Zobrazeno 1 - 10
of 95
pro vyhledávání: '"Beryl J. Ortwerth"'
Autor:
Richard T. Mathias, Roger J.W. Truscott, Beryl J. Ortwerth, Huan Wang, Steven Bassnett, Richard McNulty
Publikováno v:
The Journal of Physiology. 559:883-898
Opacification of the lens nucleus is a major cause of blindness and is thought to result from oxidation of key cellular components. Thus, long-term preservation of lens clarity may depend on the maintenance of hypoxia in the lens nucleus. We mapped t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d7d62871007cded0b7b2b82987791960
https://doi.org/10.1113/jphysiol.2004.068619
https://doi.org/10.1113/jphysiol.2004.068619
Publikováno v:
Journal of Biological Chemistry. 279:6487-6495
Post-translational modifications of proteins take place during the aging of human lens. The present study describes a newly isolated glycation product of lysine, which was found in the human lens. Cataractous and aged human lenses were hydrolyzed and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9cd1c274691373ef51606b4be9587ce1
https://doi.org/10.1074/jbc.m309090200
https://doi.org/10.1074/jbc.m309090200
Publikováno v:
Experimental Eye Research. 77:313-325
Quantitative changes in the 330 nm absorbing chromophores and 350/450 nm fluorophores of water-soluble (WS) and water-insoluble (WI) proteins of individual human cataract lenses were characterized and compared with aged normal human lens. Twenty-five
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a68c4d54682febfc5771ef24c1dd873e
https://doi.org/10.1016/s0014-4835(03)00131-3
https://doi.org/10.1016/s0014-4835(03)00131-3
Publikováno v:
Experimental Eye Research. 74:217-229
The protein-bound chromophores, which increase with aging in the human lens, act as UVA sensitizers, producing almost exclusively singlet oxygen in vitro. Direct irradiation of whole, aged human lenses with high intensity UVA light (200 mW cm(-2) for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c736e8a853fffe295ae4ff6cd3a1ebac
https://doi.org/10.1006/exer.2001.1114
https://doi.org/10.1006/exer.2001.1114
Publikováno v:
Applied Biochemistry and Biotechnology. 94:71-96
Advanced glycation end products (AGEs) and, specifically, protein-protein AGE crosslinks have long been studied for their potential role in aging, diabetic complications and Alzheimer disease. With few exceptions, the chemical nature of these structu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a345065a9fd4e26873da63bb3e42c931
https://doi.org/10.1385/abab:94:1:71
https://doi.org/10.1385/abab:94:1:71
Autor:
Beryl J. Ortwerth, Gregory Simpson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1501:12-24
The degradation of L-ascorbate (AsA) and its primary oxidation products, L-dehydroascorbate (DHA) and 2,3-L-diketogulonate (2,3-DKG) were studied under physiological conditions. Analysis determined that L-erythrulose (ERU) and oxalate were the primar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59780dd24c71e579b8eeacd9d4394fec
https://doi.org/10.1016/s0925-4439(00)00009-0
https://doi.org/10.1016/s0925-4439(00)00009-0
Publikováno v:
Experimental Eye Research. 69:375-384
The water-insoluble (WI) fraction from aged human lenses contains yellow chromophoric sensitizers, which generate reactive oxygen species (ROS) when irradiated with UVA light. The WI proteins from type I to V brunescent cataract lenses were assayed f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcb46313508752bf72d1530012a8e114
https://doi.org/10.1006/exer.1999.0709
https://doi.org/10.1006/exer.1999.0709
Autor:
Beryl J. Ortwerth, Hongying L. James
Publikováno v:
Biochemical and Biophysical Research Communications. 259:706-710
The formation of advanced glycation endproducts (AGEs) from glucose in vitro requires both oxygen and a transition metal ion, usually copper. These elements combine to produce reactive oxygen species (ROS) which degrade glucose to AGE-forming compoun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12374df34160d15fa1c6fc2fd3a4cfb5
https://doi.org/10.1006/bbrc.1999.0841
https://doi.org/10.1006/bbrc.1999.0841
Publikováno v:
Photochemistry and Photobiology. 69:259-264
Oxidation of cysteine, glutathione and ascorbate by photoexcited proteins from normal and cataractous lenses was investigated using electron paramagnetic resonance in combination with spin trapping. We report that illumination of these proteins in pH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5871f132fc03f7388989abc35c5824c8
https://doi.org/10.1111/j.1751-1097.1999.tb03284.x
https://doi.org/10.1111/j.1751-1097.1999.tb03284.x
Publikováno v:
Archives of Biochemistry and Biophysics. 351:189-196
The oxidation products of ascorbic acid (AscH − ) can rapidly glycate and crosslink lens proteins in vitro, producing fluorophores and browning products similar to those present in cataractous lenses. The accumulation of AscH − oxidation products
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::309ebfdd2dcf720f006e1d08c929e462
https://doi.org/10.1006/abbi.1997.0549
https://doi.org/10.1006/abbi.1997.0549