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Secretory form of Alzheimer amyloid precursor protein 695 in human brain lacks β/A4 amyloid immunoreactivity

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Secretory form of Alzheimer amyloid precursor protein 695 in human brain lacks β/A4 amyloid immunoreactivity. / Kametani, F; Tanaka, K; Ishii, T et al.
In: Biochemical and Biophysical Research Communications, Vol. 191, No. 2, 15.03.1993, p. 392-398.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Kametani, F, Tanaka, K, Ishii, T, Ikeda, S, Kennedy, HE & Allsop, D 1993, 'Secretory form of Alzheimer amyloid precursor protein 695 in human brain lacks β/A4 amyloid immunoreactivity', Biochemical and Biophysical Research Communications, vol. 191, no. 2, pp. 392-398. https://doi.org/10.1006/bbrc.1993.1230

APA

Kametani, F., Tanaka, K., Ishii, T., Ikeda, S., Kennedy, H. E., & Allsop, D. (1993). Secretory form of Alzheimer amyloid precursor protein 695 in human brain lacks β/A4 amyloid immunoreactivity. Biochemical and Biophysical Research Communications, 191(2), 392-398. https://doi.org/10.1006/bbrc.1993.1230

Vancouver

Kametani F, Tanaka K, Ishii T, Ikeda S, Kennedy HE, Allsop D. Secretory form of Alzheimer amyloid precursor protein 695 in human brain lacks β/A4 amyloid immunoreactivity. Biochemical and Biophysical Research Communications. 1993 Mar 15;191(2):392-398. doi: 10.1006/bbrc.1993.1230

Author

Kametani, F ; Tanaka, K ; Ishii, T et al. / Secretory form of Alzheimer amyloid precursor protein 695 in human brain lacks β/A4 amyloid immunoreactivity. In: Biochemical and Biophysical Research Communications. 1993 ; Vol. 191, No. 2. pp. 392-398.

Bibtex

@article{d06e1852f3044584912faa3e3c1537d0,
title = "Secretory form of Alzheimer amyloid precursor protein 695 in human brain lacks β/A4 amyloid immunoreactivity",
abstract = "It is not clear how Alzheimer amyloid precursor proteins (APP) are metabolized in the brain itself. Secretory forms of APP in a phosphate buffer-soluble fraction were purified from post-mortem human brain by heparin-affinity and ion-exchange chromatography and analyzed by N-terminal amino acid sequencing and SDS polyacrylamide gel electrophoresis/immunoblotting. We found apparently similar multi-isoforms of secretory APP (at 93-97, 105-112 and 123 KDa) to those that we have described recently in cerebrospinal fluid. Antisera to the initial part of the beta/A4 sequence labelled only those bands that were found to react with antiserum to the Kunitz-type inhibitor insert of APP, suggesting that beta/A4 amyloid may be generated specifically from APP-695.",
keywords = "Adult, Aged, Alzheimer Disease, Amino Acid Sequence, Amyloid, Amyloid beta-Protein Precursor, Brain, Down Syndrome, Female, Humans, Male, Middle Aged, Molecular Sequence Data",
author = "F Kametani and K Tanaka and T Ishii and S Ikeda and Kennedy, {H E} and D Allsop",
year = "1993",
month = mar,
day = "15",
doi = "10.1006/bbrc.1993.1230",
language = "English",
volume = "191",
pages = "392--398",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - Secretory form of Alzheimer amyloid precursor protein 695 in human brain lacks β/A4 amyloid immunoreactivity

AU - Kametani, F

AU - Tanaka, K

AU - Ishii, T

AU - Ikeda, S

AU - Kennedy, H E

AU - Allsop, D

PY - 1993/3/15

Y1 - 1993/3/15

N2 - It is not clear how Alzheimer amyloid precursor proteins (APP) are metabolized in the brain itself. Secretory forms of APP in a phosphate buffer-soluble fraction were purified from post-mortem human brain by heparin-affinity and ion-exchange chromatography and analyzed by N-terminal amino acid sequencing and SDS polyacrylamide gel electrophoresis/immunoblotting. We found apparently similar multi-isoforms of secretory APP (at 93-97, 105-112 and 123 KDa) to those that we have described recently in cerebrospinal fluid. Antisera to the initial part of the beta/A4 sequence labelled only those bands that were found to react with antiserum to the Kunitz-type inhibitor insert of APP, suggesting that beta/A4 amyloid may be generated specifically from APP-695.

AB - It is not clear how Alzheimer amyloid precursor proteins (APP) are metabolized in the brain itself. Secretory forms of APP in a phosphate buffer-soluble fraction were purified from post-mortem human brain by heparin-affinity and ion-exchange chromatography and analyzed by N-terminal amino acid sequencing and SDS polyacrylamide gel electrophoresis/immunoblotting. We found apparently similar multi-isoforms of secretory APP (at 93-97, 105-112 and 123 KDa) to those that we have described recently in cerebrospinal fluid. Antisera to the initial part of the beta/A4 sequence labelled only those bands that were found to react with antiserum to the Kunitz-type inhibitor insert of APP, suggesting that beta/A4 amyloid may be generated specifically from APP-695.

KW - Adult

KW - Aged

KW - Alzheimer Disease

KW - Amino Acid Sequence

KW - Amyloid

KW - Amyloid beta-Protein Precursor

KW - Brain

KW - Down Syndrome

KW - Female

KW - Humans

KW - Male

KW - Middle Aged

KW - Molecular Sequence Data

U2 - 10.1006/bbrc.1993.1230

DO - 10.1006/bbrc.1993.1230

M3 - Journal article

C2 - 8460999

VL - 191

SP - 392

EP - 398

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -