ArticleInvestigative ophthalmology & visual science2013
Exploration of molecular factors impairing superoxide dismutase isoforms activity in human senile cataractous lenses.
Article in Investigative ophthalmology & visual science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Bioavailability of AREDS1 micronutrients from softgel capsules and tablets: a pilot study.Molecular vision · 2014Trial
- Genetic variants in genes regulating lens epithelial cell homeostasis in dead bag syndrome: part 2.Journal of cataract and refractive surgery · 2026Article
- The Applications and Mechanisms of Superoxide Dismutase in Medicine, Food, and Cosmetics.Antioxidants (Basel, Switzerland) · 2023Review
- Current Approach to the Pathogenesis of Diabetic Cataracts.International journal of molecular sciences · 2023Review
- Can Antioxidants Reduce the Toxicity of Bisphenol?Antioxidants (Basel, Switzerland) · 2022Review
- Some Aspects of Development and Histological Structure of the Visual System of Nothobranchius Guentheri.Animals : an open access journal from MDPI · 2021Article
- Protein posttranslational modification (PTM) by glycation: Role in lens aging and age-related cataractogenesis.Experimental eye research · 2021Review
- Antioxidant Defenses in the Human Eye: A Focus on Metallothioneins.Antioxidants (Basel, Switzerland) · 2021Review
- Medicinal Plants and Natural Products Used in Cataract Management.Frontiers in pharmacology · 2019Review
- Effects of histone acetylation on superoxide dismutase 1 gene expression in the pathogenesis of senile cataract.Scientific reports · 2016Article
- Increased VEGF-A promotes multiple distinct aging diseases of the eye through shared pathomechanisms.EMBO molecular medicine · 2016Article
- Age and Smoking Related Changes in Metal Ion Levels in Human Lens: Implications for Cataract Formation.PloS one · 2016Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTo explore different molecular factors impairing the activities of superoxide dismutase (SOD) isoforms in senile cataractous lenses.
methodsEnzyme activity of SOD isoforms, levels of their corresponding cofactors copper (Cu), manganese (Mn), zinc (Zn), and expression of mRNA transcripts and proteins were determined in the lenses of human subjects with and without cataract. DNA from lens epithelium (LE) and peripheral blood was isolated. Polymerase chain reaction-single strand conformation polymorphism (PCR-SSCP) followed by sequencing was carried out to screen somatic mutations. The impact of intronic insertion/deletion (INDEL) variations on the splicing process and on the resultant transcript was evaluated. Genotyping of IVS4+42delG polymorphism of SOD1 gene was done by PCR-restriction fragment length polymorphism (RFLP).
resultsA significant decrease in Cu/Zn- and Mn-SOD activity (P < 0.001) and in Cu/Zn-SOD transcript (P < 0.001) and its protein (P < 0.05) were found in cataractous lenses. No significant change in the level of copper (P = 0.36) and an increase in the level of manganese (P = 0.01) and zinc (P = 0.02) were observed in cataractous lenses. A significant positive correlation between the level of Cu/Zn-SOD activity and the levels of Cu (P = 0.003) and Zn (P = 0.005) was found in the cataractous lenses. DNA sequencing revealed three intronic INDEL variations in exon4 of SOD1 gene. Splice-junction analysis showed the potential of IVS4+42delG in creating a new cryptic acceptor site. If it is involved in alternate splicing, it could result in generation of SOD1 mRNA transcripts lacking exon4 region. Transcript analysis revealed the presence of complete SOD1 mRNA transcripts. Genotyping revealed the presence of IVS4+42delG polymorphism in all subjects.
conclusionsThe decrease in the activity of SOD1 isoform in cataractous lenses was associated with the decreased level of mRNA transcripts and their protein expression and was not associated with either modulation in the level of enzyme cofactors or with INDEL variations.
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