Gelatinase A possesses a β-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease

Rex N. LePage; Amanda J. Fosang; Stephanie J. Fuller; Gillian Murphy; Genevieve Evin; Konrad Beyreuther; Colin L. Masters; David H. Small

doi:10.1016/0014-5793(95)01358-x

Gelatinase A possesses a β-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease

Rex N. LePage, Amanda J. Fosang, Stephanie J. Fuller, Gillian Murphy, Genevieve Evin, Konrad Beyreuther, Colin L. Masters, David H. Small

Research output: Contribution to journal › Article › peer-review

36 Citations (Scopus)

Abstract

The ability of the 72 kDa gelatinase A to cleave the amyloid protein precursor (APP) was investigated. HeLa cells were transfected with an APP₆₉₅ plasmid. The cells were incubated with gelatinase A, which cleaved the 110 kDa cell-surface APP, releasing a 100 kDa form of the protein. A peptide homologous to the β-secretase site was cleaved by gelatinase A adjacent to a glutamate residue at position -3 (βA4 numbering system). A peptide homologous to the alpha-secretase site was not cleaved. The results demonstrate that 72 kDa gelatinase A is not an alpha-secretase, but that it may have a β-secretase activity.

Original language	English
Pages (from-to)	267-70
Number of pages	4
Journal	FEBS Letters
Volume	377
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(95)01358-x
Publication status	Published - 1995
Externally published	Yes

Keywords

Alzheimer' disease
Amyloid
Gelatinase
Secretase
Protease

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10.1016/0014-5793(95)01358-x

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@article{b6054c60d18a49b8a9e42376705f02bb,

title = "Gelatinase A possesses a β-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease",

abstract = "The ability of the 72 kDa gelatinase A to cleave the amyloid protein precursor (APP) was investigated. HeLa cells were transfected with an APP695 plasmid. The cells were incubated with gelatinase A, which cleaved the 110 kDa cell-surface APP, releasing a 100 kDa form of the protein. A peptide homologous to the β-secretase site was cleaved by gelatinase A adjacent to a glutamate residue at position -3 (βA4 numbering system). A peptide homologous to the alpha-secretase site was not cleaved. The results demonstrate that 72 kDa gelatinase A is not an alpha-secretase, but that it may have a β-secretase activity.",

keywords = "Alzheimer' disease, Amyloid, Gelatinase, Secretase, Protease",

author = "LePage, {Rex N.} and Fosang, {Amanda J.} and Fuller, {Stephanie J.} and Gillian Murphy and Genevieve Evin and Konrad Beyreuther and Masters, {Colin L.} and Small, {David H.}",

year = "1995",

doi = "10.1016/0014-5793(95)01358-x",

language = "English",

volume = "377",

pages = "267--70",

journal = "FEBS Letters",

issn = "1873-3468",

publisher = "Elsevier",

number = "2",

}

Gelatinase A possesses a β-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease. / LePage, Rex N.; Fosang, Amanda J.; Fuller, Stephanie J.; Murphy, Gillian; Evin, Genevieve; Beyreuther, Konrad; Masters, Colin L.; Small, David H.

In: FEBS Letters, Vol. 377, No. 2, 1995, p. 267-70.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Gelatinase A possesses a β-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease

AU - LePage, Rex N.

AU - Fosang, Amanda J.

AU - Fuller, Stephanie J.

AU - Murphy, Gillian

AU - Evin, Genevieve

AU - Beyreuther, Konrad

AU - Masters, Colin L.

AU - Small, David H.

PY - 1995

Y1 - 1995

N2 - The ability of the 72 kDa gelatinase A to cleave the amyloid protein precursor (APP) was investigated. HeLa cells were transfected with an APP695 plasmid. The cells were incubated with gelatinase A, which cleaved the 110 kDa cell-surface APP, releasing a 100 kDa form of the protein. A peptide homologous to the β-secretase site was cleaved by gelatinase A adjacent to a glutamate residue at position -3 (βA4 numbering system). A peptide homologous to the alpha-secretase site was not cleaved. The results demonstrate that 72 kDa gelatinase A is not an alpha-secretase, but that it may have a β-secretase activity.

AB - The ability of the 72 kDa gelatinase A to cleave the amyloid protein precursor (APP) was investigated. HeLa cells were transfected with an APP695 plasmid. The cells were incubated with gelatinase A, which cleaved the 110 kDa cell-surface APP, releasing a 100 kDa form of the protein. A peptide homologous to the β-secretase site was cleaved by gelatinase A adjacent to a glutamate residue at position -3 (βA4 numbering system). A peptide homologous to the alpha-secretase site was not cleaved. The results demonstrate that 72 kDa gelatinase A is not an alpha-secretase, but that it may have a β-secretase activity.

KW - Alzheimer' disease

KW - Amyloid

KW - Gelatinase

KW - Secretase

KW - Protease

U2 - 10.1016/0014-5793(95)01358-x

DO - 10.1016/0014-5793(95)01358-x

M3 - Article

VL - 377

SP - 267

EP - 270

JO - FEBS Letters

JF - FEBS Letters

SN - 1873-3468

IS - 2

ER -

Gelatinase A possesses a β-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease

Abstract

Keywords

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