Enzymatic test for the detection of a riboflavin deficiency. NADPH-dependent glutathione reductase of red blood cells and its activation by FAD in vitro

Glatzle, D; Weber, F.; Wiss, Ø.

doi:10.1007/bf02147797

Cited by 98 publications

(32 citation statements)

References 6 publications

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“…A significant difference was noted between control and chlorpromazine-treated groups at both time periods in the activity determined after incubation with cofactor FAD in vitro, and in the activity coefficient, i.e., ratio of enzyme activity with to that without addition of FAD in vitro. The significant increase in the activity coefficient of glutathione reductase in the chlorpromazine-treated animals is in the same direction as that observed with dietary riboflavin deficiency (23,24). Thus, the chronic administration ofa relatively low dose of chlorpromazine produces changes in riboflavin homeostasis that are detectable by assays that are utilized to assess riboflavin deficiency clinically.…”

Section: Resultsmentioning

confidence: 55%

“…In addition, it is of interest that riboflavin metabolism in the animal as a whole appears to be disturbed in animals treated with a low dose of chlorpromazine for a 3-or 7-wk period. The ratio of the activity of erythrocyte glutathione reductase after incubation with its cofactor FAD in vitro to the activity prior to incubation (activity coefficient) has been widely used as an index of riboflavin deficiency (20,23,24). Greater than normal augmentation of activity after incubation with FAD in vitro is thought to reflect undersaturation of the apoenzyme with its cofactor due to decreased riboflavin intake (20).…”

Section: Discussionmentioning

confidence: 99%

“…Elevated glutathione reductase activity has been observed in a variety of diverse conditions, including iron deficiency (30), cobalt deficiency (31), glucose-6-phosphate dehydrogenase deficiency (29), cancer (32), uremia (23), and cirrhosis of the liver (33). It is the elevated activity coefficient, not the basal level, that appears to be the most reliable index of riboflavin deficiency (20,24).…”

Section: Discussionmentioning

confidence: 99%

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Inhibition of Riboflavin Metabolism in Rat Tissues by Chlorpromazine, Imipramine, and Amitriptyline

Pinto¹,

Huang²,

Rivlin³

1981

J. Clin. Invest.

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A B S T R A C T Prompted by recognition of the similar structures of riboflavin (vitamin B2), phenothiazine drugs, and tricyclic antidepressants, our studies sought to determine effects of drugs of these two types upon the conversion of riboflavin into its active coenzyme derivative, flavin adenine dinucleotide (FAD) in rat tissues. Chlorpromazine, a phenothiazine derivative, and imipramine and amitriptyline, both tricyclic antidepressants, each inhibited the incorporation of [14C]riboflavin into [14C]FAD in liver, cerebrum, cerebellum, and heart. A variety of psychoactive drugs structurally unrelated to riboflavin were ineffective. Chlorpromazine, imipramine, and amitriptyline in vitro inhibited hepatic flavokinase, the first oftwo enzymes in the conversion ofriboflavin to FAD.Evidence was obtained that chlorpromazine administration for a 3-or 7-wk period at doses comparable on a weight basis to those used clinically has significant effects upon riboflavin metabolism in the animal as a whole: (a) the activity coefficient of erythrocyte glutathione reductase, an FAD-containing enzyme used as an index of riboflavin status physiologically, was elevated, a finding compatible with a deficiency state, (b) the urinary excretion of riboflavin was more than twice that of age-and sex-matched pair-fed control rats, and (c) after administration of chlorpromazine for a 7-wk period, tissue levels of flavin mononucleotide and FAD were significantly lower than those of pair-fed littermates, despite consumption of a diet estimated to contain 30 times the recommended dietary allowance. The present study suggests that certain psychotropic drugs interfere with riboflavin metabolism at least in part by inhibiting the conversion of riboflavin to its coenzyme derivatives, and that as a consequence of such inhibition, the overall utilization of the vitamin is impaired.Dr. Pinto is a recipient of a Future Leaders Award of The

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Section: Resultsmentioning

confidence: 55%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Inhibition of Riboflavin Metabolism in Rat Tissues by Chlorpromazine, Imipramine, and Amitriptyline

Pinto¹,

Huang²,

Rivlin³

1981

J. Clin. Invest.

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“…EFFECT OF ENZYME ACTIVATORS Dithioerythritol was included in the reaction mixture to a final concentration of 2 mmol/l and had no significant effect on the activity of the serum enzyme. FAD has been shown to activate red cell GR (Glatzle et al, 1968;Beutler, 1969). Inclusion of FAD in the reaction mixture up to a final concentration of 10 ,umol/l (concentrations above this were slightly inhibitory) had no effect on 37 of 38 randomly selected sera.…”

Section: Materials Andmentioning

confidence: 97%

An optimized semi-automatic rate method for serum glutathione reductase activity and its application to patients with malignant disease.

Delides¹,

Spooner²,

Goldberg³

et al. 1976

J Clin Pathol

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An improved and optimized method for serum glutathione reductase is described. The reference range for normal subjects is 47-79 IU/1. The method is more sensitive than conventional enzyme tests in the detection of malignant disease. It was not raised more frequently in patients with clinical evidence of metastases than in those clinically free of such metastases, and it did not seem to correlate with prognosis among those patients who failed to survive six months from the time the analysis was first conducted.

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“…The red-cell glutathione reductase enzyme stimulation test described by Glatzle [31,32] has proved a reliable test of riboflavin status and a better measure of riboflavin deficiency than the presence of clinical lesions. Nevertheless, the presence of clinical signs of riboflavin deficiency backed up by the enzyme stimulation test is still a useful procedure for assessing the riboflavin status in a community [33], and a modification of the method is currently being used in the UK National Diet and Nutrition Survey to assess the population riboflavin status.…”

Section: Historymentioning

confidence: 99%

The Discovery and Characterization of Riboflavin

Northrop-Clewes¹,

Thurnham

2012

Ann Nutr Metab

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The first observation of a pigment in milk with yellow-green fluorescence can be traced to the English chemist Alexander Wynter Blyth in 1872, but it was not until the early 1930s that the substance was characterized as riboflavin. Interest in accessory food factors began in the latter half of the 19th century with the discovery of the first vitamin, thiamin. Thiamin was water soluble and given the name vitamin B₁. However, researchers realized that there were one or more additional water-soluble factors and these were called the vitamin B-2 complex. The search to identify these accessory food factors in milk, whole wheat, yeast, and liver began in the early 1900s. As there is no classical nutritional disease attributable to riboflavin deficiency, it was the growth-stimulating properties of the food extracts given to young rats that provided the tool with which to investigate and eventually extract riboflavin. Riboflavin was the second vitamin to be isolated and the first from the vitamin B-2 complex; the essential nature of the vitamin as a food constituent for man was shown in 1939.

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Enzymatic test for the detection of a riboflavin deficiency. NADPH-dependent glutathione reductase of red blood cells and its activation by FAD in vitro

Cited by 98 publications

References 6 publications

Inhibition of Riboflavin Metabolism in Rat Tissues by Chlorpromazine, Imipramine, and Amitriptyline

Inhibition of Riboflavin Metabolism in Rat Tissues by Chlorpromazine, Imipramine, and Amitriptyline

An optimized semi-automatic rate method for serum glutathione reductase activity and its application to patients with malignant disease.

The Discovery and Characterization of Riboflavin

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