Association of heparan sulfate proteoglycan with the neurofibrillary tangles of Alzheimer's disease

G. Perry; S. L. Siedlak; P. Richey; M. Kawai; P. Cras; R. N. Kalaria; P. G. Galloway; J. M. Scardina; B. Cordell; B. D. Greenberg; S. R. Ledbetter; P. Gambetti

doi:10.1523/jneurosci.11-11-03679.1991

Association of heparan sulfate proteoglycan with the neurofibrillary tangles of Alzheimer's disease

G. Perry, S. L. Siedlak, P. Richey, M. Kawai, P. Cras, R. N. Kalaria, P. G. Galloway, J. M. Scardina, B. Cordell, B. D. Greenberg, S. R. Ledbetter, P. Gambetti

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Abstract

The major intracytoplasmic lesion of Alzheimer's disease is the neurofibrillary tangle (NFT), which is primarily composed of paired helical filaments (PHFs). The mechanism responsible for the formation of PHFs, as well as their insolubility and apparent heterogeneity, is unknown. We found that basic fibroblast growth factor (bFGF) binds to heparinase-sensitive sites in NFTs. bFGF binding is due to a heparan sulfate proteoglycan (HSPG) immunocytochemically identified in NFTs. In the presence of polycations (e.g., Ca²⁺), HSPG will bind to free carboxyl groups in NFT proteins. HSPG binding may play a role in transforming normal soluble proteins into insoluble PHFs.

Original language	English (US)
Pages (from-to)	3679-3683
Number of pages	5
Journal	Journal of Neuroscience
Volume	11
Issue number	11
DOIs	https://doi.org/10.1523/jneurosci.11-11-03679.1991
State	Published - 1991
Externally published	Yes

ASJC Scopus subject areas

General Neuroscience

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10.1523/jneurosci.11-11-03679.1991

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Perry, G., Siedlak, S. L., Richey, P., Kawai, M., Cras, P., Kalaria, R. N., Galloway, P. G., Scardina, J. M., Cordell, B., Greenberg, B. D., Ledbetter, S. R., & Gambetti, P. (1991). Association of heparan sulfate proteoglycan with the neurofibrillary tangles of Alzheimer's disease. Journal of Neuroscience, 11(11), 3679-3683. https://doi.org/10.1523/jneurosci.11-11-03679.1991

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title = "Association of heparan sulfate proteoglycan with the neurofibrillary tangles of Alzheimer's disease",

abstract = "The major intracytoplasmic lesion of Alzheimer's disease is the neurofibrillary tangle (NFT), which is primarily composed of paired helical filaments (PHFs). The mechanism responsible for the formation of PHFs, as well as their insolubility and apparent heterogeneity, is unknown. We found that basic fibroblast growth factor (bFGF) binds to heparinase-sensitive sites in NFTs. bFGF binding is due to a heparan sulfate proteoglycan (HSPG) immunocytochemically identified in NFTs. In the presence of polycations (e.g., Ca2+), HSPG will bind to free carboxyl groups in NFT proteins. HSPG binding may play a role in transforming normal soluble proteins into insoluble PHFs.",

author = "G. Perry and Siedlak, {S. L.} and P. Richey and M. Kawai and P. Cras and Kalaria, {R. N.} and Galloway, {P. G.} and Scardina, {J. M.} and B. Cordell and Greenberg, {B. D.} and Ledbetter, {S. R.} and P. Gambetti",

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doi = "10.1523/jneurosci.11-11-03679.1991",

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T1 - Association of heparan sulfate proteoglycan with the neurofibrillary tangles of Alzheimer's disease

AU - Perry, G.

AU - Siedlak, S. L.

AU - Richey, P.

AU - Kawai, M.

AU - Cras, P.

AU - Kalaria, R. N.

AU - Galloway, P. G.

AU - Scardina, J. M.

AU - Cordell, B.

AU - Greenberg, B. D.

AU - Ledbetter, S. R.

AU - Gambetti, P.

PY - 1991

Y1 - 1991

N2 - The major intracytoplasmic lesion of Alzheimer's disease is the neurofibrillary tangle (NFT), which is primarily composed of paired helical filaments (PHFs). The mechanism responsible for the formation of PHFs, as well as their insolubility and apparent heterogeneity, is unknown. We found that basic fibroblast growth factor (bFGF) binds to heparinase-sensitive sites in NFTs. bFGF binding is due to a heparan sulfate proteoglycan (HSPG) immunocytochemically identified in NFTs. In the presence of polycations (e.g., Ca2+), HSPG will bind to free carboxyl groups in NFT proteins. HSPG binding may play a role in transforming normal soluble proteins into insoluble PHFs.

AB - The major intracytoplasmic lesion of Alzheimer's disease is the neurofibrillary tangle (NFT), which is primarily composed of paired helical filaments (PHFs). The mechanism responsible for the formation of PHFs, as well as their insolubility and apparent heterogeneity, is unknown. We found that basic fibroblast growth factor (bFGF) binds to heparinase-sensitive sites in NFTs. bFGF binding is due to a heparan sulfate proteoglycan (HSPG) immunocytochemically identified in NFTs. In the presence of polycations (e.g., Ca2+), HSPG will bind to free carboxyl groups in NFT proteins. HSPG binding may play a role in transforming normal soluble proteins into insoluble PHFs.

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Association of heparan sulfate proteoglycan with the neurofibrillary tangles of Alzheimer's disease

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