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, Jahrgang 392, Nr. 1, 04.2023, S. 215-234.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Review › Forschung
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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 -