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

Expression of the repressible acid phosphatase (rAPase) gene, PHO5, of Saccharomyces cerevisiae is repressed by a certain level of inorganic phosphate (Pi) in the medium and is derepressed when the Pi concentration is lowered. The Pi signals are conveyed to PHO5 by a regulatory system consisting of proteins coded for by the PHO2, PHO4, PHO80 and PHO81 genes. We have found that the transcription of PHO81 is regulated by Pi through the PHO regulatory system. Increasing the dosage of PHO4 and PHO81 by ligating each gene to YEp13 gives rise to, respectively, considerable and weak synthesis of rAPase by cultivation of the transformants in high-Pi medium; but in low-Pi medium, increased dosage of PHO4 stimulates the rAPase synthesis significantly, whereas PHO81 has no effect. Increased dosage of PHO2 stimulates rAPase synthesis considerably in low-Pi but not in high-Pi. A coordinate increase of PHO80 cancels the dosage effect of PHO4, but not that of PHO81. Coordinate increases of PHO80 and PHO2 give rise to the same phenotype as an increased dosage of PHO80 alone. The level of the PHO4 protein was found to be the limiting factor of the rAPase synthesis and the copy number of the PHO5 gene not to be. These facts accord with the idea that the PHO80 protein transmits the Pi signals to the PHO5 gene via the PHO4 protein, whereas the PHO2 protein does not have a direct function in the signal transmission.
Mol Gen Genet 1989 May
PMID:Function of the PHO regulatory genes for repressible acid phosphatase synthesis in Saccharomyces cerevisiae. 267 50

Acetylcholinesterase and fluoride-resistant acid phosphatase activities were contrasted in alternative serial sections of rat dorsal root ganglia. The morphometric analysis demonstrated no correlation between cellular size and enzymatic activity. Differences with previous works in this area are discussed.
Cell Mol Biol 1989
PMID:Acetyl-cholinesterase and fluoride-resistant acid phosphatase activities in dorsal root ganglia in the rat. 270 52

Adherent peritoneal exudate cells rich in macrophages were harvested from Cornell K-strain chickens 42 hr after i.p. stimulation with Sephadex G-50. Glass-adherent monolayers were obtained on coverslips and subjected to in vitro exposure to methyl methanesulfonate (MMS) at various doses for 1 hr. Solvent (0.17% ethanol final concentration) and sham (RPMI 1640 growth media) exposures were also performed. At selected times after exposure, the macrophages were analyzed for cell viability, adherence, DNA damage, and functional activity. Although MMS doses of 5 x 10(-3) M and 1 x 10(-3) M concentrations resulted in significant cytoxicity, 2 x 10(-4) M had no significant cytotoxic effect. However, this exposure resulted in DNA damage as measured by alkaline elution. Concomitant with the DNA damage was a significant decrease in the phagocytic activity of macrophages. Repair of MMS-induced DNA lesions in macrophages was indicated by a normal DNA alkaline elution profile 10 hr postrecovery. Functional activity of cells also returned to normal levels. In contrast, the incidence of Fc receptor-positive cells detected by rosetting increased immediately after MMS exposure, and phagocytosis of opsonized SRBCs was not affected by 2 x 10(-4) M MMS treatment. Similarly, MMS treatment did not alter the acid phosphatase activity of macrophages. However, bactericidal ability of MMS-treated macrophages for unopsonized Escherichia coli was significantly depressed. These results suggest that the avian macrophage is a useful target cell for examining possible relationships between genotoxic and immunotoxic effects of environmental mutagens.
Environ Mol Mutagen 1989
PMID:Toxic effects of methyl methanesulfonate (MMS) on activated macrophages from chickens. 270 55

The c-fos serum response element (SRE) and a sarcomeric actin promoter element (CArG box) are similar in sequence and are recognized, respectively, by the serum response factor (SRF) and the CArG-binding factor (CBF). Although the transcriptional controls for the c-fos and sarcomeric actin genes are rather different, SRF and CBF have been found to be indistinguishable by all criteria tested. They exhibited similar chromatographic properties, sedimentation rates, and temperature stabilities. In mobility shift assays, the SRE competed more strongly than the actin CArG box for formation of either the SRF-SRE or the CBF-CArG complex. The symmetric inverted repeat of the left side of the Xenopus cytoskeletal actin SRE also competed, even more strongly, for each complex. The site-specific binding of each protein was inhibited both by orthophenanthroline, whose effects were reversed by zinc addition, and by treatment with potato acid phosphatase. Furthermore, immune serum raised against the c-fos SRF also recognized the actin CBF. We discuss how transcriptional control of these diverse genes might be obtained with a single similar factor.
Mol Cell Biol 1989 Feb
PMID:The sarcomeric actin CArG-binding factor is indistinguishable from the c-fos serum response factor. 271 Jan 14

A number of drugs which are known to affect lysosomes and their enzyme activities were used in an attempt to inhibit or delay the onset of denervation changes in rat muscles. The following parameters were used: the occurrence of fibrillations in electromyographs; diameters of muscle fibers; acid phosphatase activity; acetylcholinesterase activity and distribution in end plates. Differences between denervated and non-denervated limbs were evaluated and compared in the different treatment groups. The various parameters were differently affected by the different drugs. Chloroquin, thiouracil and streptomycin appeared to be more effective than other treatments in the inhibition of denervation changes.
Cell Mol Biol 1989
PMID:An attempt to prevent or delay denervation changes in rat muscles. 273 Nov 90

To evaluate the possible role of intracellular phosphatases in the local regulation of prostatic functions, the effect of sodium orthovanadate (VO4), an inhibitor of phosphotyrosyl protein phosphatases, was studied on both protein phosphorylation and acid phosphatase activity. Secretory and non-secretory epithelial cells were isolated from normal and metaplastic prostates and incubated with [32P]phosphate in the presence and in the absence of VO4; the phosphoproteins were separated by electrophoresis and the gels were either directly submitted to autoradiography or after an alkali treatment to reveal those proteins enriched in phosphotyrosine. Prior to alkali treatment, several phosphoproteins were evidenced and in less than half of the cell preparations a slight increase in labeling intensity under vanadate (less than 75%) was observed in two phosphoproteins, p57 and p44. After alkali treatment: (1) the effect of VO4 on p57 remained in the order of 44-45% and it was restricted to less than half of non-secretory cell preparations; (2) its effect on p44 was intensified (134-207%) and observed in all cell types and in more than 80% of all preparations; and (3) in half of non-secretory cell preparations from metaplastic glands, an effect of VO4 on p35 (127%) became evident. In all instances, with normal and/or metaplastic prostates, protein phosphorylation activity, either total or alkali-resistant and in the presence or in the absence of VO4, was always higher in non-secretory epithelial cells as compared to secretory cells.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Cell Endocrinol 1989 Jun
PMID:Effect of vanadate on protein phosphorylation and on acid phosphatase activity in the canine prostate. 275 42

Lysosomes are defined traditionally with the marker enzyme acid phosphatase. We showed recently that lysosomes from human fibroblasts can be separated into a light and dense fraction as well as prelysosomal population. We now provide evidence that although acid phosphatase is enriched in all three fractions, the marker enzyme in the prelysosomal compartment is qualitatively distinct from that of the lysosomes. Ultrastructural analysis showed that the acid phosphatase in the prelysosomal vesicles deposited an extremely electron-dense reaction product, entirely obliterating the lumen of the vesicle, in contrast to that of the light and dense lysosomes which deposited a fine and diffuse product scattered throughout the luminal space. Biochemical analysis showed that only 51% of the acid phosphatase in the prelysosomes was inhibited by tartrate, while 80% of that in the lysosomes was tartrate-inhibitable. Immunoprecipitation with antibodies specific for various isozymes of acid phosphatase showed that 39% of the acid phosphatase in the prelysosomes was of the 'lysosomal' type whereas over 50% of the acid phosphatase in the lysosomes was of this type. These results showed that acid phosphatase in the prelysosomes of human cultured fibroblasts can be distinguished from that of the lysosomes cytochemically, biochemically, and immunologically and that lysosomes, as marked by acid phosphatase, are a heterogeneous organelle.
Mol Cell Biochem 1989 Jun 01
PMID:Heterogeneity of lysosomes in human fibroblasts. 277 Jul 20

The level of resistance to infection in inbred mice with the murine malaria species Plasmodium chabaudi AS is genetically determined. Resistant C57BL/6, which are able to eliminate the parasite by 4 weeks, develop marked splenomegaly and survive the infection. Susceptible A/J mice, which succumb to infection (mean survival time = 10 days), develop only minimal splenomegaly. In order to determine if gross differences in the organization, number, and type of spleen cells are related to the outcome of infection with P. chabaudi AS, the development of splenomegaly was examined by enzyme and immunohistochemical methods during the first week after infection. Cryostat sections of spleens removed from normal animals of both strains and at 4 and 7 days after intraperitoneal infection with 10(6) parasitized erythrocytes were stained for enzyme (acid phosphatase and nonspecific esterase) and immunohistochemistry with conventional monoclonal antibodies against T cells, B cells, and macrophages as well as with novel rat anti-mouse monoclonal antibodies which define discrete subpopulations of macrophages in the mouse spleen. The livers of normal and infected animals of each strain were also examined. The results of this study demonstrate (1) differences between normal, uninfected B6 and A/J mice in the organization and number of one subpopulation of macrophages in the spleen, the marginal metallophilic macrophages, and (2) marked histological changes in the spleen and liver during the course of infection in both resistant C57BL/6 and susceptible A/J mice. These changes include depletion of cells from the marginal zone of the spleen which, in the case of the marginal metallophilic macrophages, appears to be more severe in susceptible A/J mice.
Exp Mol Pathol 1989 Aug
PMID:Histological changes in the spleen and liver of C57BL/6 and A/J mice during Plasmodium chabaudi AS infection. 278 81

The hepatic transport mechanism for the fluorescent bivalent hydrophilic organic cation lucigenin (LU) was characterized employing kinetic and morphological methods. The extraction of LU by the perfused rat liver was 50% and uptake was saturable. LU did not inhibit the carrier-mediated hepatic uptake of the model organic cationic compounds tributylmethyl ammonium (type 1) and vecuronium (type 2) in isolated hepatocytes, whereas the uptake of LU in the perfused liver was not affected by either type of cation or by the cardiac glycoside cymarin, a potent type 2 inhibitor. The cytoskeleton-disrupting agents cytochalasin B and nocodazole, however, significantly lowered hepatic uptake of LU. In the intact liver, LU did not stimulate fluid phase endocytosis, as indicated by a lack of effect on the internalization of horseradish peroxidase. These kinetic data point to adsorptive endocytosis as the most probable uptake mechanism. This was confirmed by the inhibitory effect of neomycin and the polycation poly(L-lysine) on LU uptake. Fluorescence microscopy revealed that LU accumulated in the hepatocytes in discrete vesicular structures. Partial co-localization of rhodamine-dextran and acid phosphatase with LU indicated that part of the LU fluorescence was present in lysosomes, although not all lysosomes contained LU. Taken together, we conclude that we identified a novel vesicular pathway for uptake of organic cations by hepatocytes.
Mol Pharmacol 1989 Oct
PMID:Vesicular uptake system for the cation lucigenin in the rat hepatocyte. 281 56

The structural gene for an acid phosphatase coded for by the gene appA of Escherichia coli K12 was cloned from a cosmid library into pBR322 and the restriction map determined. Several appA deletion plasmids and a smaller appA+ plasmid were constructed by in vitro recombination techniques and tested for their ability to complement an appA1 mutation. The appA gene was localized within a 2.1 kb segment. Its orientation was determined by construction of a hybrid plasmid carrying an appA-lacZ fusion. beta-galactosidase synthesized from the appA promoter was negatively regulated by cyclic AMP.
Mol Gen Genet 1987 Jul
PMID:Cloning and characterization of the pH 2.5 acid phosphatase gene, appA: cyclic AMP mediated negative regulation. 282 63


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>