ArticleMolecular vision2010
Examining the influence of ultraviolet C irradiation on recombinant human γD-crystallin.
Article in Molecular vision, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Unravelling γD-crystallin aggregation pathway to understand cataract formation using fluorescence correlation spectroscopy.Molecular vision · 2025Article
- Unravelling γD-crystallin aggregation pathway to understand cataract formation using fluorescence correlation spectroscopy.Molecular vision · 2025Article
- Human γS-Crystallin Resists Unfolding Despite Extensive Chemical Modification from Exposure to Ionizing Radiation.The journal of physical chemistry. B · 2022Article
- UV Effect on Human Anterior Lens Capsule Macro-Molecular Composition Studied by Synchrotron-Based FTIR Micro-Spectroscopy.International journal of molecular sciences · 2021Article
- Mechanism of human γD-crystallin protein aggregation in UV-C light.Molecular vision · 2021Article
- Amorphous aggregation of tau in the presence of titanium dioxide nanoparticles: biophysical, computational, and cellular studies.International journal of nanomedicine · 2019Article
- Article
- Gold Nanocluster Protection of Protein from UVC Radiation: A Model Study on Bovine Serum Albumin.ACS omega · 2017Article
- Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.Investigative ophthalmology & visual science · 2017Article
- Small molecules, both dietary and endogenous, influence the onset of lens cataracts.Experimental eye research · 2017Review
- A potential role for endogenous proteins as sacrificial sunscreens and antioxidants in human tissues.Redox biology · 2015Article
- UV radiation effects on a DNA repair enzyme: conversion of a [4Fe-4S](2+) cluster into a [2Fe-2S] (2+).Radiation and environmental biophysics · 2015Article
- Article
- Understanding the Physical and Molecular Basis of Stability of Arabidopsis DNA Pol λ under UV-B and High NaCl Stress.PloS one · 2015Article
- Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal models.Current pharmaceutical design · 2014Review
- Comparative analysis of human γD-crystallin aggregation under physiological and low pH conditions.PloS one · 2014Article
- Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage.Biochemistry · 2013Article
- The human W42R γD-crystallin mutant structure provides a link between congenital and age-related cataracts.The Journal of biological chemistry · 2013Article
- Lysine-specific molecular tweezers are broad-spectrum inhibitors of assembly and toxicity of amyloid proteins.Journal of the American Chemical Society · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeHuman γD crystallin is a principal protein component of the human eye lens and associated with the development of juvenile and mature-onset cataracts. Exposure to ultraviolet (UV) light is thought to perturb protein structure and eventually lead to aggregation. This work is aimed at exploring the effects of UV-C irradiation on recombinant human γD-crystallin (HGDC).
methodsRecombinant HGDC proteins were expressed in E. coli strain BL21(DE3) harboring plasmid pEHisHGDC and purified using chromatographic methods. The proteins were then exposed to UV-C light (λ(max)=254 nm, 15 W) at the intensity of 420, 800, or 1850 μW/cm(2). The UV-C-unexposed, supernatant fraction of UV-C-exposed, and re-dissolved precipitated fraction of UV-C exposed preparations were characterized by SDS-PAGE, turbidity measurement, CD spectroscopy, tryptophan fluorescence spectroscopy, acrylamide fluorescence quenching analysis, and sulfhydryl group measurements.
resultsThe turbidity of the HGDC sample solution was found to be positively correlated with HGDC concentration, UV-C irradiation intensity, and UV-C irradiation duration. When exposed to UV-C, HGDC sample solutions became visibly turbid and a noticeable amount of larger protein particle, perceptible to the naked eye, was observed upon prolonged irradiation. The precipitated fraction of irradiated HGDC sample was found to be re-dissolved by guanidine hydrochloride. Electrophoresis, acrylamide fluorescence quenching, and spectroscopic analyses revealed differences in structures among the non-irradiated HGDC, the supernatant fraction of irradiated HGDC, and the re-dissolved precipitated fraction of irradiated HGDC. Through the use of L-cysteine, the measurements of sulfhydryl contents, and the reducing as well as non-reducing SDS-PAGE, our data further suggested that disulfide bond formation and/or cleavage probably play an important role in aggregation and/or precipitation of HGDC elicited by UV-C irradiation.
conclusionsOur findings highlight the close connections among disulfide bond cleavage and/or formation, intermolecular interactions, and the resultant formation of aggregates of HGDC induced by UV-C irradiation. The results from this research may not only contribute to the understanding of the environmental factors causing protein aggregation but also have implications for deciphering the molecular mechanism of cataractogenesis.
Indexed as
Identifiers
21197112PMC3008712W169182329What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.