Lens crystallins and oxidation: the special case of gammaS

Autor: Karine Prat, O. A. Bateman, Annette Tardieu, Françoise Bonneté, Fériel Skouri-Panet, Nicolette H. Lubsen
Přispěvatelé: Institut de minéralogie, de physique des matériaux et de cosmochimie (IMPMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de recherche pour le développement [IRD] : UR206-Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de minéralogie, cristallographie de Paris (LMCP), Université Pierre et Marie Curie - Paris 6 (UPMC)-IPG PARIS-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Cancérologie expérimentale, Institut National de la Santé et de la Recherche Médicale (INSERM), Protéines : biochimie structurale et fonctionnelle (PBSF), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Muséum national d'Histoire naturelle (MNHN)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de recherche pour le développement [IRD] : UR206-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Institut de Physique du Globe de Paris (IPG Paris)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2001
Předmět:
Spectrometry
Mass
Electrospray Ionization
Protein Conformation
Radical
Dimer
[SDV]Life Sciences [q-bio]
030303 biophysics
Molecular Sequence Data
Biophysics
Cataract formation
Photochemistry
Biochemistry
03 medical and health sciences
chemistry.chemical_compound
Crystallin
Lens
Crystalline
medicine
Animals
Humans
Scattering
Radiation
Amino Acid Sequence
030304 developmental biology
0303 health sciences
Sequence Homology
Amino Acid
Organic Chemistry
Hydrogen-Ion Concentration
Crystallins
eye diseases
[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biophysics
Cold Temperature
Crystallography
Monomer
medicine.anatomical_structure
chemistry
Lens (anatomy)
Cattle
sense organs
[PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph]
Dimerization
Oxidation-Reduction
Zdroj: Biophysical Chemistry
Biophysical Chemistry, Elsevier, 2001, 89 (1), pp.65-76. ⟨10.1016/s0301-4622(00)00216-7⟩
Biophysical Chemistry, 2001, 89 (1), pp.65-76. ⟨10.1016/s0301-4622(00)00216-7⟩
ISSN: 0301-4622
DOI: 10.1016/s0301-4622(00)00216-7⟩
Popis: International audience; Among lens crystallins, gamma -crystallins are particularly sensitive to oxidation, because of their high amount of Cys and Met residues. They have the reputation to induce, upon ageing, lens structural modifications leading to opacities. A combination of small angle X-ray scattering and chromatography was used to study the oxidation of gamma -crystallins. At pH 7.0, all the gamma -crystallins under study were checked to have the same structure in solution. Under gentle oxidation conditions at pH 8.0, human gammaS (h gammaS) and bovine gammaS (b gammaS) formed disulfide-linked dimers, whereas the other b gamma -crystallins did not. Cys20 was shown to be responsible for dimer formation since the C20S mutant only formed monomers. The h gammaS dimers were stable for weeks and did not form higher oligomers. In contrast, monomeric gammaS-crystallins freshly prepared at pH 8.0, and submitted to more drastic oxidation by X-ray induced free radicals, were rapidly transformed into higher oligomers. So, only extensive oxidation causing partial unfolding could be detrimental to the lens and linked to cataract formation. The gammaS-crystallins lack the temperature-induced opacification observed with the other gamma -crystallins and known as cold cataract. The oxidation-induced associative behaviour and cold cataract are therefore demonstrated to be uncoupled. (C) 2001 Elsevier Science B.V. All rights reserved.
Databáze: OpenAIRE
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