[Recent insulin-dependent diabetes: at least 2 daily injections with self-controlled blood sugar].
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Adult↗
Biomedical subjects
R Rosa
Publications and source records attributed to R Rosa.
[Screening for hemoglobinopathies and G6PD deficiencies in Morocco].
Screening for abnormal hemoglobins and G6PD deficiency was conducted in adult and new born Maroccans from Casablanca. The results presented deal with HbS and HbC traits, alpha, gamma, and delta mutations, the presence of detectable amount of Hb Bart's and the G6PD deficiency frequency.
Adult↗
Neurological findings in triosephosphate isomerase deficiency.
Two siblings with hemolytic anemia caused by triosephosphate isomerase deficiency developed a progressive neurological syndrome featuring dystonic movements, tremor, pyramidal tract signs, and evidence of spinal motor neuron involvement. Intelligence was unaffected. The findings in these patients and in 14 previously published cases indicate that neurological manifestations are an integral part of the disorder and suggest that specific structures in the basal ganglia, brainstem, and spinal cord bear the brunt of the pathological process, which does not affect the cerebral cortex.
Anemia, Hemolytic↗
Hereditary triose phosphate isomerase deficiency: seven new homozygous cases.
Seven new homozygous cases of hereditary triosephosphate isomerase (TPI) deficiency have been detected in five unrelated families. Two of the families originate in France, the others from Algeria, Yugoslavia, and Morocco. Only the parents coming from Algeria and Morocco were first cousins. In the other parents no evidence of consanguinity was found. All seven patients exhibited the same symptoms, i.e. hemolytic anemia appearing very early after birth associated with progressive neuromuscular symptoms. Expression of the deficiency is heterogeneous; this had previously been pointed out in the previously reported cases of TPI deficiency. Red cell TPI activity was 3 to 4% of the normal mean in the patients and 50 to 60% in the parents. The latter did not exhibit any clinical symptoms. The levels of red cell glycolytic intermediates and the characteristics of the mutated TPI could be studied in four of the patients only. Substantial increases of red cell dihydroxyacetone phosphate and of fructose 1,6-diphosphate, normal Km of TPI for glyceraldehyde phosphate, and thermoinstability of the enzyme were found. In addition the electrophoretic pattern showed no significant modification of the mobility of the TPI bands, but abnormal decreased staining of the two more anodal bands.
Carbohydrate Epimerases↗
Biochemical and immunological arguments for homology between red cell and liver phosphoglyceromutase isozymes.
Phosphoglyceromutase (2,3-bisphospho-D-glycerate:2- phospho-D-glycerate phosphotransferase, EC 2.7.5.3) from the red cell is compared with the muscle and the liver forms of the enzyme obtained from rabbits. Partially purified samples were used for this study. The electrophoretic mobility of red cell phosphoglyceromutase is completely different from that of muscle and similar to that of liver. The muscle isozyme can hybridize with liver or red blood cell phosphoglyceromutase. N-Ethylmaleimide, an SH group reagent, completely inhibits muscle phosphoglyceromutase activity and slightly inhibits the activity of the enzyme from liver and from red cells. Both liver and red cell isozymes are completely inactivated by heating at 60 degrees C for 15 min, whereas a 25% decrease in inactivity is noted for the muscle enzyme. Finally, chicken antibody directed against human red cell phosphoglyceromutase reacts with the enzyme isolated from rabbit red cells and liver, but not with that obtained from muscle.
Animals↗
Evidence for the presence of a hybrid of phosphoglyceromutase/bisphosphoglyceromutase in the red cells: partial characterization of the hybrid.
Purified phosphoglyceromutase was hybridized in vitro with pure biphosphoglyceromutase . The hybrid showed an electrophoretic mobility identical to that of the intermediate band of red cell phosphoglyceromutase activity in the hemolysate patterns. Electrophoretic tests showed that the partially purified hybrid displayed both bisphosphoglyceromutase and phosphoglyceromutase activities and that the sample contained also a small portion of non-hybrid bisphosphoglyceromutase . By constrast to a non-hybrid mixture of the two purified mutases the hybrid exhibited heat instability of bisphosphoglyceromutase activity and neutralization of phosphoglyceromutase activity by anti- bisphosphoglyceromutase antibody.
Bisphosphoglycerate Mutase↗
Cell-free translation of messenger RNA for human bisphosphoglyceromutase.
mRNAs prepared from different human tissues were translated in a cell-free reticulocyte lysate system and, when present, the neosynthesized bisphosphoglyceromutase ( BPGM ) was specifically isolated by immunoprecipitation and analyzed by polyacrylamide gel electrophoresis. Analysis of the translation products showed that bisphosphoglyceromutase was synthesized in vitro with its mature molecular weight and messenger RNA specifying the synthesis of BPGM exhibited a sedimentation coefficient of 12 S in human reticulocytes. This synthesis seems to be highly tissue specific since we could not evidence any synthesis of this enzyme using mRNA obtained from non erythroid tissue. The BPGM synthesis represents 0.1% of the total neosynthesized non heme proteins in human reticulocyte and ten times less (0.01%) in human fetal liver.
Animals↗
Purification of human erythrocyte phosphoglyceromutase.
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Chromatography, Affinity↗
In vivo effect of volume expansion on rectal gland function. II. Hemodynamic changes.
Intravascular volume expansion causes a 300% increase in the rate of fluid secretion from, and blood flow to, the in vivo rectal gland of the spiny dogfish Squalus acanthias. Similar increases are also observed in explanted rectal glands perfused through a catheter from the dorsal aorta of a volume-expanded dogfish. Stimulation of rectal gland secretion by volume expansion is not associated with a change in the ratio of chloride secreted to oxygen consumed by the rectal gland and the oxygen extraction ratio, suggesting that an increase in blood flow is necessary to support the increased rate of chloride secretion. Perfusion of the explanted gland with bumetanide (10(-4) M) completely inhibits the secretory response to volume expansion but does not prevent the increase in blood flow. Bumetanide also inhibits dibutyryl adenosine 3',5'-cyclic monophosphate- and theophylline-induced increases in chloride secretion but does not inhibit the hyperemic response. Somatostatin inhibits the secretory response of the explanted gland to volume expansion but does not prevent the increase in blood flow. Although an increase in blood flow is necessary to support the increased energy requirement of enhanced transport, the secretory response and the increase in blood flow appear to be independently regulated and mediated, at least in part, by humoral factors.
Animals↗
[Diphosphoglyceromutase deficiency: new cases associated with erythrocytosis].
New cases of diphosphoglyceromutase (DPGM) have been detected, associated with erythrocytosis in two unrelated families. The deficiency appears to be inherited as an autosomal dominant trait. Diphosphoglycerate phosphatase activity paralleled DPGM activity in all the subjects. Three of the latter displayed complete DPGM deficiency with about 0.4% of the normal 2,3-diphosphoglycerate (2,3 DPG) level. The other four showed partial deficiency (about 50% normal mean) with a similar decrease in 2,3-DPG level. The P50 values are in agreement with the red cell 2,3-DPG concentrations. Il all the deficient subjects the ATP level was elevated and the pattern of glycolytic intermediates was disturbed, with an increase in fructose 1,6-diphosphate, triose-phosphates, 3-phosphoglycerate, glucose 1,6-diphosphate, and reduced or normal levels of glucose-6-phosphate and fructose-6-phosphate.
Adult↗
Pattern of pyruvate kinase isozymes in erythroleukemia cell lines and in normal human erythroblasts.
To further investigate the erythroid nature of the two human erythroleukemia cell lines, K562 and HEL-60, and to define the ontogeny of pyruvate kinase (PK) isozymes (R, M2) in developing human erythroid cells, we have studied the isozymic alterations, if any, during differentiation of these cell lines in vitro and normoblasts isolated from fetal liver in vivo. PK activity of erythroleukemic cell lines was intermediate between that observed in leukocytes and in fetal liver erythroblasts. These cell lines contained a high level of M2-PK, but R-PK was always present, albeit at low concentrations, in all the clones or subclones we studied. Erythroblasts from fetal liver were separated according to density on a Stractan gradient. R-PK levels were nearly constant in the different fractions, whereas M2-PK levels markedly decreased as the erythroblasts became mature and almost completely disappeared in late erythroid cells. Thus, these results clearly demonstrate the erythroid origin of these cell lines.
Cell Line↗
Purification of human erythrocyte phosphoglycerate kinase by dye ligand affinity chromatography.
A new method for the purification of human erythrocyte phosphoglycerate-kinase involving affinity chromatography on dye-ligand media (Red A), in the presence of 3-phosphoglycerate and ATP, is described. The method is rapid and technically simple. The purity of the enzyme was verified by electrophoresis in polyacrylamide gel in the presence of sodium dodecylsulphate, by amino acid analysis and by immunoprecipitation in Ouchterlony plates. Peptide mapping of tryptic digests of the purified enzyme was performed and the immunoneutralization of the enzyme activity evaluated with rabbit antibodies.
Chromatography, Affinity↗
Partial characterization of the inactive mutant form of human red cell bisphosphoglyceromutase and comparison with an alkylated form.
The trifunctional enzyme bisphosphoglyceromutase (or diphosphoglycerate mutase) (EC 2.7.5.4) was purified from human red cells and injected into two chickens. Specific anti-bisphosphoglyceromutase antibodies were produced that displayed a single precipitation line on Ouchterlony plates and on immunoelectrophoresis. No cross-reaction of these antibodies was detected with phosphoglyceromutase, the common glycolytic enzyme. Immunoneutralization of bisphosphoglyceromutase and of its two other activities, i.e., bisphosphoglycerate phosphatase and phosphoglyceromutase, was observed for a purified preparation. The anti-bisphosphoglyceromutase antibody reacts with the inactive enzyme present in the hemolysate of a mutant human subject. It also binds bisphosphoglyceromutase inactivated by N-ethylmaleimide, a strong alkylating agent of SH groups. Active bisphosphoglyceromutase is stable at 55 degrees C, whereas the inactive forms of the mutant and of the alkylated hemolysates are thermolabile. These forms can be protected against thermal precipitation by 4 mM 2,3-diphosphoglycerate and 4 mM 3-phosphoglycerate. These findings afford evidence that the binding of the substrates on the bisphosphoglyceromutase molecule is not prevented by alkylation nor by the mutation of the hereditary inactive enzyme.
Alkylation↗
The profile of the glycolytic system and the metabolic activity of chicken erythrocytes.
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Animals↗
Comparative levels between enzymes of the glycolytic pathway from erythrocytes and somatic tissues of the chicken Gallus gallus domesticus.
A comparative study on the glycolytic enzymes from chicken erythrocytes and somatic tissues has been carried out, the results being shown as active units per mg protein in supernatants of 1085, 12,100 and 106,000 g fractionated centrifugation. The profiles of the glycolytic enzymes have been analyzed in terms of their activity relative to hexokinase and as the ratios between pairs of enzymes bearing a product-substrate relationship. Chicken erythrocyte displays a very peculiar profile of glycolytic enzymes. It possesses a FruP2-activated pyruvate kinase of the L isoenzyme type, which does not seem to be the predominant isoenzyme together with the M type, the content in glycolytic enzymes being much lower than in the somatic tissues.
Adenosine Triphosphate↗
Intra-aortic balloon counterpulsation in an experimental model of myocardial infarction.
The efficacy of intra-aortic balloon counterpulsation for heart failure during acute myocardial infarction has been controversial, and early intervention has been suggested as crucial. We have examined this type of therapy in the intact anesthetized dog during complete occlusion of the proximal left anterior descending coronary artery with a balloon-tipped catheter. Group 1 (n = 8) represented untreated animals undergoing four hours of ischemia. Group 2 (n = 7) consisted of animals undergoing counterpulsation with an intra-aortic balloon after 15 minutes of ischemia. Initially, stroke volume and the mean rate of left ventricular fiber shortening were similarly diminished in both groups, while filling pressure rose proportionately. After four hours, the mean rate of fiber shortening, stroke volume, and left ventricular filling pressure rose to a greater extent in untreated compared to treated animals (p less than 0.01). The degree of swelling in ischemic tissue and the number of sites with ST-segment elevation and their sums were comparable in the two groups. Thus, intra-aortic counterpulsation applied early in the course of ischemia can improve global left ventricular dysfunction without affecting the extent of myocardial injury.
Animals↗
A new case of phosphoglycerate kinase deficiency: PGK Creteil associated with rhabdomyolysis and lacking hemolytic anemia.
A new case of phosphoglycerate kinase (PGK) deficiency is described. The propositus displayed episodes of rhabdomyolysis crises and acute renal failure but did not exhibit any sign of hemolysis. A severe deficiency in phosphoglycerate kinase was revealed in muscle and was also found in erythrocytes, white cells and platelets. A partial defect in the same enzyme was present in the mother's and the two daughters' erythrocytes, indicating a X-linked recessive genetic transmission of the enzyme defect. In the propositus, erythrocyte ATP concentration was normal, although 2,3-diphosphoglycerate and triose phosphate levels were moderately increased. Lactate production from glucose, in vitro, was close to normal in intact red cells. The partial PGK was characterized by an increased Km for ADP and more especially for ATP, reduced thermostability, and diminished electrophoretic mobility. Lack of this enzyme, which is a key step in the glycolytic process (generation of one molecule of ATP), is thought to be responsible for rhabdomyolysis, a fact that has not been reported previously.
Acute Kidney Injury↗
Hereditary pyruvate kinase abnormalities associated with erythrocytosis.
A familial erythrocytosis is described. The propositus is a 52-year-old man who was found, on routine testing, to have an erythrocytosis with a Hb level of 19.8 g/dl. Physical examination and laboratory findings revealed an associated hemolysis. The P50 of the stripped hemolysis was normal. The 2,3-DPG level was reduced to 15% of normal but that of ATP was increased more than twofold. Red cell diphosphoglycerate mutase activity was normal as were the levels of all red cell glycolytic and hexose monophosphate shunt enzymes with the exception of pyruvate kinase (PK). The level of the latter was elevated to 24.5 U/g (normal: 6.2 +/- 1.1). The electrophoretic pattern of hemolysate PK was abnormal, showing three additional bands, one of these migrated as the M2 isozyme. The findings were similar in the propositus's daughter and her daughter and in one of the two brothers of the propositus. The second brother and the son of the first brother was exhibited erythrocytosis but their red cell 2,3-DPG levels were normal. In addition, the level of their RBC PK was reduced to between 50% and 60% of normal and the abnormal electrophoretic bands were absent. The erythrocytosis appears to be inherited as an autosomal-dominant trait. The relationship between the PK abnormalities appears complex.
Adenosine Triphosphate↗