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Title: Structure-function relationships of the retinol-binding protein receptor, STRA6
Author: Brown, Lindsay Anne
ISNI:       0000 0004 2718 1913
Awarding Body: University of Leeds
Current Institution: University of Leeds
Date of Award: 2011
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Retinol (Vitamin A) and its derivatives are essential in a wide range of biological processes, from embryonic growth and development, to the correct functioning of the adult brain, spanning almost all vertebrate organ systems. Retinol transport in plasma is facilitated by retinol-binding protein (REP), which binds retinol with high affinity for transport to target tissues. Evidence supporting the existence of a specific, cell-surface receptor for REP that mediates cellular uptake of retinol, has accumulated over more than three decades, culminating in the recent identification of multi- transmembrane domain protein, STRA6, as the elusive REP receptor, thus ending the controversy surrounding its very existence. Of previously unknown function, STRA6 lacks sequence homology to any protein in the human genome, and thus represents a unique type of cell-surface receptor. Given the diverse and potent biological activity of retinol and its derivatives, expression of STRA6 is widespread in both embryonic development and adult organ systems, with marked expression in blood- organ barriers including the eye and placenta. Consistent with this ubiquitous expression and the requirement for tight regulation of retinol uptake, severe multi system pathological phenotypes can be attributed to mutations in the human receptor.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available