ArticleJournal of ophthalmology2010
Inhibition of methylglyoxal-mediated protein modification in glyoxalase I overexpressing mouse lenses.
Article in Journal of ophthalmology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Article
- Glycation-mediated protein crosslinking and stiffening in mouse lenses are inhibited by carboxitin in vitro.Glycoconjugate journal · 2021Article
- AGE-RAGE Axis in the Pathophysiology of Chronic Lower Limb Ischemia and a Novel Strategy for Its Treatment.The International journal of angiology : official publication of the International College of Angiology, Inc · 2020Review
- Multiscale Process Modelling in Translational Systems Biology of Leishmania major: A Holistic view.Scientific reports · 2020Article
- AGE-RAGE Stress, Stressors, and Antistressors in Health and Disease.The International journal of angiology : official publication of the International College of Angiology, Inc · 2018Review
- Glyoxalase I is differentially expressed in cutaneous neoplasms and contributes to the progression of squamous cell carcinoma.The Journal of investigative dermatology · 2015Article
- Role of advanced glycation endproducts and glyoxalase I in diabetic peripheral sensory neuropathy.Translational research : the journal of laboratory and clinical medicine · 2012Review
- Protection from diabetes-induced peripheral sensory neuropathy--a role for elevated glyoxalase I?Experimental neurology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Objective. Here we tested the role of Glo I in the prevention of advanced glycation end product (AGE) formation in transgenic mouse lenses. Methods. A transgenic animal line that expressed high levels of human Glo I in the lens was developed from the C57B6 mouse strain. The role of Glo I in the inhibition of MGO-AGE formation was tested in organ-cultured lenses. Results. Organ culture of Wt and Glo I lenses with 5 mM D, L-glyceraldehyde (GLD) enhanced MGO by 29-fold and 17-fold in Wt lenses and Glo I lenses, respectively. Argpyrimidine levels were 192 +/- 73 pmoles/mg protein, and hydroimidazolone levels were 22 +/- 0.7 units/mug protein in GLD-incubated Wt lenses. In Glo I lenses, formation of AGEs was significantly inhibited; the argpyrimidine levels were 82 +/- 18 pmoles/mg protein, and the HI levels were 2.6 +/- 2.3 units/mug protein. Incubation of Wt lens proteins with 5 mM ribose for 7 days resulted in the formation of pentosidine. However, the levels were substantially higher in Glo I lens proteins incubated with ribose. Conclusion. Our study provides direct evidence that Glo I activity plays an important role in the regulation of AGE synthesis in the lens; while Glo I activity blocks the formation of MGO-AGEs, it might promote the formation of sugar-derived AGEs.
Identifiers
What 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.