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ADAMs family members as amyloid precursor protein -secretases.

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ADAMs family members as amyloid precursor protein -secretases. / Allinson, Tobias M. J.; Parkin, Edward T.; Turner, Anthony J. et al.
In: Journal of Neuroscience Research, Vol. 74, No. 3, 01.11.2003, p. 342-352.

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

Harvard

Allinson, TMJ, Parkin, ET, Turner, AJ & Hooper, NM 2003, 'ADAMs family members as amyloid precursor protein -secretases.', Journal of Neuroscience Research, vol. 74, no. 3, pp. 342-352. https://doi.org/10.1002/jnr.10737

APA

Allinson, T. M. J., Parkin, E. T., Turner, A. J., & Hooper, N. M. (2003). ADAMs family members as amyloid precursor protein -secretases. Journal of Neuroscience Research, 74(3), 342-352. https://doi.org/10.1002/jnr.10737

Vancouver

Allinson TMJ, Parkin ET, Turner AJ, Hooper NM. ADAMs family members as amyloid precursor protein -secretases. Journal of Neuroscience Research. 2003 Nov 1;74(3):342-352. doi: 10.1002/jnr.10737

Author

Allinson, Tobias M. J. ; Parkin, Edward T. ; Turner, Anthony J. et al. / ADAMs family members as amyloid precursor protein -secretases. In: Journal of Neuroscience Research. 2003 ; Vol. 74, No. 3. pp. 342-352.

Bibtex

@article{b9382081d68645ff91621bbaeae3a480,
title = "ADAMs family members as amyloid precursor protein -secretases.",
abstract = "In the non-amyloidogenic pathway, the Alzheimer's amyloid precursor protein (APP) is cleaved within the amyloid- domain by -secretase precluding deposition of intact amyloid- peptide. The large ectodomain released from the cell surface by the action of -secretase has several neuroprotective properties. Studies with protease inhibitors have shown that -secretase is a zinc metalloproteinase, and several members of the adamalysin family of proteins, tumour necrosis factor- convertase (TACE, ADAM17), ADAM10, and ADAM9, all fulfil some of the criteria required of -secretase. We review the evidence for each of these ADAMs acting as the -secretase. What seems to be emerging from numerous studies, including those with mice in which each of the ADAMs has been knocked out, is that there is a team of zinc metalloproteinases able to cleave APP at the -secretase site. We also discuss how upregulation of -secretase activity by muscarinic agonists, cholesterol-lowering drugs, steroid hormones, non-steroidal anti-inflammatory drugs, and metal ions may explain some of the therapeutic actions of these agents in Alzheimer's disease.",
keywords = "ADAMs • -secretase • cholesterol • non-amyloidogenic • zinc metalloproteinase",
author = "Allinson, {Tobias M. J.} and Parkin, {Edward T.} and Turner, {Anthony J.} and Hooper, {Nigel M.}",
year = "2003",
month = nov,
day = "1",
doi = "10.1002/jnr.10737",
language = "English",
volume = "74",
pages = "342--352",
journal = "Journal of Neuroscience Research",
issn = "0360-4012",
publisher = "Wiley-Liss Inc.",
number = "3",

}

RIS

TY - JOUR

T1 - ADAMs family members as amyloid precursor protein -secretases.

AU - Allinson, Tobias M. J.

AU - Parkin, Edward T.

AU - Turner, Anthony J.

AU - Hooper, Nigel M.

PY - 2003/11/1

Y1 - 2003/11/1

N2 - In the non-amyloidogenic pathway, the Alzheimer's amyloid precursor protein (APP) is cleaved within the amyloid- domain by -secretase precluding deposition of intact amyloid- peptide. The large ectodomain released from the cell surface by the action of -secretase has several neuroprotective properties. Studies with protease inhibitors have shown that -secretase is a zinc metalloproteinase, and several members of the adamalysin family of proteins, tumour necrosis factor- convertase (TACE, ADAM17), ADAM10, and ADAM9, all fulfil some of the criteria required of -secretase. We review the evidence for each of these ADAMs acting as the -secretase. What seems to be emerging from numerous studies, including those with mice in which each of the ADAMs has been knocked out, is that there is a team of zinc metalloproteinases able to cleave APP at the -secretase site. We also discuss how upregulation of -secretase activity by muscarinic agonists, cholesterol-lowering drugs, steroid hormones, non-steroidal anti-inflammatory drugs, and metal ions may explain some of the therapeutic actions of these agents in Alzheimer's disease.

AB - In the non-amyloidogenic pathway, the Alzheimer's amyloid precursor protein (APP) is cleaved within the amyloid- domain by -secretase precluding deposition of intact amyloid- peptide. The large ectodomain released from the cell surface by the action of -secretase has several neuroprotective properties. Studies with protease inhibitors have shown that -secretase is a zinc metalloproteinase, and several members of the adamalysin family of proteins, tumour necrosis factor- convertase (TACE, ADAM17), ADAM10, and ADAM9, all fulfil some of the criteria required of -secretase. We review the evidence for each of these ADAMs acting as the -secretase. What seems to be emerging from numerous studies, including those with mice in which each of the ADAMs has been knocked out, is that there is a team of zinc metalloproteinases able to cleave APP at the -secretase site. We also discuss how upregulation of -secretase activity by muscarinic agonists, cholesterol-lowering drugs, steroid hormones, non-steroidal anti-inflammatory drugs, and metal ions may explain some of the therapeutic actions of these agents in Alzheimer's disease.

KW - ADAMs • -secretase • cholesterol • non-amyloidogenic • zinc metalloproteinase

U2 - 10.1002/jnr.10737

DO - 10.1002/jnr.10737

M3 - Journal article

VL - 74

SP - 342

EP - 352

JO - Journal of Neuroscience Research

JF - Journal of Neuroscience Research

SN - 0360-4012

IS - 3

ER -