Native mass spectrometry and surface induced dissociation provide insight into the post-translational modifications of tetrameric AQP0 isolated from bovine eye lens

SR Harvey, C O'Neale, KL Schey… - Analytical …, 2022 - ACS Publications
Aquaporin-0 (AQP0) is a tetrameric membrane protein and the most abundant membrane
protein in the eye lens. Interestingly, there is little to no cellular turnover once mature lens …

Spatial analysis of human lens aquaporin-0 post-translational modifications by MALDI mass spectrometry tissue profiling

DB Gutierrez, D Garland, KL Schey - Experimental Eye Research, 2011 - Elsevier
Aquaporin-0 (AQP0), the major integral membrane protein in lens fiber cells, becomes
highly modified with increasing age. The functional consequences of these modifications are …

[HTML][HTML] MALDI imaging mass spectrometry spatially maps age-related deamidation and truncation of human lens aquaporin-0

JL Wenke, KL Rose, JM Spraggins… - … ophthalmology & visual …, 2015 - jov.arvojournals.org
Purpose: To spatially map human lens Aquaporin-0 (AQP0) protein modifications, including
lipidation, truncation, and deamidation, from birth through middle age using matrix-assisted …

Post-translational modifications of aquaporin 0 (AQP0) in the normal human lens: spatial and temporal occurrence

LE Ball, DL Garland, RK Crouch, KL Schey - Biochemistry, 2004 - ACS Publications
Because of the lack of protein turnover in fiber cells of the ocular lens, Aquaporin 0 (AQP0),
the most abundant membrane protein in the lens, undergoes extensive post-translational …

Novel fatty acid acylation of lens integral membrane protein aquaporin-0

KL Schey, DB Gutierrez, Z Wang, J Wei, AC Grey - Biochemistry, 2010 - ACS Publications
Fatty acid acylation of proteins is a well-studied co-or posttranslational modification typically
conferring membrane trafficking signals or membrane anchoring properties to proteins …

Protein aging: truncation of aquaporin 0 in human lens regions is a continuous age-dependent process

A Korlimbinis, Y Berry, D Thibault, KL Schey… - Experimental eye …, 2009 - Elsevier
The human lens is ideal for the study of macromolecular aging because cells in the centre,
along with their constituent proteins, are present for our entire lives. We examined the major …

[HTML][HTML] Water permeability of C-terminally truncated aquaporin 0 (AQP0 1-243) observed in the aging human lens

LE Ball, M Little, MW Nowak, DL Garland… - … & visual science, 2003 - arvojournals.org
purpose. To first assess the distribution of posttranslationally truncated products of
aquaporin 0 (AQP0) in dissected sections of a normal human lens and to determine the …

[HTML][HTML] The C terminus of lens aquaporin 0 interacts with the cytoskeletal proteins filensin and CP49

KML Rose, RG Gourdie, AR Prescott… - … & visual science, 2006 - arvojournals.org
purpose. Aquaporin 0 (AQP0), the most abundant membrane protein in the lens, is a water-
permeable channel, has a role in fiber cell adhesion, and is essential for fiber cell structure …

Proteolysis and mass spectrometric analysis of an integral membrane: aquaporin 0

J Han, KL Schey - Journal of Proteome Research, 2004 - ACS Publications
Due to hydrophobicity, structural analysis of integral membrane proteins poses a formidable
challenge for current mass spectrometry-based proteomics approaches. Herein, we …

Spatial distributions of phosphorylated membrane proteins aquaporin 0 and MP20 across young and aged human lenses

DB Gutierrez, DL Garland, JH Schwacke… - Experimental eye …, 2016 - Elsevier
In the human ocular lens it is now realized that post-translational modifications can alter
protein function and/or localization in fiber cells that no longer synthesize proteins. The …