Anchorless risk or released benefit?

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Anchorless risk or released benefit? An updated view on the ADAM10-mediated shedding of the prion protein. / Mohammadi, Behnam; Song, Feizhi; Matamoros-Angles, Andreu; Shafiq, Mohsin; Damme, Markus; Puig, Berta; Glatzel, Markus; Altmeppen, Hermann Clemens.

In: CELL TISSUE RES, Vol. 392, No. 1, 04.2023, p. 215-234.

Research output: SCORING: Contribution to journalSCORING: Review articleResearch

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@article{58c66f7fd7544d0885b2ccd88585ee12,
title = "Anchorless risk or released benefit?: An updated view on the ADAM10-mediated shedding of the prion protein",
abstract = "The prion protein (PrP) is a broadly expressed glycoprotein linked with a multitude of (suggested) biological and pathological implications. Some of these roles seem to be due to constitutively generated proteolytic fragments of the protein. Among them is a soluble PrP form, which is released from the surface of neurons and other cell types by action of the metalloprotease ADAM10 in a process termed 'shedding'. The latter aspect is the focus of this review, which aims to provide a comprehensive overview on (i) the relevance of proteolytic processing in regulating cellular PrP functions, (ii) currently described involvement of shed PrP in neurodegenerative diseases (including prion diseases and Alzheimer's disease), (iii) shed PrP's expected roles in intercellular communication in many more (patho)physiological conditions (such as stroke, cancer or immune responses), (iv) and the need for improved research tools in respective (future) studies. Deeper mechanistic insight into roles played by PrP shedding and its resulting fragment may pave the way for improved diagnostics and future therapeutic approaches in diseases of the brain and beyond.",
author = "Behnam Mohammadi and Feizhi Song and Andreu Matamoros-Angles and Mohsin Shafiq and Markus Damme and Berta Puig and Markus Glatzel and Altmeppen, {Hermann Clemens}",
note = "{\textcopyright} 2022. The Author(s).",
year = "2023",
month = apr,
doi = "10.1007/s00441-022-03582-4",
language = "English",
volume = "392",
pages = "215--234",
journal = "CELL TISSUE RES",
issn = "0302-766X",
publisher = "Springer",
number = "1",

}

RIS

TY - JOUR

T1 - Anchorless risk or released benefit?

T2 - An updated view on the ADAM10-mediated shedding of the prion protein

AU - Mohammadi, Behnam

AU - Song, Feizhi

AU - Matamoros-Angles, Andreu

AU - Shafiq, Mohsin

AU - Damme, Markus

AU - Puig, Berta

AU - Glatzel, Markus

AU - Altmeppen, Hermann Clemens

N1 - © 2022. The Author(s).

PY - 2023/4

Y1 - 2023/4

N2 - The prion protein (PrP) is a broadly expressed glycoprotein linked with a multitude of (suggested) biological and pathological implications. Some of these roles seem to be due to constitutively generated proteolytic fragments of the protein. Among them is a soluble PrP form, which is released from the surface of neurons and other cell types by action of the metalloprotease ADAM10 in a process termed 'shedding'. The latter aspect is the focus of this review, which aims to provide a comprehensive overview on (i) the relevance of proteolytic processing in regulating cellular PrP functions, (ii) currently described involvement of shed PrP in neurodegenerative diseases (including prion diseases and Alzheimer's disease), (iii) shed PrP's expected roles in intercellular communication in many more (patho)physiological conditions (such as stroke, cancer or immune responses), (iv) and the need for improved research tools in respective (future) studies. Deeper mechanistic insight into roles played by PrP shedding and its resulting fragment may pave the way for improved diagnostics and future therapeutic approaches in diseases of the brain and beyond.

AB - The prion protein (PrP) is a broadly expressed glycoprotein linked with a multitude of (suggested) biological and pathological implications. Some of these roles seem to be due to constitutively generated proteolytic fragments of the protein. Among them is a soluble PrP form, which is released from the surface of neurons and other cell types by action of the metalloprotease ADAM10 in a process termed 'shedding'. The latter aspect is the focus of this review, which aims to provide a comprehensive overview on (i) the relevance of proteolytic processing in regulating cellular PrP functions, (ii) currently described involvement of shed PrP in neurodegenerative diseases (including prion diseases and Alzheimer's disease), (iii) shed PrP's expected roles in intercellular communication in many more (patho)physiological conditions (such as stroke, cancer or immune responses), (iv) and the need for improved research tools in respective (future) studies. Deeper mechanistic insight into roles played by PrP shedding and its resulting fragment may pave the way for improved diagnostics and future therapeutic approaches in diseases of the brain and beyond.

U2 - 10.1007/s00441-022-03582-4

DO - 10.1007/s00441-022-03582-4

M3 - SCORING: Review article

C2 - 35084572

VL - 392

SP - 215

EP - 234

JO - CELL TISSUE RES

JF - CELL TISSUE RES

SN - 0302-766X

IS - 1

ER -