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Photosensitized Oxidation of Lens Proteins Exposed to UVA-Visible Light at Low Oxygen Concentration: Its Effect on the Proteasome System

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Studies on the Cornea and Lens

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Abstract

This chapter describes the photosensitizing properties of the colored compounds generated in the human lens during aging and their effect on the proteasomal system. All the experiments were performed using UVA-visible light and a low oxygen concentration, which corresponds to the actual condition in this tissue. The colored and cross-linked lens proteins, which are increasingly generated as a function of aging, do not undergo additional cross-linking when exposed to UVA-visible light under a low oxygen pressure. The photosensitized damage observed in these conditions is restricted to oxidation processes located near the chromophore. Interestingly, a glucose-derived chromophore with identical spectral and chromatographic properties as those found in one of the components of the water-soluble fractions of cataractous human eye lenses produces increased protein oxidation and protein cross-linking when lens proteins were exposed to UVA-visible light under a 5 % oxygen atmosphere. In addition, increased proteasome peptidase activity was observed. The behavior of this protective system in human lenses corresponding to various age groups is also described in this chapter.

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Abbreviations

AGEs:

Advanced glycation end products

ASC:

Ascorbate

BLPs:

Bovine lens proteins

CML:

Carboxymethyllysine

GDC:

Glucose decomposition chromophore

Glc:

Glucose

LP:

Lens protein

RH:

Reduced substrate

RH•+ :

R• and ROxid represent the intermediate radical cation, the neutral radical and the oxidized form of the substrate, respectively

ROS:

Reactive oxygen species

S:

Sensitizer

Threo:

Threose

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Acknowledgments

These studies were supported by CONICYT (Chile), bi-national projects ECOS (France)/CONICYT (Chile), and the European Union.

Author information

Authors and Affiliations

  1. Faculty of Chemistry, Department of Physical Chemistry, Pontifical Catholic University of Chile, Casilla 306, Correo 22, Santiago, Chile

    Eduardo Silva

  2. Laboratory of Cellular Biology of Aging, UR4-IFR83, Pierre-and-Marie-Curie University, Paris, France

    Felipe Ávila & Bertrand Friguet

  3. Interdisciplinary Research Program of Excellence in Healthy Aging (PIEI-ES), Universidad de Talca, Talca, Chile

    Felipe Ávila

  4. Adaptation Biologique et Vieillissement, Institute of Biology Paris-Seine, INSERM U1164, UPMC University, Paris, France

    Bertrand Friguet

Authors
  1. Eduardo Silva
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  2. Felipe Ávila
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  3. Bertrand Friguet
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Corresponding author

Correspondence to Eduardo Silva .

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Editors and Affiliations

  1. Innovative Vision Products Inc., Moscow, Russia, Innovative Vision Products, Inc.,, County of New Castle, Delaware, USA

    Mark A. Babizhayev

  2. Department of Ophthalmology and Visual Sciences, Truhlsen Eye Institute, College of Medicine, University of Nebraska Medical Center; Key Laboratory of Protein Chemistry and Developmental Biology of Education Ministry of China, College of Life Sciences, Hunan Normal University, Changsha, Hunan, China, Omaha, Nebraska, USA

    David Wan-Cheng Li

  3. Department of Pharmaceutical Sciences and Oklahoma Center for Neuroscience, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA

    Anne Kasus-Jacobi

  4. Department of Ophthalmology, University of Pristina, Faculty of Medicine, Kosovska Mitrovica, Serbia

    Lepša Žorić

  5. Ophthalmology, Miguel Hernandez University, Alicante, Spain

    Jorge L. Alió

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Silva, E., Ávila, F., Friguet, B. (2015). Photosensitized Oxidation of Lens Proteins Exposed to UVA-Visible Light at Low Oxygen Concentration: Its Effect on the Proteasome System. In: Babizhayev, M., Li, DC., Kasus-Jacobi, A., Žorić, L., Alió, J. (eds) Studies on the Cornea and Lens. Oxidative Stress in Applied Basic Research and Clinical Practice. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-1935-2_14

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