Alzheimer amyloid β/A4 peptide binding sites and a possible 'APP-secretase' activity associated with rat brain cortical membranes

Biomedical and Life Sciences

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https://doi.org/10.1016/0006-8993(91)90905-B
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Keywords

Alzheimer Disease, Amyloid beta-Peptides, Animals, Binding Sites, Cerebral Cortex, Chromatography, High Pressure Liquid, Drug Stability, Ligands, Male, Membranes, Peptides, Rats, Rats, Inbred Strains

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Alzheimer amyloid β/A4 peptide binding sites and a possible 'APP-secretase' activity associated with rat brain cortical membranes. / Allsop, D; Yamamoto, T; Kametani, F et al.
In: Brain Research, Vol. 551, No. 1-2, 14.06.1991, p. 1-9.

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

Bibtex

@article{fdf676d841544fa59add236d1f859aec,

title = "Alzheimer amyloid β/A4 peptide binding sites and a possible 'APP-secretase' activity associated with rat brain cortical membranes",

abstract = "We carried out ligand binding experiments on membranes from rat brain cortical grey matter using radioiodinated beta/A4 8-17, with non-specific binding determined by the addition of 10 microM unlabelled peptide. Specific, reversible binding amounted to 60-75% of total binding and showed a clear dependence on time, temperature, pH and membrane concentration. Kinetic analyses indicated a high-affinity binding site with an apparent KD of 440 pM. However, the ligand was partly degraded with loss of the Ser8, Lys16 and Leu17 residues. Excision of the two C-terminal amino acids was inhibited by EDTA, EGTA, dithiothreitol or Zn2+ but was stimulated by Ca2+ or Mn2+. These studies demonstrate high-affinity binding sites for beta/A4 8-17 (or its derivatives) in rat brain, suggesting that this region may contain a physiologically important amino acid sequence and identify a potential membrane-associated amyloid precursor protein (APP) secretase activity.",

keywords = "Alzheimer Disease, Amyloid beta-Peptides, Animals, Binding Sites, Cerebral Cortex, Chromatography, High Pressure Liquid, Drug Stability, Ligands, Male, Membranes, Peptides, Rats, Rats, Inbred Strains",

author = "D Allsop and T Yamamoto and F Kametani and N Miyazaki and T Ishii",

year = "1991",

month = jun,

day = "14",

doi = "10.1016/0006-8993(91)90905-B",

language = "English",

volume = "551",

pages = "1--9",

journal = "Brain Research",

issn = "0006-8993",

publisher = "Elsevier",

number = "1-2",

}

RIS

TY - JOUR

T1 - Alzheimer amyloid β/A4 peptide binding sites and a possible 'APP-secretase' activity associated with rat brain cortical membranes

AU - Allsop, D

AU - Yamamoto, T

AU - Kametani, F

AU - Miyazaki, N

AU - Ishii, T

PY - 1991/6/14

Y1 - 1991/6/14

N2 - We carried out ligand binding experiments on membranes from rat brain cortical grey matter using radioiodinated beta/A4 8-17, with non-specific binding determined by the addition of 10 microM unlabelled peptide. Specific, reversible binding amounted to 60-75% of total binding and showed a clear dependence on time, temperature, pH and membrane concentration. Kinetic analyses indicated a high-affinity binding site with an apparent KD of 440 pM. However, the ligand was partly degraded with loss of the Ser8, Lys16 and Leu17 residues. Excision of the two C-terminal amino acids was inhibited by EDTA, EGTA, dithiothreitol or Zn2+ but was stimulated by Ca2+ or Mn2+. These studies demonstrate high-affinity binding sites for beta/A4 8-17 (or its derivatives) in rat brain, suggesting that this region may contain a physiologically important amino acid sequence and identify a potential membrane-associated amyloid precursor protein (APP) secretase activity.

AB - We carried out ligand binding experiments on membranes from rat brain cortical grey matter using radioiodinated beta/A4 8-17, with non-specific binding determined by the addition of 10 microM unlabelled peptide. Specific, reversible binding amounted to 60-75% of total binding and showed a clear dependence on time, temperature, pH and membrane concentration. Kinetic analyses indicated a high-affinity binding site with an apparent KD of 440 pM. However, the ligand was partly degraded with loss of the Ser8, Lys16 and Leu17 residues. Excision of the two C-terminal amino acids was inhibited by EDTA, EGTA, dithiothreitol or Zn2+ but was stimulated by Ca2+ or Mn2+. These studies demonstrate high-affinity binding sites for beta/A4 8-17 (or its derivatives) in rat brain, suggesting that this region may contain a physiologically important amino acid sequence and identify a potential membrane-associated amyloid precursor protein (APP) secretase activity.

KW - Alzheimer Disease

KW - Amyloid beta-Peptides

KW - Animals

KW - Binding Sites

KW - Cerebral Cortex

KW - Chromatography, High Pressure Liquid

KW - Drug Stability

KW - Ligands

KW - Male

KW - Membranes

KW - Peptides

KW - Rats

KW - Rats, Inbred Strains

U2 - 10.1016/0006-8993(91)90905-B

DO - 10.1016/0006-8993(91)90905-B

M3 - Journal article

C2 - 1913140

VL - 551

SP - 1

EP - 9

JO - Brain Research

JF - Brain Research

SN - 0006-8993

IS - 1-2

ER -

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