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Phosphorylase and Uridine Diphosphoglucose Glycogen Synthetase in the Retina
B. THOMAS HUTCHINSON, M.D.;
TOICHIRO KUWABARA, M.D.
Arch Ophthalmol. 1962;68(4):538-545.
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Since Claude Bernard1 first discovered glycogen in 1857, it has been recognized as the principle storage form of carbohydrate in animal tissues and has been found to occur in more or less abundance in nearly all types of animal cells. Recently Kuwabara and Cogan2 described the distribution of histochemically demonstrable glycogen in the retina and showed its synthesis in vitro. The amount of glycogen varied widely in different species and appeared to be inversely proportional to the vascularity of the retinas. This species variation prompted further study into retinal glycogen metabolism and has resulted in the present report on the activity of phosphorylase and of uridine diphosphoglucose (UDPG) glycogen synthetase in the retina.
Evidence from various sources3-8 now suggests that the UDPG pathway (an irreversible reaction acting in conjunction with amylo-1,4 1,6 transglucosidase or branching enzyme) is responsible for glycogen synthesis in the body and that phosphorylase activity (effecting
. . . [Full Text PDF of this Article]
Author Affiliations
Boston
Howe Laboratory of Ophthalmology, Harvard University Medical School, Massachusetts Eye and Ear Infirmary.
Footnotes
Submitted for publication March 19, 1962.
This investigation was carried out during the tenure of a Postdoctoral Fellowship from the National Institute of Neurological Diseases and Blindness, United States Public Health Service.
The investigation was supported by a U.S. Public Health Service Research Grant B-3015 from the National Institute of Neurological Diseases and Blindness, United States Public Health Service.
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