Chondroitin Sulfate Proteoglycans Are a Common Component of Neuronal Inclusions and Astrocytic Reaction in Neurodegenerative Diseases

David A. Dewitt; P. L. Richey; D. Praprotnik; J. Silver; G. Perry

Chondroitin Sulfate Proteoglycans Are a Common Component of Neuronal Inclusions and Astrocytic Reaction in Neurodegenerative Diseases

David A. Dewitt, P. L. Richey, D. Praprotnik, J. Silver, G. Perry

Research output: Contribution to journal › Article

Abstract

Previously, we showed three differentially sulfated forms of chondroitin sulfate proteoglycans (CSPG) associated with senile plaques, astrocytes and neurofibrillary tangles in Alzheimer's disease. Here, monoclonal antibodies were used to demonstrate CSPGs in other neurodegenerative diseases. CSPGs were found associated with inclusions of Parkinson's, diffuse Lewy body, Pick's diseases, and progressive supranuclear palsy. Reacting astrocytes in each of these neurodegenrative diseases and Huntington's disease showed immunoreactivity for CSPG. CSPG distribution in a variety of neurodegenerative diseases suggests that similar mechanisms may be involved in the accumulation of proteoglycans in a number of filamentous inclusions.

Original language	Undefined/Unknown
Journal	Faculty Publications and Presentations
State	Published - Jan 1 1994
Externally published	Yes

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title = "Chondroitin Sulfate Proteoglycans Are a Common Component of Neuronal Inclusions and Astrocytic Reaction in Neurodegenerative Diseases",

abstract = "Previously, we showed three differentially sulfated forms of chondroitin sulfate proteoglycans (CSPG) associated with senile plaques, astrocytes and neurofibrillary tangles in Alzheimer's disease. Here, monoclonal antibodies were used to demonstrate CSPGs in other neurodegenerative diseases. CSPGs were found associated with inclusions of Parkinson's, diffuse Lewy body, Pick's diseases, and progressive supranuclear palsy. Reacting astrocytes in each of these neurodegenrative diseases and Huntington's disease showed immunoreactivity for CSPG. CSPG distribution in a variety of neurodegenerative diseases suggests that similar mechanisms may be involved in the accumulation of proteoglycans in a number of filamentous inclusions.",

author = "Dewitt, {David A.} and Richey, {P. L.} and D. Praprotnik and J. Silver and G. Perry",

year = "1994",

month = jan,

day = "1",

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journal = "Faculty Publications and Presentations",

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T1 - Chondroitin Sulfate Proteoglycans Are a Common Component of Neuronal Inclusions and Astrocytic Reaction in Neurodegenerative Diseases

AU - Dewitt, David A.

AU - Richey, P. L.

AU - Praprotnik, D.

AU - Silver, J.

AU - Perry, G.

PY - 1994/1/1

Y1 - 1994/1/1

N2 - Previously, we showed three differentially sulfated forms of chondroitin sulfate proteoglycans (CSPG) associated with senile plaques, astrocytes and neurofibrillary tangles in Alzheimer's disease. Here, monoclonal antibodies were used to demonstrate CSPGs in other neurodegenerative diseases. CSPGs were found associated with inclusions of Parkinson's, diffuse Lewy body, Pick's diseases, and progressive supranuclear palsy. Reacting astrocytes in each of these neurodegenrative diseases and Huntington's disease showed immunoreactivity for CSPG. CSPG distribution in a variety of neurodegenerative diseases suggests that similar mechanisms may be involved in the accumulation of proteoglycans in a number of filamentous inclusions.

AB - Previously, we showed three differentially sulfated forms of chondroitin sulfate proteoglycans (CSPG) associated with senile plaques, astrocytes and neurofibrillary tangles in Alzheimer's disease. Here, monoclonal antibodies were used to demonstrate CSPGs in other neurodegenerative diseases. CSPGs were found associated with inclusions of Parkinson's, diffuse Lewy body, Pick's diseases, and progressive supranuclear palsy. Reacting astrocytes in each of these neurodegenrative diseases and Huntington's disease showed immunoreactivity for CSPG. CSPG distribution in a variety of neurodegenerative diseases suggests that similar mechanisms may be involved in the accumulation of proteoglycans in a number of filamentous inclusions.

M3 - Article

JO - Faculty Publications and Presentations

JF - Faculty Publications and Presentations

ER -