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Effects Of Glycosylation On The Structure And Function Of The Extracellular Chaperone Clusterin, Elise Stewart, Andrew Aquilina, Simon B Easterbrook-Smith, D Murphy-Durland, C Jacobsen, S Moestrup, Mark Wilson

J. A. Aquilina

Clusterin is the first well characterized, constitutively secreted extracellular chaperone that binds to exposed regions of hydrophobicity on non-native proteins. It may help control the folding state of extracellular proteins by targeting them for receptor-mediated endocytosis and intracellular lysosomal degradation. A notable feature of secreted clusterin is its heavy glycosylation. Although carbohydrate comprises approximately 20−25% of the total mass of the mature molecule, its function is unknown. Results from the current study demonstrate that deglycosylation of human serum clusterin had little effect on its overall secondary structure content but produced a small increase in solvent-exposed hydrophobicity and enhanced the propensity …