Glycolytic enzymes in polyamine-treated bovine retina

Title:

Glycolytic enzymes in polyamine-treated bovine retina

Creator:

Venza, I., Valenti, A., Ruggeri, P., Denaro, L., and Teti, D.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:55debbe9-59a0-4524-82f2-d79befad4488
uuid:55debbe9-59a0-4524-82f2-d79befad4488
issn:0862-8408

Subject:

Fyziologie člověka a srovnávací fyziologie, polyaminy, sítnice, polyamines, retina, LDH isoenzymes, MDH isoenzymes, 14, and 612

Type:

article, články, model:article, and TEXT

Format:

print, bez média, and svazek

Description:

The retina is characterized by glycolysis under aerobic conditions, mediated by lactate dehydrogenase isoenzyme-5 (LDH-5) as well as by the soluble isoenzyme of malate dehydrogenase. Bovine retina LDH and MDH isoenzymes and their activities were studied after polyamine treatment. Our results showed that LDH-5 isoenzyme presented the highest activity in untreated as well as in putrescine-treated retina. Decreased activity was present when the retina was treated with spermidine or spermine. It was demonstrated that retinic LDH-5 had a high affinity for lactate which enabled the isoenzyme to be more effective than the other LDH isoenzymes in the conversion of NADH to NAD. Therefore, the putrescine enhancing LDH-5 activity appeared to be capable of stimulating NAD-mediated rhodopsin regeneration. Putrescine induced a marked increase of both MDH isoenzymes - soluble (s-MDH) and mitochondrial (m-MDH), while spermine and spermidine mostly affected the soluble form of the enzyme. Putrescine induced a three-fold increase in s-MDH and m-MDH activities, while spermine and spermidine induced a four to five-fold increase in s-MDH. These results document the differential effects of polyamine treatment on LDH and MDH isoenzyme activities., I. Venza, A. Valenti, P. Ruggeri, L. Denaro, D. Teti., and Obsahuje bibliografii

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 2000 Volume:49 | Number:2

Harvested from:

CDK

Metadata only:

false