scholarly journals Post-translational Modification of .ALPHA.B-Crystallin of Normal Human Lens.

2000 ◽  
Vol 23 (2) ◽  
pp. 226-230 ◽  
Author(s):  
Akira KAMEI ◽  
Takayuki HAMAGUCHI ◽  
Nobuyuki MATSUURA ◽  
Hiroshi IWASE ◽  
Katsuyoshi MASUDA
Keyword(s):  
Human Lens ◽  
Post Translational Modification ◽  
Normal Human

Pathogenesis of Age-related Cataract: a systematic review of proteomic studies

2020 ◽  
Vol 17 ◽  
Author(s):  
Christina Karakosta ◽  
Argyrios Tzamalis ◽  
Michalis Aivaliotis ◽  
Ioannis Tsinopoulos
Keyword(s):  
Systematic Review ◽  
Oxidant Stress ◽  
Critical Role ◽  
Human Lens ◽  
Nuclear Cataract ◽  
Cataract Formation ◽  
Post Translational Modification ◽  
Ability To Act ◽  
Age Related

Background/Objective:: The aim of this systematic review is to identify all the available data on human lens proteomics with a critical role to age-related cataract formation in order to elucidate the physiopathology of the aging lens. Materials and Methods:: We searched on Medline and Cochrane databases. The search generated 328 manuscripts. We included nine original proteomic studies that investigated human cataractous lenses. Results:: Deamidation was the major age-related post-translational modification. There was a significant increase in the amount of αA-crystallin D-isoAsp58 present at all ages, while an increase in the extent of Trp oxidation was apparent in cataract lenses when compared to aged normal lenses. During aging, enzymes with oxidized cysteine at critical sites included GAPDH, glutathione synthase, aldehyde dehydrogenase, sorbitol dehydrogenase, and PARK7. Conclusion:: D-isoAsp in αA crystallin could be associated with the development of age-related cataract in human, by contributing to the denaturation of a crystallin, and decreasing its ability to act as a chaperone. Oxidation of Trp may be associated with nuclear cataract formation in human, while the role of oxidant stress in age-related cataract formation is dominant.

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 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.

scholarly journals Distribution of peptidyl-glycine alpha-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors.

1996 ◽  
Vol 44 (1) ◽  
pp. 3-12 ◽  
Author(s):  
L Saldise ◽  
A Martínez ◽  
L M Montuenga ◽  
A Treston ◽  
D R Springall ◽  
...  
Keyword(s):  
Human Lung ◽  
Regulatory Peptides ◽  
Lung Tumors ◽  
Normal Lung ◽  
Post Translational Modification ◽  
Human Lung Tissue ◽  
Lung Epithelial ◽  
Normal Human ◽  
Myelinated Nerves ◽  
Intrinsic Ganglia

C-terminal alpha-amidation is a post-translational modification necessary for the biological activity of many regulatory peptides produced in the respiratory tract. This modification is a two-step process catalyzed by two separate enzyme activities, both derived from the peptidyl-glycine alpha-amidating mono-oxygenase (PAM) precursor. The distribution of these two enzymes, peptidyl-glycine alpha-hydroxylating monoxygenase (PHM) and peptidyl-alpha-hydroxyglycine a amidating lyase (PAL), was studied in the normal lung and in lung tumors using immunocytochemical methods and in situ hybridization. In normal lung the enzymes were located in some cells of the airway epithelium and glands, the endothelium of blood vessels, some chondrocytes of the bronchial cartilage, the alveolar macrophages, smooth muscle cells, neurons of the intrinsic ganglia, and in myelinated nerves. A total of 24 lung tumors of seven different histological types were studied. All cases contained PAM-immunoreactive cells with various patterns of distribution. All immunoreactive cells were positive for the PHM antiserum but only some of them for the PAL antiserum. The distribution of PAM co-localizes with some other previously described amidated peptides, suggesting that amidation is an important physiological process taking place in the normal and malignant human lung tissue.

Sign in / Sign up

Export Citation Format

Share Document