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Beryl J. Ortwerth

Researcher at University of Missouri

Publications -  106
Citations -  3462

Beryl J. Ortwerth is an academic researcher from University of Missouri. The author has contributed to research in topics: Lens protein & Ascorbic acid. The author has an hindex of 34, co-authored 106 publications receiving 3349 citations.

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High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis

TL;DR: The results suggest that redox imbalance in cellular senescent systems such as the ocular lens may lead to irreversible ascorbate oxidation and protein crosslinking by xylosone, which may play an important role in the pathogenesis of "brunescent" cataracts.
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Regulation of tissue oxygen levels in the mammalian lens

TL;DR: The distribution of mitochondria was mapped in living lenses by 2‐photon microscopy and it was found that a steep gradient of PO2 was maintained within the tissue, leading to PO2 < 2 mmHg in the core, indicating the presence of non‐mitochondrial oxygen consumers.
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The non-oxidative degradation of ascorbic acid at physiological conditions.

TL;DR: ERU is an extremely reactive ketose, which rapidly glycates and crosslinks proteins, and therefore may mediate the AsA-dependent modification of protein (ascorbylation) seen in vitro, and also proposed to occur in vivo in human lens during diabetic and age-onset cataract formation.
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Ascorbic acid-induced crosslinking of lens proteins: evidence supporting a Maillard reaction.

TL;DR: The incubation of calf lens extracts with 20 mM ascorbic acid under sterile conditions for 8 weeks caused extensive protein crosslinking, which was not observed with either 20 mM sorbitol or 20 mM glucose, and ascorBic acid did induce the formation of high-molecular-weight protein aggregates as determined by Agarose A-5m chromatography.
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Vitamin C mediates chemical aging of lens crystallins by the Maillard reaction in a humanized mouse model.

TL;DR: Data strongly implicate vitamin C in lens crystallin aging and may serve as a model for protein aging in other tissues particularly rich in vitamin C, such as the hippocampal neurons and the adrenal gland.