Changes in the lactate dehydrogenase isoenzyme pattern during differentiation of rabbit bone-marrow erythroid cells

Setchenska, Milka S.; Arnstein, H. R. V.

doi:10.1042/bj1700193

Cited by 20 publications

(4 citation statements)

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“…During development of rabbit bone marrow erythroid cells, changes in the activities of several enzymes have been observed to occur at the time of condensation of the nucleus in orthochromatic erythroblasts (Denton et al, 1975;Hulea et al, 1975;Spencer & Peller, 1976;Hulea & Arnstein, 1977;Setchenska & Arnstein, 1978. In the present study, we have found that the activity of (results not shown).…”

Section: Discussionsupporting

confidence: 57%

“…If the hormonal signal for erythroid cell differentiation acts through the adenylate cyclase/cyclic AMP/protein kinase system, the disappearance of the response of adenylate cyclase to erythropoietin may be related to the life-time of the receptors (Vassileva-Popova & Yanev, 1975). The decrease in phosphodiesterase activity is probably due to cessation of the synthesis of the relevant messenger RNA following condensation of the nucleus in orthochromatic erythroblasts (Denton & Arnstein, 1973), as well as to protein degradation, which has been shown to be a selective process (Setchenska & Arnstein, 1978) and thus could preferentially affect specific enzymes.…”

Section: Discussionmentioning

confidence: 99%

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Cyclic AMP phosphodiesterase activity during differentiation of rabbit erythroid bone marrow cells

Setchenska¹,

Arnstein²,

Vassileva-Popova³

1981

Biochemical Journal

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Changes in the activity of cyclic AMP phosphodiesterase during differentiation of rabbit bone marrow erythroid cells were investigated. The cells were separated by velocity sedimentation at unit gravity into six fractions corresponding to different stages of development: proerythroblasts, basophilic cells, polychromatic cells, early orthochromatic and late orthochromatic cells and reticulocytes. Cyclic AMP phosphodiesterase was found to be very active in the most immature cells, the proerythroblasts, which also have the highest content of cyclic AMP. After differentiation into basophilic erythroblasts, a 4-fold decrease in cyclic AMP phosphodiesterase activity was observed. In these cells the amount of cyclic AMP was about 80% lower than that in proerythroblasts. In polychromatic cells a further drop in phosphodiesterase activity occurred. After the final cell division the enzyme activity was very low and the levels of cyclic AMP in the early and late orthochromatic cells remained constant. Kinetic studies demonstrated a heterogeneity of erythroid cell cyclic AMP phosphodiesterase: high affinity, low-Km (5.5 X 10(-6) M) and low affinity, high-Km (0.1 X 10(-3) M) enzymes were found. The phosphodiesterase activity was dependent on the presence of Mg2+ and was activated by Ca2+ at low Mg2+ concentrations (1 mM). The changes in cyclic AMP phosphodiesterase activity during differentiation and maturation of erythroid cells suggest the possible importance of this enzyme in the physiological control of cyclic AMP concentrations in developing erythroblasts. The loss of cyclic AMP phosphodiesterase activity after cessation of cell division supports the concept of the significance of the final cell division in erythroblast differentiation.

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Section: Discussionsupporting

confidence: 57%

Section: Discussionmentioning

confidence: 99%

Cyclic AMP phosphodiesterase activity during differentiation of rabbit erythroid bone marrow cells

Setchenska¹,

Arnstein²,

Vassileva-Popova³

1981

Biochemical Journal

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“…Lactate dehydrogenase activity was determined by activity against 0.66 mM sodium pyruvate in the presence of 100 mM Hepes, pH 7.6, and 0.13 mM NADH at 25°C. Oxidation of NADH was measured by the change of absorbance at 340 nm (20). Glucose-6-phosphate dehydrogenase activity was determined against 3.3 mM glucose-6-phosphate in the presence of 50 mM Tris, pH 7.8, 3 mM MgCl 2 , and 0.2 mM NADP at 25°C.…”

Section: Methodsmentioning

confidence: 99%

A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis

Song

Lee

2008

Journal of Biological Chemistry

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The biogenesis of cytosolic iron-sulfur (Fe-S) proteins in mammalian cells is poorly understood. In Saccharomyces cerevisiae, there is a pathway dedicated to cytosolic Fe-S protein maturation that involves several essential proteins. One of these is Nar1, which intriguingly is homologous to iron-only hydrogenases, ancient enzymes that catalyze the formation of hydrogen gas in anaerobic bacteria. There are two orthologues of Nar1 in mammalian cells, iron-only hydrogenase-like protein 1 (IOP1) and IOP2 (also known as nuclear prelamin A recognition factor). We examined IOP1 for a potential role in mammalian cytosolic Fe-S protein biogenesis. We found that knockdown of IOP1 in both HeLa and Hep3B cells decreases the activity of cytosolic aconitase, an Fe-S protein, but not that of mitochondrial aconitase. Knockdown of IOP2, in contrast, had no effect on either. The decrease in aconitase activity upon IOP1 knockdown is rescued by expression of a small interference RNA-resistant version of IOP1. Upon loss of its Fe-S cluster, cytosolic aconitase is known to be converted to iron regulatory protein 1, and consistent with this, we found that IOP1 knockdown increases transferrin receptor 1 mRNA levels and decreases ferritin heavy chain protein levels. IOP1 knockdown also leads to a decrease in activity of xanthine oxidase, a distinct cytosolic Fe-S protein. Taken together, these results provide evidence that IOP1 is involved in mammalian cytosolic Fe-S protein maturation. Iron-sulfur (Fe-S)2 proteins play an essential role in multiple physiologic processes, including electron transport, enzyme catalysis, and regulation of gene expression (1). Among the most studied of these proteins are those involved in mitochondrial oxidative phosphorylation, but it is clear that these proteins are present in other cellular compartments, including the cytoplasm and nucleus. The synthesis and maturation of Fe-S proteins in eukaryotes is complex, and much of our current understanding of this pathway derives from studies in yeast (2). The central elements of this pathway are as follows. The cysteine desulfurase Nfs1 (also known as IscS) removes sulfur from the amino acid cysteine. This sulfur is then combined with iron to form Fe-S clusters. These clusters, which can take on many forms, including [2Fe-2S] and [4Fe-4S] clusters, are then combined with apoproteins, resulting in Fe-S proteins. The initial steps of the pathway, including the desulfuration of cysteine and assembly of Fe-S clusters, occur within the mitochondrion. Thus, defects in mitochondrial Fe-S assembly impact Fe-S proteins not only in the mitochondrion but also in the cytosol. The Fe-S clusters are then transported to the appropriate compartments for subsequent assembly of the mature Fe-S proteins. A substantial amount is known about the initial steps. Less is known of the compartment-specific assembly. In yeast, a cytoplasmic iron-sulfur protein assembly pathway has been characterized (3). This pathway comprises at least four distinct proteins: cytosolic Fe-S cluster-defi...

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“…This correlation may be explained if young red blood cells have high levels of LDH. However, Setchenska et al (1978) reported that in erythroblast cells only the LDH 5 iso-enzyme was present. Fetuses with an LDH value greater than 400 units also had thrombocytopenia and increased AST values, which are signs of chronic stress.…”

Section: Discussionmentioning

confidence: 99%

Fetal lactic dehydrogenase variation in normal pregnancy and in cases of severe intra-uterine growth restriction

Verspyck

Gaillard

Parnet³

et al. 1999

Prenat. Diagn.

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Physiological and pathological fetal levels of lactic dehydrogenase (LDH), including its five different iso‐enzymes are still poorly known. Our objectives were to compare total LDH levels and its five iso‐enzymes between a control group of healthy fetuses and a group of fetuses with severe intra‐uterine growth restriction (IUGR), and to determine the biochemical associations and the prognostic value of elevated LDH activity in fetuses with IUGR. Total LDH levels, haematologic values and liver enzyme activities were measured in 108 healthy fetuses from 17 to 37 weeks of gestation and in 44 fetuses with severe IUGR. Total fetal LDH in plasma from the healthy fetuses were constant throughout pregnancy (mean (SD)=305·09 (46·97)). Total LDH values in plasma significantly increased in cases of IUGR (p=0·003), and the degree of increase was significantly correlated with fetal erythroblastosis (n=44, r=0·80, p<0·001). LDH 5 significantly decreased in the IUGR group (p=0·03). Total LDH values strictly above 400IU/l (a value equal to the mean+2SD in the healthy fetus group) were found to be significantly associated with thrombocytopenia (p<0·001), erythroblastosis (p=0·008) and an increase in AST value (p=0·03). These results suggest that the fetal LDH value in plasma is a useful biological marker for severe chronic distress. Copyright © 1999 John Wiley & Sons, Ltd.

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Changes in the lactate dehydrogenase isoenzyme pattern during differentiation of rabbit bone-marrow erythroid cells

Cited by 20 publications

References 21 publications

Cyclic AMP phosphodiesterase activity during differentiation of rabbit erythroid bone marrow cells

Cyclic AMP phosphodiesterase activity during differentiation of rabbit erythroid bone marrow cells

A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis

Fetal lactic dehydrogenase variation in normal pregnancy and in cases of severe intra-uterine growth restriction

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