Soluble derivatives of the β amyloid protein precursor of Alzheimer's disease are labeled by antisera to the β amyloid protein

Mark R. Palmert; Sandra L. Siedlak; Marcia Berman Podlisny; Barry Greenberg; Earl R. Shelton; Hardy W. Chan; Marianne Usiak; Dennis J. Selkbe; George Perry; Steven G. Younkin

doi:10.1016/0006-291X(89)91052-8

Soluble derivatives of the β amyloid protein precursor of Alzheimer's disease are labeled by antisera to the β amyloid protein

Mark R. Palmert, Sandra L. Siedlak, Marcia Berman Podlisny, Barry Greenberg, Earl R. Shelton, Hardy W. Chan, Marianne Usiak, Dennis J. Selkbe, George Perry, Steven G. Younkin

Neuroscience

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63 Scopus citations

Abstract

The amyloid deposited in Alzheimer's disease (AD) is composed primarily of a 39-42 residue polypeptide (βAP) that is derived from a larger β amyloid protein precursor (βAPP). In previous studies, we and others identified full-length, membrane-associated forms of the βAPP and showed that these forms are processed into soluble derivatives that lack the carboxyl-terminus of the full-length forms. In this report, we demonstrate that the soluble ∼125 and ∼105 kDa forms of the βAPP found in human cerebrospinal fluid are specifically labeled by several different antisera to the βAP. This finding indicates that both soluble derivatives contain all or part of the βAP sequence, and it suggests that one or both of these forms may be the immediate precursor of the amyloid deposited in AD.

Original language	English (US)
Pages (from-to)	182-188
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	165
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(89)91052-8
State	Published - Nov 30 1989

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(89)91052-8

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Palmert, M. R., Siedlak, S. L., Podlisny, M. B., Greenberg, B., Shelton, E. R., Chan, H. W., Usiak, M., Selkbe, D. J., Perry, G., & Younkin, S. G. (1989). Soluble derivatives of the β amyloid protein precursor of Alzheimer's disease are labeled by antisera to the β amyloid protein. Biochemical and Biophysical Research Communications, 165(1), 182-188. https://doi.org/10.1016/0006-291X(89)91052-8

Palmert, MR, Siedlak, SL, Podlisny, MB, Greenberg, B, Shelton, ER, Chan, HW, Usiak, M, Selkbe, DJ, Perry, G & Younkin, SG 1989, 'Soluble derivatives of the β amyloid protein precursor of Alzheimer's disease are labeled by antisera to the β amyloid protein', Biochemical and Biophysical Research Communications, vol. 165, no. 1, pp. 182-188. https://doi.org/10.1016/0006-291X(89)91052-8

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title = "Soluble derivatives of the β amyloid protein precursor of Alzheimer's disease are labeled by antisera to the β amyloid protein",

abstract = "The amyloid deposited in Alzheimer's disease (AD) is composed primarily of a 39-42 residue polypeptide (βAP) that is derived from a larger β amyloid protein precursor (βAPP). In previous studies, we and others identified full-length, membrane-associated forms of the βAPP and showed that these forms are processed into soluble derivatives that lack the carboxyl-terminus of the full-length forms. In this report, we demonstrate that the soluble ∼125 and ∼105 kDa forms of the βAPP found in human cerebrospinal fluid are specifically labeled by several different antisera to the βAP. This finding indicates that both soluble derivatives contain all or part of the βAP sequence, and it suggests that one or both of these forms may be the immediate precursor of the amyloid deposited in AD.",

author = "Palmert, {Mark R.} and Siedlak, {Sandra L.} and Podlisny, {Marcia Berman} and Barry Greenberg and Shelton, {Earl R.} and Chan, {Hardy W.} and Marianne Usiak and Selkbe, {Dennis J.} and George Perry and Younkin, {Steven G.}",

note = "Funding Information: ACKNOWLEDGMENTS. We thank Satish Sharma and Jim Cornette of the Upjohn Company for antibody preparation and Linda Maggiora and Tom Lobl of the Upjohn Company for peptide synthesis and purification. We would also like to thank George Glenner and DuPont for providing the anti-OAPt-10 antiserum. Supported by USPHS grants AGO6656 (SGY), MH43444 (SGY),5T32GM0250 (MRP), K04-AGO0415 (GP), AGO7775 (GP), AGO791 1 (LEAD award, DJS), and grants from the the American Health Assistance Foundation (GP) and the State of Ohio (GPSGY).",

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AU - Palmert, Mark R.

AU - Siedlak, Sandra L.

AU - Podlisny, Marcia Berman

AU - Greenberg, Barry

AU - Shelton, Earl R.

AU - Chan, Hardy W.

AU - Usiak, Marianne

AU - Selkbe, Dennis J.

AU - Perry, George

AU - Younkin, Steven G.

N1 - Funding Information: ACKNOWLEDGMENTS. We thank Satish Sharma and Jim Cornette of the Upjohn Company for antibody preparation and Linda Maggiora and Tom Lobl of the Upjohn Company for peptide synthesis and purification. We would also like to thank George Glenner and DuPont for providing the anti-OAPt-10 antiserum. Supported by USPHS grants AGO6656 (SGY), MH43444 (SGY),5T32GM0250 (MRP), K04-AGO0415 (GP), AGO7775 (GP), AGO791 1 (LEAD award, DJS), and grants from the the American Health Assistance Foundation (GP) and the State of Ohio (GPSGY).

PY - 1989/11/30

Y1 - 1989/11/30

N2 - The amyloid deposited in Alzheimer's disease (AD) is composed primarily of a 39-42 residue polypeptide (βAP) that is derived from a larger β amyloid protein precursor (βAPP). In previous studies, we and others identified full-length, membrane-associated forms of the βAPP and showed that these forms are processed into soluble derivatives that lack the carboxyl-terminus of the full-length forms. In this report, we demonstrate that the soluble ∼125 and ∼105 kDa forms of the βAPP found in human cerebrospinal fluid are specifically labeled by several different antisera to the βAP. This finding indicates that both soluble derivatives contain all or part of the βAP sequence, and it suggests that one or both of these forms may be the immediate precursor of the amyloid deposited in AD.

AB - The amyloid deposited in Alzheimer's disease (AD) is composed primarily of a 39-42 residue polypeptide (βAP) that is derived from a larger β amyloid protein precursor (βAPP). In previous studies, we and others identified full-length, membrane-associated forms of the βAPP and showed that these forms are processed into soluble derivatives that lack the carboxyl-terminus of the full-length forms. In this report, we demonstrate that the soluble ∼125 and ∼105 kDa forms of the βAPP found in human cerebrospinal fluid are specifically labeled by several different antisera to the βAP. This finding indicates that both soluble derivatives contain all or part of the βAP sequence, and it suggests that one or both of these forms may be the immediate precursor of the amyloid deposited in AD.

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Soluble derivatives of the β amyloid protein precursor of Alzheimer's disease are labeled by antisera to the β amyloid protein

Abstract

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