Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.10.1 (ERK)
 95,504 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In 130 pregnant women (41 without complications, 40 with prematurity, 49 with EPH-Gestosis) Serumferritin, ferrochelatase (FCH), delta-aminolaevulinic-aciddehydratase (D-ALA-D), porphobilinogendeaminase (PBG-D) as well as hematologic routine parameters were measured. Regarding serumferritin, both uncomplicated and cases with pathologic conditions revealed a significant decrease in group II (28th week of pregnancy) as compared to group I (12th to 28th week of pregnancy). Women with EPH-Gestosis showed the lowest values. Activities of hemesynthesizing enzymes did not show any significant differences, neither between the two groups nor between uncomplicated and pathologic cases. Compared to healthy, non pregnant women; in pregnant women we found a significant increase in D-ALA-D and PBG-D, but a significant decrease in FCH. Enzyme pattern in pregnancy reveals an increased synthesis of porphobilinogen and an increased conversion of porphobilinogen to porphyrin. The low activity of FCH we measured in our study could be a reason for the elevation of free protoporphyrin in the erythrocytes.
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PMID:[Heme synthesis and iron status in pregnancy]. 29 36

A diapause associated protein was electrophoretically isolated from the hemolymph of diapausing last instar larvae of the pink bollworm Pectinophora gossypiella. This protein (M(r) approximately 490,000, glycolipoprotein) was given the name Pectinophora diapause protein (PDP). It is composed of one subunit (M(r) 103,000). The concentration of PDP increased dramatically in the hemolymph of diapausing larvae from 17.4% in prediapause (PD) phase to 29.2% in early diapause (ED) phase reaching a level of 38.6% in larval hemolymph of middiapause (MD) phase. The concentrations of total proteins in the hemolymph of active feeding (A), PD, ED, and MD larvae were 69.8, 106,6, 113.3, and 118 mg/ml, respectively, while those in the fat body of the same larvae were 7.1, 7.4, 8.8, and 4.5 mg/g, respectively. In Pectinophora a drop in the concentration of fat body proteins coincided with a corresponding increase in hemolymph proteins, which suggests an active release of protein from the fat body into the hemolymph during the development of diapause. A partial amino acid sequence of pectinophorin showed the first 15 amino acids starting from the amino terminus of the peptide chain: N-ALA-LYS-THR-ILEU-VAL-GLU-ASN-MET-PRO-PRO-THR-PRO-LEU-ASN-ALA-C.
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PMID:A diapause associated protein of the pink bollworm Pectinophora gossypiella Saunders. 142 41

1. The present work undertakes a comparative study on the hexachlorobenzene (HCB) porphyria induction in female rats of Wistar and CHBBTHOM strains. The purpose was to characterize the CHBBTHOM strain with respect to the haem metabolic pathway, its regulatory mechanisms and its response to foreign drugs. 2. After 7 weeks of treatment it was observed that the hepatic porphyrins increased 140 times, ALA-synthase 4 times and PCL was 73% inhibited in the Wistar strain. 3. On the other hand the animals of CHBBTHOM strain showed lesser alteration on these parameters; hepatic porphyrins increased only 3-fold, ALA-synthase 1.7-fold and PLC was only 22% inhibited. 4. Total iron liver content was nearly equal in both strains of rats. 5. The results obtained would indicate that the lower susceptibility of the CHBBTHOM strain to acquire porphyria does not seem to be due to either: (1) congenital alterations of any parameters of the haem metabolic pathway, since the behaviour of normal animals from both strains was similar; or (2) a lower hepatic iron content in such animals. 6. These findings would suggest that the differential response to HCB to this strain would be looked for in another metabolic pathway, such as that involved in the metabolization process of the toxic.
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PMID:Influence of the strain of rats on the induction of hexachlorobenzene induced porphyria. 274 8

The caudate-putamen (CDp) and the globus pallidus (GP) are sites rich in both leucine (LEU) and methionine-enkephalin (MET-ENK) and in ENK receptors. Since chemical and electrolytic lesions of the CDp and GP result in a reduction in ENKs and their receptors and in motor asymmetry, there may be a role for CDp and GP ENKs in rotational behavior and bodily asymmetry. To test this possibility, various doses of D-ALA-2-LEU-ENK, D-ALA-2-MET-ENK, naloxone and naltrexone were injected into the CDp and GP through chronically implanted cannulae. The injections of MET and LEU-ENK caused dose-dependent ipsiversive rotations while injections of naloxone and naltrexone caused contraversive rotations. All of the drug injections also caused bodily asymmetries which were in the same direction as the circling. Intraperitoneal injections of naloxone dose-dependently blocked the rotational behavior induced by the most effective dose of the ENKs used. ENK injections into sites adjacent to the CDp and GP (i.e., cortex, nucleus accumbens and the region bordering the bed nucleus of the stria terminalis and the bed nucleus of anterior commissure) failed to produce any significant circling. These results clearly suggest that CDp and GP ENKs cause ipsiversive rotational behavior and bodily asymmetry and must be considered as one element of the control exerted by the basal ganglia over the motor system.
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PMID:Asymmetric behavior induced by enkephalinergic agents in the basal ganglia. 405 7

A total of 34 cancer patients, all of them subjected to radical surgery of the stomach or large bowel were studied. Group I (n = 5) received during the first postoperative days total parenteral nutrition with a caloric support of 35-45 kcal/kg/day and 12,5 gr N in a 8,5% L-aminoacid solution (Freamine II). Group II (n = 9) received an isotonic solution of 3% L-aminoacid without caloric support. Serum amino acids (AA) were determined daily (Perkin-Elmer KLA-1 Analyzer), as well as nitrogen balance (NB) and serum albumin (Alb) on the preoperative, 1st, and 6th postoperative day: Both groups experienced a progressive increase of serum AA during the period of study. Group II showed levels of branched-AA significantly higher than group I, as well as the total of essential-AA. MET, GLY and PHE were considerably elevated in both groups. ALA did not change in group I showing subnormal values in group II. NB was significantly higher in group I, but none of the groups studied has recovered the initial values of Alb after six days of treatment.
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PMID:[Effect of energy administration on the amino acid level in the postoperative phase]. 642 37

Serum gastrin I (GLU-GLY-PRO-TRYP-LEU(GLU)6-ALA-[formula, see text]-GLY-TRY-MET-ASP-PHE-CO-NH2) concentrations were investigated by radioimmunoassay in 50 mothers and their newborn infants immediately after birth. The mean serum gastrin concentration in maternal blood was 52.80 +/- 13.37 (SD) pg/ml, and in cord blood 84.12 +/- 42.90 (SD) pg/ml. Both values were significantly higher than serum gastrin levels found in normal, healthy, nonpregnant women (Mean +/- SD = 32.34 +/- 18.35 pg/ml). There were no statistically significant differences in the cord serum gastrin concentrations with respect to sex, weight and length of the infant and age and parity of the mother.
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PMID:Serum gastrin I concentrations of mother and newborn immediately after birth. 745 1

The determination of plasma and whole blood free amino acid concentrations in arterial and portal venous blood during post prandial state in the rat was used to estimate the role of the erythrocytes in amino acid exchanges. The erythrocyte contents were calculated from plasma, whole blood concentrations and the hematocrit. The veno-arterial concentration differences in plasma were significant for all amino acids except a-aminobutyrate and ornithine whereas in the erythrocytes only 8 amino acids exhibit significant differences (ASP, ALA, VAL, MET, ILE, LEU, TYR, PHE). For 6 amino acids, a significant correlation between the plasma and the erythrocyte concentration has been found (VAL, ILE, LEU, TYR, PHE, HIS). These data suggest that in vivo during the time of contact between blood and organ tissues, some amino acids but not all are significantly taken up by the erythrocytes. Thus, it may be concluded that erythrocyte amino acid blood transport in arterio-venous portal exchanges, concerns particularly tyrosine and essential amino acids. The erythrocyte amino acid transport represents quantitatively about 20 per cent of the total blood transport.
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PMID:Role of the plasma and erythrocytes in veno-arterial portal changes during post prandial state in the rat. 978 55

D-aspartate (D-Asp) uptake by suspensions of cerebral rat brain astrocytes (RBA) maintained in long-term culture was studied as a means of characterizing function and regulation of Glutamate/Aspartate (Glu/Asp) transporter isoforms in the cells. A-asp influx is Na+-dependent with Km = 5 microm and Vmax = 0.7 nmoles x min(-1) x mg protein-1. Influx is sigmoidal as f[Na+] with Na+Km approximately 12 microm and Hill coefficient of 1.9. The cells establish steady-state D-Asp gradients >3,000-fold. Phorbol ester (PMA) enhances uptake, and gradients near 6,000-fold are achieved due to a 2-fold increase in Vmax, with no change in Km. At initial [D-Asp] = 10 microm, RBA take up more than 90% of total D-Asp, and extracellular levels are reduced to levels below 1 microm. Ionophores that dissipate the Delta(mu)Na+ inhibit gradient formation. Genistein (GEN, 100 microm), a PTK inhibitor, causes a 40% decrease in d-Asp. Inactive analogs of PMA (4alpha-PMA) and GEN (daidzein) have no detectable effect, although the stimulatory PMA response still occurs when GEN is present. Further specificity of action is indicated by the fact that PMA has no effect on Na+-coupled ALA uptake, but GEN is stimulatory. d-Asp uptake is strongly inhibited by serine-O-sulfate (S-O-S), threohydroxy-aspartate (THA), L-Asp, and L-Glu, but not by D-Glu, kainic acid (KA), or dihydrokainate (DHK), an inhibition pattern characteristic of GLAST and EAAC1 transporter isoforms. mRNA for both isoforms was detected by RT-PCR, and Western blotting with appropriate antibodies shows that both proteins are expressed in these cells.
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PMID:Characterization of Na+-coupled glutamate/aspartate transport by a rat brain astrocyte line expressing GLAST and EAAC1. 1142 96

Through a genomic survey of the Caenorhabditis elegans genome for genes encoding tyrosine kinase receptors (RTK) we identified a family of four RTKs which are structurally related to vascular endothelial growth factor receptors (VEGFRs). We named this family the ver gene family (for Vascular Endothelial growth factor receptor Related). It was intriguing to find this type of RTK in an animal devoid of a vascular system. The common sites of expression of the ver genes are specialized cells of neural origin: ver-1 (T17A3.1) is expressed in the support (glial) cells of amphid and phasmid neurons, ver-2 (T17A3.8) in ADL, a pair of chemosensorial neurons, and ver-3 (F59F3.1) in the ALA neuron. In mammals, the VEGFRs are associated with angiogenesis and neurogenesis. We provide here the first observation that these molecules may be primarily and solely involved in neurogenesis in a living organism.
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PMID:Caenorhabditis elegans receptors related to mammalian vascular endothelial growth factor receptors are expressed in neural cells. 1216 Dec 75

In order to determine the interrelationship between dietary iron and zinc levels, the effects of dietary iron levels (2, 10, 20, and 40 microg/g) on changes in iron and zinc status and zinc enzyme activities (aminolevulinic acid dehydratase ALA-D EC 4.2.1.24 and alkaline phosphatase ALK-P EC 3.1.3.1) in male Wistar rats were investigated using adequate and marginally deficient zinc diets (25 and 5 microg/g). When rats were fed 5 microg Zn/g diets, body weight gain and food intake remained unchanged at a Fe diet intake of 20 microg/g or greater. Similar tendencies were obtained for hemoglobin, hematocrit, plasma iron, and transferrin saturation. In contrast, liver, spleen, and femur iron concentrations increased gradually with increased iron intake. Feeding diets containing 25 microg Zn/g did not alter these parameters. The percentages of apparent iron absorption in both dietary zinc groups tended to increase with decreasing dietary iron and attained maximum levels at an Fe intake of 10 microg/g. However, In the case of rats fed Fe at concentrations of 2 microg/g Iron absorption decreased. Regardless of the dietary zinc level, rats fed diets with an Fe concentration of 2 microg/g had decreased zinc absorption and plasma ALK-P activity. However, ALA-D activity was not influenced by dietary iron.
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PMID:The effect of dietary iron levels on changes in iron status and zinc-dependent enzyme activities in rats fed two levels of dietary zinc. 1277 12


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