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Analysis of the folding of proteolipid protein (PLP) at the endoplasmic reticulum; links to dysmyelination diseases

Reference	C12935
Principal Investigator / Supervisor	Professor Philip Woodman
Co-Investigators / Co-Supervisors	Professor Stephen High, Dr Eileithyia Swanton
Institution	The University of Manchester
Department	Life Sciences
Funding type	Research
Value (£)	196,140
Status	Completed
Type	Research Grant
Start date	07/08/2000
End date	06/01/2004
Duration	41 months

Abstract

Proteolipid protein (PLP) is a non-glycosylated, polytopic membrane protein which is the major molecular component of myelin. Mutations within the PLP gene that prevent the gene product from folding properly at the ER give rise to severe neurodegenerative diseases, such as Pelizaeus-Merzbacher (PMD) and X-linked spastic paraplegia (SPG-2). Specifically, misfolding of PLP may be the primary cause of the widespread oligodendrocyte apoptosis that is associated with PMD. The primary aim of this project is to identify the molecular components that assist in the folding of PLP at the ER and to understand how misfolded PLP is processed by the ER quality control machinery. Based on these studies, we also intend to investigate how misfolding of PLP leads to activation of an apoptotic signalling pathway.

Summary

unavailable

Committee	Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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