d-GIycerate

Kattermann, R; Holldorf, August; Holzer, Helmut

doi:10.1016/b978-0-12-395630-9.50048-7

Cited by 5 publications

(6 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Once obstruction had lasted for some time a decrease in LCAT activity could be measured. These results would support animal experiments by Kattermann and Wolfrum [15] and Calandra et al [16] who found only little change or even activation of LCAT activity in rats after administration of u-naphthyl-iso thiocyanate or after obstruction by ligation of the bile duct. I n these experiments a fall in the LCAT activity occurred 21 days after the obstruction.…”

Section: Discussionsupporting

confidence: 89%

See 1 more Smart Citation

Serum Cholesterol Esterification in Liver Disease. Combined Determinations of Lecithin: Cholesterol Acyltransferase and Lipoprotein‐X

Wengeler¹,

Greten²,

Seidel³

1972

Eur J Clin Investigation

View full text Add to dashboard Cite

Indirect evidence suggests that lecithin : cholesterol acyltransferase (LCAT) is synthesized in the liver. There are, however, controversial reports in the literature correlating LCAT activity with various forms of liver disease. The purpose of this study was to determine LCAT activity in icteric patients. These were classified not only by the aonventional methods, but also with respect to the presence or absence of LP-X, an abnormal plasma lipoprotein, highly specific for demonstrating or excluding cholestasis. LCAT was measured a t different stages of the disease. The patients were divided into 4 groups: I. Hepatitis with cholestasis (LP-X pos.) [li]; 11. Hepatitis without cholestsis (LP-X neg.) [12]; 111. Extrahepatic biliary obstruction (LP-9 pos.) [lo]; IV. Chronic liver failure (LP-5 neg./pos.) [ll]. Compared to normal controls [lJ], patients from group I had low, group I1 had normal, group I11 had normal and group IV had low LC$T activity.In vitro studies clearly excluded the existence of circulating inhibitors of LCST. From these data it is suggested that the ratio of esterified to unesterified cholesterol in liver disease depends on two factors: LCXT activity and the occurrence of the abnormal lipoprotein-X. Furthermore these results indicate that combined determinations of LCAT and LP-X may prove to be useful techniques for differentiating intra-and extrahepatic cholestasis.K e y words: LCAT. LP-S, lipids in liver disease.

show abstract

Section: Discussionsupporting

confidence: 89%

“…Lecithin : cholesterol acyltransferase (LCAT) activity in serum was measured in a control group of 15 healthy volunteers (aged 20 to 49 years). None of these volunteers had abnormal liver function tests and both their lipid levels as well as their lipoprotein patterns were within the normal range.…”

Section: Materials and Methods Patientsmentioning

confidence: 99%

Serum Cholesterol Esterification in Liver Disease. Combined Determinations of Lecithin: Cholesterol Acyltransferase and Lipoprotein‐X

Wengeler¹,

Greten²,

Seidel³

1972

Eur J Clin Investigation

View full text Add to dashboard Cite

show abstract

“…Since D-glycerate dehydrogenase works equally well with either NAD or NADP in both directions, one of its functions might well be that of transhydrogenase catalysing the transfer of reducing units from NADPH to NAD with hydroxypyruvate and Dglycerate acting in catalytic amounts. Both these substances have been reported to be present in animal tissues (Holzer & Holldorf, 1957b;Kattermann, Dold & Holzer, 1961). Another function of the soluble D-glycerate dehydrogenase might be to act in conjunction with the mitochondrial D-ahydroxy acid dehydrogenase as a shuttle system for the transfer of reducing units from the cytoplasm to the respiratory chain with the regeneration of oxidized NAD.…”

Section: Discussionmentioning

confidence: 99%

THE OXIDATION OF d- AND l-GLYCERATE BY RAT LIVER

Dawkins¹,

Dickens²

1965

Biochemical Journal

View full text Add to dashboard Cite

1. The interconversion of hydroxypyruvate and l-glycerate in the presence of NAD and rat-liver l-lactate dehydrogenase has been demonstrated. Michaelis constants for these substrates together with an equilibrium constant have been determined and compared with those for pyruvate and l-lactate. 2. The presence of d-glycerate dehydrogenase in rat liver has been confirmed and the enzyme has been purified 16-20-fold from the supernatant fraction of a homogenate, when it is free of l-lactate dehydrogenase, with a 23-29% recovery. The enzyme catalyses the interconversion of hydroxypyruvate and d-glycerate in the presence of either NAD or NADP with almost equal efficiency. d-Glycerate dehydrogenase also catalyses the reduction of glyoxylate, but is distinct from l-lactate dehydrogenase in that it fails to act on pyruvate, d-lactate or l-lactate. The enzyme is strongly dependent on free thiol groups, as shown by inhibition with p-chloromercuribenzoate, and in the presence of sodium chloride the reduction of hydroxypyruvate is activated. Michaelis constants for these substrates of d-glycerate dehydrogenase and an equilibrium constant for the NAD-catalysed reaction have been calculated. 3. An explanation for the lowered V(max.) with d-glycerate as compared with dl-glycerate for the rabbit-kidney d-alpha-hydroxy acid dehydrogenase has been proposed.

show abstract

“…by specifically altering the accumulation of each of the three classes of pathological compounds. As for fructose loading, it is known that Dglyceric acid is a fructose metabolite located after the socalled D-glyceraldehyde crossroad (Figure 1) (Hue and Hers, 1972), and it has been shown both on rats and pigs that fructose and D-glyceraldehyde loading lead to accumulation of D-glyceric acid in liver tissue (Kattermann et al, 1961;Sestorf et al, 1972). It is therefore reasonable to assume that the increase in Dglyceric acid excretion after fructose loading is caused by a direct conversion of fructose to D-glyceric acid.…”

Section: Discussionmentioning

confidence: 96%

In vivostudies on the metabolic derangement in a patient with D‐glyceric acidaemia and hyperglycinaemia

Kølvraa

Gregersen

Christensen

1983

J of Inher Metab Disea

View full text Add to dashboard Cite

In a mentally retarded boy, who excreted elevated amounts of glycine, D-glyceric acid and acylglycines and whose cells exhibited diminished D-glycerate dehydrogenase and glycine cleavage activity, investigations have been undertaken aiming at characterizing the relationship between the different accumulations. This was done in vivo by trying in a specific manner to alter in turn the degree of accumulation of each of the three classes of compounds and then monitoring changes in the others. The results suggest, that the D-glyceric acid accumulation is directly caused by the genetic defect, since the D-glyceric acid excretion was not altered by changes in degree of accumulation of either glycine or acylglycines. Similarly alterations in acylglycine excretion caused alterations in glycine but not in D-glyceric acid excretion. Based on these findings a model for the pathogenesis behind the accumulations of acylglycines and glycine is proposed.

show abstract

d-GIycerate

Cited by 5 publications

References 3 publications

Serum Cholesterol Esterification in Liver Disease. Combined Determinations of Lecithin: Cholesterol Acyltransferase and Lipoprotein‐X

Serum Cholesterol Esterification in Liver Disease. Combined Determinations of Lecithin: Cholesterol Acyltransferase and Lipoprotein‐X

THE OXIDATION OF d- AND l-GLYCERATE BY RAT LIVER

In vivostudies on the metabolic derangement in a patient with D‐glyceric acidaemia and hyperglycinaemia

Contact Info

Product

Resources

About