Mamma Mia, P-glycoprotein binds again.

Callaghan, R; Gelissen, IC; George, AM; Hartz, AMS

Mamma Mia, P-glycoprotein binds again.

Callaghan, R Gelissen, IC George, AM Hartz, AMS

Permalink

Publisher:: Wiley
Publication Type:: Journal Article
Citation:: FEBS letters, 2020, 594, pp. 4076-4084
Issue Date:: 2020-10-06

Closed Access

	Filename	Description	Size
	1873-3468.13951.pdf	Published version	598 kB	Adobe PDF	View/Open

Copyright Clearance Process

Recently Added
In Progress
Closed Access

This item is closed access and not available.

Full metadata record

Field	Value	Language
dc.contributor.author	Callaghan, R
dc.contributor.author	Gelissen, IC
dc.contributor.author	George, AM
dc.contributor.author	Hartz, AMS
dc.date.accessioned	2020-12-18T01:14:49Z
dc.date.available	2020-09-29
dc.date.available	2020-12-18T01:14:49Z
dc.date.issued	2020-10-06
dc.identifier.citation	FEBS letters, 2020, 594, pp. 4076-4084
dc.identifier.issn	0014-5793
dc.identifier.issn	1873-3468
dc.identifier.uri	http://hdl.handle.net/10453/144827
dc.description.abstract	The levels of amyloid peptides in the brain are regulated by a clearance pathway from neurons to the blood-brain barrier. The first step is thought to involve diffusion from the plasma membrane to the interstitium. However, amyloid peptides are hydrophobic and avidly intercalate within membranes. The ABC transporter P-glycoprotein is implicated in the clearance of amyloid peptides across the blood-brain, but its role at neurons is undetermined. We here propose that P-glycoprotein mediates 'exit' of amyloid peptides from neurons. Indeed, amyloid peptides have physicochemical similarities to substrates of P-glycoprotein, but their larger size represents a conundrum. This review probes the plausibility of a mechanism for amyloid peptide transport by P-glycoprotein exploiting evolving biochemical and structural models.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	Wiley
dc.relation.ispartof	FEBS letters
dc.relation.isbasedon	10.1002/1873-3468.13951
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	0304 Medicinal and Biomolecular Chemistry, 0601 Biochemistry and Cell Biology, 0603 Evolutionary Biology
dc.subject.classification	Biochemistry & Molecular Biology
dc.title	Mamma Mia, P-glycoprotein binds again.
dc.type	Journal Article
utslib.citation.volume	594
utslib.location.activity	England
utslib.for	0304 Medicinal and Biomolecular Chemistry
utslib.for	0601 Biochemistry and Cell Biology
utslib.for	0603 Evolutionary Biology
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney
utslib.copyright.status	closed_access	*
pubs.consider-herdc	false
dc.date.updated	2020-12-18T01:14:35Z
pubs.publication-status	Published
pubs.volume	594

Abstract:

The levels of amyloid peptides in the brain are regulated by a clearance pathway from neurons to the blood-brain barrier. The first step is thought to involve diffusion from the plasma membrane to the interstitium. However, amyloid peptides are hydrophobic and avidly intercalate within membranes. The ABC transporter P-glycoprotein is implicated in the clearance of amyloid peptides across the blood-brain, but its role at neurons is undetermined. We here propose that P-glycoprotein mediates 'exit' of amyloid peptides from neurons. Indeed, amyloid peptides have physicochemical similarities to substrates of P-glycoprotein, but their larger size represents a conundrum. This review probes the plausibility of a mechanism for amyloid peptide transport by P-glycoprotein exploiting evolving biochemical and structural models.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/144827