2009 journal article
Changes in Ferritin H- and L-Chains in Canine Lenses with Age-Related Nuclear Cataract
INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE, 50(1), 305–310.
MeSH headings : Aging; Animals; Apoferritins / metabolism; Cataract / metabolism; Cataract / veterinary; Dog Diseases / metabolism; Dogs; Electrophoresis, Polyacrylamide Gel / veterinary; Enzyme-Linked Immunosorbent Assay / veterinary; Fluorescent Antibody Technique, Indirect / veterinary; Lens, Crystalline / metabolism; Microscopy, Fluorescence / veterinary
TL;DR:
There are significant differences in the characteristics of ferritin H-chain and its distribution in canine cataractous lenses compared with noncataractsous lenses, which allows this molecule to sequester more iron.
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UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
PURPOSE To determine potential differences in the characteristics of the iron storage protein ferritin and its heavy (H) and light (L) subunits in fiber cells from cataractous and noncataractous lenses of older dogs. METHODS Lens fiber cell homogenates were analyzed by SDS-PAGE, and ferritin chains were immunodetected with ferritin chain-specific antibodies. Ferritin concentration was measured by ELISA. Immunohistochemistry was used to localize ferritin chains in lens sections. RESULTS The concentration of assembled ferritin was comparable in noncataractous and cataractous lenses of similarly aged dogs. The ferritin L-chain detected in both lens types was modified and was approximately 11 kDa larger (30 kDa) than standard L-chain (19 kDa) purified from canine liver. The H-chain identified in cataractous fiber cells (29 kDa) differed from the 21-kDa standard canine H-chain and from the 12-kDa modified H-chain present in fiber cells of noncataractous lenses. Histologic analysis revealed that the H-chain was distributed differently throughout cataractous lenses compared with noncataractous lenses. There was also a difference in subunit makeup of assembled ferritin between the two lens types. Ferritin from cataractous lenses contained more H-chain and bound 11-fold more iron than ferritin from noncataractous lenses. CONCLUSIONS There are significant differences in the characteristics of ferritin H-chain and its distribution in canine cataractous lenses compared with noncataractous lenses. The higher content of H-chain in assembled ferritin allows this molecule to sequester more iron. In addition, the accumulation of H-chain in deeper fiber layers of the lens may be part of a defense mechanism by which the cataractous lens limits iron-catalyzed oxidative damage.