Investigations of the Enzymes Involved in the Fructose Breakdown in the Cattle Lens

Bibliographic Data

ID23540352
AuthorsMarguerite Schinkel (0000-0001-5804-5701, corresponding author), Christian Ohrloff, Stephan Zierz, Otto Hockwin
Year2009
Volume14
Issue3
Pages221-229
Publication date2009-12-04
Peer ReviewedYes
Open AccessYes
TypeARTICLE
VenueOphthalmic Research (JOURNAL)
Journal identifiersISSN: 0030-3747 • E-ISSN: 1423-0259
PublisherS. Karger AG (PUBLISHER • CH)
DOI10.1159/000265196
OpenAlexW6285247
LanguageEN
Citations received11

By introducing fructose into the glycolysis, it is possible to stimulate ATP formation. As is the case in animal experiments, in human lenses, too, the first step is the phosphorylation to fructose-1-phosphate via the enzyme ketohexokinase. The present investigation deals with the question whether enzymes present in the lens are responsible for the further steps in fructose degradation. Particularly the aldolase isoenzyme C splits fructose-1-phosphate into glyceraldehyde and dihydroxyacetone phosphate in the same way as in glucose catabolism. Dihydroxyacetone phosphate can further be directly degraded and thus utilized to ATP formation. From glyceraldehyde, glycerol (aldose reductase) or glycerate (aldehyde dehydrogenase) can be formed. The presence of triosekinase, which phosphorylates glyceraldehyde directly to glyceraldehyde-3-phosphate, could only be determined in the lens tissue of young animals. The presence of glycerokinase (glycerol → glycerophosphate) could not be verified. Thus, in the old lens tissue 1 ATP molecule net per fructose molecule can be formed. In older age, the glucose breakdown is limited by hexokinase and phosphofructokinase, so that the glucose, after transformation via the sorbitol pathway to fructose, can also be utilized for the energy metabolism.

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