Post-translational Modifications of Aquaporin 0 (AQP0) in the Normal Human Lens:  Spatial and Temporal Occurrence†

Biochemistry ◽  
2004 ◽  
Vol 43 (30) ◽  
pp. 9856-9865 ◽  
Author(s):  
Lauren E. Ball ◽  
Donita L. Garland ◽  
Rosalie K. Crouch ◽  
Kevin L. Schey
Keyword(s):  
Human Lens ◽  
Post Translational Modifications ◽  
Normal Human ◽  
Temporal Occurrence

Syneretic Response of Aging Normal Human Lens to Pressure

2003 ◽  
Vol 44 (1) ◽  
pp. 258 ◽  
Author(s):  
Frederick A. Bettelheim ◽  
Martin J. Lizak ◽  
J. Samuel Zigler
Keyword(s):  
Human Lens ◽  
Normal Human

Covalent changes at the N- and C-terminal regions of gamma crystallin during aging of the normal human lens

1987 ◽  
Vol 45 (2) ◽  
pp. 207-214 ◽  
Author(s):  
Larry Takemoto ◽  
Toshio Kodama ◽  
Dolores Takemoto
Keyword(s):  
Human Lens ◽  
Gamma Crystallin ◽  
Normal Human

scholarly journals A Survey of Membrane Proteins in Human Serum

2012 ◽  
Vol 5 ◽  
pp. PRI.S9374 ◽  
Author(s):  
Nguyen Tien Dung ◽  
Phan Van Chi
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Human Serum ◽  
Transmembrane Domain ◽  
Tissue Sample ◽  
Ionization Mass ◽  
Post Translational Modifications ◽  
Molecular Weights ◽  
Normal Human ◽  
Nano Liquid Chromatography

Serum and membrane proteins are two of the most attractive targets for proteomic analysis. Previous membrane protein studies tend to focus on tissue sample, while membrane protein studies in serum are still limited. In this study, an analysis of membrane proteins in normal human serum was carried out. Nano-liquid chromatography-electrospray ionization mass spectrometry (NanoLC-ESI-MS/MS) and bioinformatics tools were used to identify membrane proteins. Two hundred and seventeen membrane proteins were detected in the human serum, of which 129 membrane proteins have at least one transmembrane domain (TMD). Further characterizations of identified membrane proteins including their subcellular distributions, molecular weights, post translational modifications, transmembrane domains and average of hydrophobicity, were also implemented. Our results showed the potential of membrane proteins in serum for diagnosis and treatment of diseases.

scholarly journals Scanning EM studies of normal human lens fibres and fibres from nuclear cataracts

Eye ◽  
1991 ◽  
Vol 5 (1) ◽  
pp. 86-92 ◽  
Author(s):  
R J Stirling ◽  
P G Griffiths
Keyword(s):  
Human Lens ◽  
Normal Human ◽  
Scanning Em

scholarly journals Structure Elucidation of a Novel Yellow Chromophore from Human Lens Protein

2004 ◽  
Vol 279 (44) ◽  
pp. 45441-45449 ◽  
Author(s):  
Rongzhu Cheng ◽  
Qi Feng ◽  
Ognyan K. Argirov ◽  
Beryl J. Ortwerth
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Water Soluble ◽  
Human Lens ◽  
Lens Protein ◽  
Two Dimensional ◽  
Cross Link ◽  
Lens Proteins ◽  
Lysine Residues ◽  
Normal Human

We report here the isolation of a novel acid-labile yellow chromophore from the enzymatic digest of human lens proteins and the identification of its chemical structure by liquid chromatography-mass spectrometry, liquid chromatography-tandem mass spectrometry, and1H,13C, and two-dimensional NMR. This new chromophore exhibited a UV absorbance maximum at 343 nm and fluorescence at 410 nm when excited at 343 nm. Analysis of the purified compound by reversed-phase HPLC with in-line electrospray ionization mass spectrometry revealed a molecular mass of 370 Da. One- and two-dimensional NMR analyses elucidated the structure to be 1-(5-amino-5-carboxypentyl)-4-(5-amino-5-carboxypentylamino)-3-hydroxy-2,3-dihydropyridinium, a cross-link between the ϵ-amino groups of two lysine residues, and a five-carbon ring. Because this cross-link contains two lysine residues and a dihydropyridinium ring, we assigned it the trivial name of K2P. Quantitative determinations of K2P in individual normal human lens or cataract lens water-soluble and water-insoluble protein digests were made using a high-performance liquid chromatograph equipped with a diode array detector. These measurements revealed a significant enhancement of K2P in cataract lens proteins (613 ± 362 pmol/mg of water-insoluble sonicate supernatant (WISS) protein or 85 ± 51 pmol/mg of WS protein) when compared with aged normal human lens proteins (261 ± 93 pmol/mg of WISS protein or 23 ± 15 pmol/mg of water-soluble (WS) protein). These data provide chemical evidence for increased protein cross-linking during aging and cataract developmentin vivo. This new cross-link may serve as a quantitatively more significant biomarker for assessing the role of lens protein modifications during aging and in the pathogenesis of cataract.

Particle Irradiation Induces FGF2 Expression in Normal Human Lens Cells

2000 ◽  
Vol 154 (5) ◽  
pp. 477-484 ◽  
Author(s):  
P. Y. Chang ◽  
K. A. Bjornstad ◽  
E. Chang ◽  
M. McNamara ◽  
M. H. Barcellos-Hoff ◽  
...  
Keyword(s):  
Human Lens ◽  
Particle Irradiation ◽  
Lens Cells ◽  
Fgf2 Expression ◽  
Normal Human

scholarly journals Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity

2014 ◽  
Vol 462 (1) ◽  
pp. 77-88 ◽  
Author(s):  
Kristen E. Funk ◽  
Stefani N. Thomas ◽  
Kelsey N. Schafer ◽  
Grace L. Cooper ◽  
Zhongping Liao ◽  
...  
Keyword(s):  
Human Brain ◽  
Tau Protein ◽  
Protein Function ◽  
Lysine Methylation ◽  
Post Translational Modification ◽  
Post Translational Modifications ◽  
Aggregation Propensity ◽  
Normal Human ◽  
Tau Aggregation

Diverse post-translational modifications regulate tau protein function and misfolding. In the present study we identified lysine methylation as a tau post-translational modification in normal human brain, and found it depressed tau aggregation propensity when modelled in vitro.

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