ArticleInvestigative ophthalmology & visual science2010
Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.
Article in Investigative ophthalmology & visual science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 73 citations in OpenAlex.
- Trehalose Restrains the Fibril Load towards α-Lactalbumin Aggregation and Halts Fibrillation in a Concentration-Dependent Manner.Biomolecules · 2021Article
- Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.Journal of structural biology · 2020Review
- The genetic landscape of crystallins in congenital cataract.Orphanet journal of rare diseases · 2020Article
- Biophysical Elucidation of Fibrillation Inhibition by Sugar Osmolytes in α-Lactalbumin: Multispectroscopic and Molecular Docking Approaches.ACS omega · 2020Article
- Trehalose Inhibits the Heat-Induced Formation of the Amyloid-Like Structure of Soluble Proteins Isolated from Human Cataract Lens.The protein journal · 2020Article
- Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.Biochimica et biophysica acta. General subjects · 2020Article
- RETRACTED: Peptide-induced formation of protein aggregates and amyloid fibrils in human and guinea pig αA-crystallins under physiological conditions of temperature and pH.Experimental eye research · 2019Article
- Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Rosmarinic Acid Restores Complete Transparency of Sonicated Human Cataract Ex Vivo and Delays Cataract Formation In Vivo.Scientific reports · 2018Article
- Amyloid β-Sheet Secondary Structure Identified in UV-Induced Cataracts of Porcine Lenses using 2D IR Spectroscopy.Journal of molecular biology · 2017Article
- Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.Investigative ophthalmology & visual science · 2017Article
- A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.Biophysical journal · 2017Article
- Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.Frontiers in physiology · 2017Article
- Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.Protein science : a publication of the Protein Society · 2016Article
- The βγ-crystallins: native state stability and pathways to aggregation.Progress in biophysics and molecular biology · 2014Review
- An alternative structural isoform in amyloid-like aggregates formed from thermally denatured human γD-crystallin.Protein science : a publication of the Protein Society · 2014Article
- Tyrosine/cysteine cluster sensitizing human γD-crystallin to ultraviolet radiation-induced photoaggregation in vitro.Biochemistry · 2014Article
- Comparative analysis of human γD-crystallin aggregation under physiological and low pH conditions.PloS one · 2014Article
- Electrostatic origin of in vitro aggregation of human γ-crystallin.The Journal of chemical physics · 2013Article
- Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage.Biochemistry · 2013Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
purposeMature-onset cataract results from the formation of light-scattering aggregates of lens crystallins. Although oxidative or mutational damage may be a prerequisite, little is known of the initiation or nucleation of these aggregated states. In mice carrying mutations in gamma-crystallin genes, a truncated form of gamma-crystallin formed intranuclear filamentous inclusions within lens fiber cells. Previous studies have shown that bovine crystallins and human gammaD-crystallin form amyloid fibrils under denaturing conditions in vitro. The amyloid fibril formation of human gammaC-crystallin (HgammaC-Crys) induced by low pH, together with characterization of a partially unfolded intermediate in the process were investigated.
methodsHgammaC-Crys was expressed and purified from Escherichia coli. Partially unfolded intermediates were detected by tryptophan fluorescence spectroscopy and UV resonance Raman spectroscopy. The aggregation into amyloid fibrils was monitored by solution turbidity and fluorescence assay. The morphology of aggregates was characterized using transmission electron microscopy (TEM). Secondary structure of the peptides in their fibrillar state was characterized using Fourier transform infrared spectroscopy (FTIR).
resultsThe structure of HgammaC-Crys was perturbed at low pH. Partially unfolded intermediates were detected when solution pH was lowered to pH 3. At pH 3, HgammaC-Crys aggregated into amyloid fibrils. The kinetics and extent of the reaction was dependent on protein concentration, pH, and temperature. TEM images of aggregates revealed aggregation stages from short to long fibrils and from long fibrils to light-scattering fibril networks. FTIR spectroscopy confirmed the cross-beta character of the secondary structure of these fibrils.
conclusionsHgammaC-Crys formed amyloid fibrils on incubation at low pH via a partially unfolded intermediate. This process could contribute to the early stages of the formation of light-scattering species in the eye lens.
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