Small-angle neutron and X-ray scattering analysis of the supramolecular organization of rhodopsin in photoreceptor membrane

Feldman, T. B.; Ivankov, Oleksandr I.; Куклин, А. И.; Murugova, T. N.; Yakovleva, M. A.; Smitienko, O. A.; Kolchugina, I. B.; Round, Adam; Gordeliy, Valentin; Belushkin, Α. V.; Оstrovsky, М. А.

doi:10.1016/j.bbamem.2019.05.022

Cited by 12 publications

(2 citation statements)

References 54 publications

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“…POSs from bovine retina tissue, which was isolated within 3 h after slaughter, were prepared as described previously [ 57 ]. Retinas were added to 50% sucrose solution in Buffer A comprising 10 mM MOPS pH 7.4, 30 mM NaCl, 60 mM KCl, 2 mM MgCl 2 , 0.1 mM phenylmethylsulfonyl fluoride (PMSF), 1 mM dithiothreitol, and 0.01% NaN 3 (1 mL per each retina).…”

Section: Methodsmentioning

confidence: 99%

Lipofuscin Granule Bisretinoid Oxidation in the Human Retinal Pigment Epithelium forms Cytotoxic Carbonyls

Yakovleva

Донцов

Трофимова

et al. 2021

IJMS

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Age-related macular degeneration (AMD) is the primary cause of central blindness among the elderly. AMD is associated with progressive accumulation of lipofuscin granules in retinal pigment epithelium (RPE) cells. Lipofuscin contains bisretinoid fluorophores, which are photosensitizers and are phototoxic to RPE and neuroretinal cells. In the presence of oxygen, bisretinoids are also oxidized, forming various products, consisting primarily of aldehydes and ketones, which are also potentially cytotoxic. In a prior study, we identified that in AMD, bisretinoid oxidation products are increased in RPE lipofuscin granules. The purpose of the present study was to determine if these products were toxic to cellular structures. The physicochemical characteristics of bisretinoid oxidation products in lipofuscin, which were obtained from healthy donor eyes, were studied. Raman spectroscopy and time-of-flight secondary ion mass spectrometry (ToF–SIMS) analysis identified the presence of free-state aldehydes and ketones within the lipofuscin granules. Together, fluorescence spectroscopy, high-performance liquid chromatography, and mass spectrometry revealed that bisretinoid oxidation products have both hydrophilic and amphiphilic properties, allowing their diffusion through lipofuscin granule membrane into the RPE cell cytoplasm. These products contain cytotoxic carbonyls, which can modify cellular proteins and lipids. Therefore, bisretinoid oxidation products are a likely aggravating factor in the pathogenesis of AMD.

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Section: Methodsmentioning

confidence: 99%

Lipofuscin Granule Bisretinoid Oxidation in the Human Retinal Pigment Epithelium forms Cytotoxic Carbonyls

Yakovleva

Донцов

Трофимова

et al. 2021

IJMS

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“…In fact, rhodopsin is equally active as a monomer, and the organization in the ROS disc membranes is still debated (monomer, dimer, longer stretches?) ( Fotiadis et al, 2004 ; Chabre and LeMaire, 2005 ; Mishra et al, 2016 ; Zhang et al, 2016 ; Feldman et al, 2019 ; Zhao et al, 2019 ). Invertebrate visual rhodopsins are probably rigidly immobilized in their native membrane, which allows to discern the polarization plane of the incoming light ( Gärtner, 2000 ; Stavenga et al, 2000 ).…”

Section: Spectral and Structural Properties And Solubilizationmentioning

confidence: 99%

Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering

Grip

Ganapathy

2022

Front. Chem.

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The first member and eponym of the rhodopsin family was identified in the 1930s as the visual pigment of the rod photoreceptor cell in the animal retina. It was found to be a membrane protein, owing its photosensitivity to the presence of a covalently bound chromophoric group. This group, derived from vitamin A, was appropriately dubbed retinal. In the 1970s a microbial counterpart of this species was discovered in an archaeon, being a membrane protein also harbouring retinal as a chromophore, and named bacteriorhodopsin. Since their discovery a photogenic panorama unfolded, where up to date new members and subspecies with a variety of light-driven functionality have been added to this family. The animal branch, meanwhile categorized as type-2 rhodopsins, turned out to form a large subclass in the superfamily of G protein-coupled receptors and are essential to multiple elements of light-dependent animal sensory physiology. The microbial branch, the type-1 rhodopsins, largely function as light-driven ion pumps or channels, but also contain sensory-active and enzyme-sustaining subspecies. In this review we will follow the development of this exciting membrane protein panorama in a representative number of highlights and will present a prospect of their extraordinary future potential.

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Supramolecular organization of rhodopsin in rod photoreceptor cell membranes

Park

2021

Pflugers Arch - Eur J Physiol

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Small-angle neutron and X-ray scattering analysis of the supramolecular organization of rhodopsin in photoreceptor membrane

Cited by 12 publications

References 54 publications

Lipofuscin Granule Bisretinoid Oxidation in the Human Retinal Pigment Epithelium forms Cytotoxic Carbonyls

Lipofuscin Granule Bisretinoid Oxidation in the Human Retinal Pigment Epithelium forms Cytotoxic Carbonyls

Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering

Supramolecular organization of rhodopsin in rod photoreceptor cell membranes

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