Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of aluminum and other metal ions on the synthesis of nerve growth factor (NGF) by cultured mouse brain astroglial cells have been investigated. Natural NGF formation was dependent on the AlCl3 concentration of the cell culture medium; it was stimulated at low concentrations but was inhibited at higher concentrations. Catechol-stimulated NGF formation was also inhibited at AlCl3/catechol molar ratios > 0.3, whereas ZnCl2 and CaCl2 had no effect under similar conditions. Ethylenediamine-N,N,N',N'-tetraacetate (EDTA) and citrate blocked the inhibitory effect of Al(III). These observations were explained by the complex formation between Al(III) and catechols.
Biochem Mol Biol Int 1996 Apr
PMID:Effects of aluminum(III) on catechol-stimulated nerve growth factor biosynthesis by cultured mouse brain astroglial cells. 872 96

The present study was designed to test the hypothesis that Ca2+ is required for the successful induction of the decidual cell reaction (DCR) in mice following stimulation with concanavalin A (Con A). Con A (125 micrograms) administered intraluminally on Day 4 of pseudopregnancy increased uterine vascular permeability increased uterine weight, and induced morphological and histological transformations that were clearly indicative of decidualization. Radioactive CaCl2 (1 mmol liter-1, 600 mCi mmol-1 introduced into the uterine lumen with either Con A or saline was subsequently incorporated into the uterine tissue and detected only in the luminal epithelium by microautoradiography techniques. The intraluminal administration of CaCl2 in combination with Con A increased the magnitude of the lectin-induced DCR. In contrast, the administration of other cationic chloride solutions, at various concentrations and tonicity, either had no effect (viz. Na+, Mg2+, and Ba2+) or reduced (viz. K+, Zn2+, Cd2+, and La3+) this uterine response. While ionophore A23187 was also deciduogenic, it suppressed the DCR when administered before Con A and enhanced the DCR when administered after Con A. The Ca2+ channel blockers, nifedipine, verapamil, nicardipine, and diltiazem, the Ca(2+)-calmodulin inhibitor, W7, and the Ca(+)-ATPase inhibitor, thapsigargin also effectively reduced the uterine response to Con A when administered intraluminally. However, the Con A A-induced DCR was not influenced by the Ca+ chelators, EGTA, EDTA, BAPTA, and BAPTA-AM. The results confirm that Con A is deciduogenic in pseudopregnant mice and suggest that luminal Ca2+ plays an important role in facilitating the induction of the lectin-induced DCR by influencing the metabolism of the luminal epithelium.
Biochem Mol Med 1996 Apr
PMID:The role of calcium in the artificially induced decidual cell reaction in pseudopregnant mice. 873 85

A protein phosphatase that dephosphorylates pyruvate kinase (PK) in vitro was purified and characterized from the foot muscle of the anoxia tolerant gastropod mollusc Busycon canaliculatum. Purification involved three steps: negative chromatography through Blue Dextran and CM Sephadex, affinity chromatography on DEAE Sephadex and gel exclusion chromatography on Sephacryl S-400. Pyruvate kinase phosphatase (PK-Pase) activity was monitored by following changes in PK I50 values for L-alanine that had previously been linked to changes in the degree of PK phosphorylation. The purified PK-Pase gave a single band on SDS-polyacrylamide gel electrophoresis with a molecular weight of 41 +/- 1 kdaltons. Isoelectric focusing analysis showed that the PK-Pase had an isoelectric point of 4.2 +/- 0.1. Kinetic analysis showed that the enzyme was a Type 2C protein phosphatase with a pH optimum of 6.5. Maximal activity required the presence of magnesium ions (KM = 7.9 +/- 0.6 microM) although high concentrations of Mg2+ were inhibitory (I50 = 2.3 +/- 0.4 mM). The protein phosphatase activity was not affected by either spermine, cAMP, cGMP, potassium phosphate, tartrate, NaF, HgCl2, citrate or concentrations of CaCl2 less than 10 mM. The enzyme could also use ATP, ADP, and GTP as substrates.
Biochem Mol Biol Int 1996 May
PMID:Purification and characterization of a protein phosphatase that dephosphorylates pyruvate kinase in an anoxia tolerant animal. 873 44

Previous reports have suggested a role played by peripheral benzodiazepine receptors (PBZ) in the regulation of calcium. The aid of this investigation was to evaluate the effects of Ro 5-4864 (PBZ agonist) and PK11195 (PBZ antagonist) in guinea pig trachea and their possible role in the regulation of calcium. Ro 5-4864 and PK 11195 showed spasmolytic effects on the contraction curve induced by acetylcholine. Moreover, Ro 5-4864, PK 11195 and diltiazem (a Ca2+ -antagonistic drug) shifted to the right the contraction curves induced by acetylcholine, potassium chloride (KCl), calcium chloride (CaCl2), or by Bay K 8644. These results demonstrate that the benzodiazepines and their antagonists may exhibit Ca2+ -antagonistic activity. Ro 5-4864 and PK 11195 may exert this effect at a site that is a component of, or is associated with, voltage operated calcium channels (VOC).
Res Commun Mol Pathol Pharmacol 1995 Dec
PMID:Effects of RO 5-4864 and PK 11195 on guinea pig trachea. 874 80

Actin in the low ionic strength buffer solution G (0.1 mM ATP, 0.1 mM CaCl2, 2 mM Tris-Cl (pH 8.0), 5 mM 2-mercaptoethanol and 1 mM NaN3) was diluted to the concentration below 10 micrograms/ml at 7 degrees C. Viscometry showed associations of actin monomers and increasing the extent of dilution, maximally about 75% of actin were precipitated. Actin filaments were observed by electron microscope in the diluted solution. Ca2+ plays a role in the filaments' formation. It seems that a phase transition like change in the actin states arose at this concentration range.
Biochem Mol Biol Int 1995 Dec
PMID:Dilution beyond a transition concentration and the enhanced filaments' formation of actin in the low ionic strength buffer. 874 46

DNA topoisomerase I was partially purified from the hepatopancreas of the shrimp Penaeus japonicus. The specific activity of the final preparation was 7,000,000 units/mg of protein with SV40 viral DNA as substrate. SDD-polyacrylamide gel electrophoresis of the final preparation yielded two major bands of proteins with M(r) 70,000 and M(r) 67,000, as well as less intense bands of proteins with M, 64,000 and M(r) 56,000. Incubation of the partially purified enzyme fraction with rabbit antiserum against human DNA topoisomerase I, allowed all these proteins except that of M(r) 56,000, to be positively reacted. Treatment of the partially purified DNA topoisomerase I with tyrosine kinase p43v-abl resulted in phosphorylation of only the two major subunits. Phosphorylation by tyrosine kinase p43v-abl or dephosphorylation by phosphotyrosyl protein phosphatase resulted in a decrease of the enzymatic activity. The treatment with shrimp alkaline phosphatase abolished the enzymatic activity of the purified DNA topoisomerase I in a dose-dependent manner. Thus, the DNA topoisomerase I was apparently isolated from the hepatopancreas of the shrimp P. japonicus in a phosphorylated form, and this phosphorylation was essential for expression of enzymatic activity in vitro. The activity of DNA topoisomerase I is inhibited by ZnCl2, CuCl2 and Pb(NH3)3 at millimolar concentrations, but less inhibition was observed with CaCl2.
Comp Biochem Physiol B Biochem Mol Biol 1996 Jun
PMID:Modification of DNA topoisomerase I enzymatic activity with phosphotyrosyl protein phosphatase and alkaline phosphatase from the hepatopancreas of the shrimp Penaeus japonicus (Crustacea:Decapoda). 875 89

The subunit structure of soluble goat hepatic lectin was studied by determining molecular weight under nondenaturing conditions by gel filtration and denaturing conditions by SDS PAGE. Affinity purified lectin was subjected to HPLC on asahipack column equilibrated with 10 mM Tris-HCl pH 7.5, containing 1 mM CaCl2, 1mM 2-mercaptoethanol and 0.1M NaCl. The lectin was eluted under single peak at retention time of 12 min. corresponding to molecular weight of 38Kd. On SDS-PAGE in the presence and absence of 2-mercaptoethanol protein moved as single band with Rm 0.45, which corresponds to molecular weight of 20 Kd. The results suggest that soluble goat hepatic lectin is a dimmer of identical subunits which are linked together by noncovalent interactions. The interaction of monoclonal antibodies raised against soluble goat hepatic lectin (MGHL/20) with hemagglutinin from different species as sheep, human, rat, bovine and chicken was studied in PBS by solid phase binding assay. MGHL/20 showed 29.89% binding with these lectin. However no binding was found with Ca++ dependent membrane bound lectin. These results indicate that soluble goat hepatic lectin possesses antigenic structural relationship with soluble 14 K lectin family.
Biochem Mol Biol Int 1996 Aug
PMID:Subunit structure of Ca++ dependent soluble goat hepatic lectin: evidence that it has antigenic structural relationship with soluble 14K lectin family. 886 13

LR-A/113 is a benzothiazepine drug similar to diltiazem with Ca(2+)-antagonist properties. Our previous studies showed that LR-A/113 determines anthypertensive effects comparable to diltiazem in normotensive and hypertensive rats. The aim of this study is to determine LR-A/113 effects respect to verapamil and diltiazem on CaCl2, aconitine and ouabain arrhythmias. Experiments were carried out on normotensive anesthetized rats and guinea pigs treated with CaCl2, aconitine and ouabaine and pretreated or not with verapamil, diltiazem or LR-A/113. Verapamil, diltiazem and LR-A/113, significantly delayed onset of arrhythmias and cardiac standstill induced by CaCl2 and aconitine. Moreover, pretreatments with verapamil, diltiazem or LR-A/113 reduced occurrence of arrhythmias in animals. In our models of arrhythmias LR-A/113 showed a significant antiarrhythmic effect of a magnitude almost similar to diltiazem but lower than for verapamil.
Res Commun Mol Pathol Pharmacol 1996 Aug
PMID:Antiarrhythmic effects of LR-A/113 a new calcium antagonistic drug. 888 94

The total proteolytic activity of ISP1 determined after its partial purification by size exclusion HPLC increased 3.0, 7.3 and 27.3 times in sporulating, growing and netropsin-treated cells, respectively, as compared with the corresponding original activity in crude cytoplasmic preparations at the same CaCl2 concentration of 3 mM. A similar rise in proteolytic activity occurred on increasing the Ca2+ concentration in the crude cytoplasm from 3 to 30 mM. This activation in the cytoplasm of netropsin-treated and sporulating cells was not reversed by subsequent lowering of CaCl2 concentration back to 3 mM by dialysis. Moreover, a similar activation appeared even after the same dialysis of cytoplasm that had not been exposed to 30 mM CaCl2. The activation was probably due to the processing of ISP1, as established by SDS-PAGE and immunoblotting, but an involvement of additional regulation factor(s), e.g. an inhibitor or other molecules, is possible.
Biochem Mol Biol Int 1996 Nov
PMID:Activation of the intracellular Ca(2+)-dependent serine protease ISP1 of bacillus megaterium by purification or by high Ca2+ concentrations. 895 84

The structure of a parallel left-handed double-helical form of gramicidin was detected by circular dichroism spectroscopy and determined using 500 and 600 MHz NMR in CaCl2/methanol solution. Measurements of TOCSY, DQF-COSY and NOESY spectra were converted into 604 distance and 48 torsional angle constraints for structure calculations. Stereospecific assignments and chi 1 angles were calculated using 3J alpha beta, d alpha beta (i,i), dN beta(i,i) and dN gamma(i,i). chi 2 angles were determined using d alpha beta(i,i), dN beta(i,i), d beta delta(i,i), dN gamma(i,i) and d alpha gamma(i,i). The calculations of initial structures were performed using the distance geometry/simulated annealing method in XPLOR. The initial structures were further refined and energy minimized using simulated annealing/molecular dynamics methods. Back-calculations for every generated structure were also performed to check their consistency with the experimental data. 187 final structures with no violations above the threshold conditions (0.05 A, 5 degrees, 5 degrees, 0.5 A and 5 degrees for bonds, angles, improper, NOE and cdihe, respectively) were produced from the 200 initial structures. Twenty structures with the lowest NOE energies were used for further analysis. The average r.m.s. deviations for the 20 structures are 0.64 A for backbone and 1.1 A for all non-hydrogen atoms. Gramicidin in this form, with approximately 5.7 residues per turn, is a parallel double helical dimer. The length along the helix axis is about 30 A and the inner pore diameter varies from 1 to 2 A. It is different from all other gramicidin structures determined to date. The presence of Ca2+ stabilises a conformation that prevents the binding of monovalent cations. It is likely that this structure is related to a non-channel, antibiotic role of gramicidin.
J Mol Biol 1996 Dec 13
PMID:Solution structure of a parallel left-handed double-helical gramicidin-A determined by 2D 1H NMR. 898 Jun 84


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