJ. Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 1994; 10: 373–403.
- 32 Verbeek, MM. Otte-Holler, I. Wesseling, P. A lysosomal marker for activated microglial cells involved in Alzheimer classic senile plaques. Acta Neuropathol. 1995; 90: 493–503.
- 33 Mackenzie IR., Hao C., Munoz DG. Role in microglia in senile plaque formation. Neurobiol. Aging 1995; 16: 797–804.
- 34 Cras P. Kawai M. Siedlak S. et al. Neuronal and microglial involvement in β-amyloid protein deposition in Alzheimer's disease. Am. J. Pathol. 1990; 137: 241–246.
- 35 Perlmutter LS., Scott SA., Barron E., Chui HC. MHC class II-positive microglia in human brain: Association with Alzheimer lesions. J. Neurosci. Res. 1992; 33: 549–558.
- 36 Yan SD. Chen X. Fu J. et al. RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 1996; 382: 685–691.
- 37 El Khoury, J., Hickman SE., Thomas CA., Cao L., Silverstein SC., Loike JD. Scavenger receptor-mediated adhesion of microglia to β-amyloid fibrils. Nature 1996; 382: 716–719.
