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)

Two new classes of mutants, phoF and phoG, lacking the constitutive acid phosphatase activity, were isolated. They both complemented each other and the phoC mutation. No linkage was detected among these three complementary genes.
Mol Gen Genet 1975 Nov 03
PMID:Two new genes controlling the constitutive acid phosphatase synthesis in Saccharomyces cerevisiae. 76 26

The phoE locus, one of the loci in which mutations lack the activity for repressible acid phosphatase, was found to be the structural gene for the enzyme by examining the enzymic characteristics of repressible acid phosphatase activity using cell extracts prepared from the leaky phoE mutants, the PHOE revertants and the PHOE recombinants between the different phoE mutants. Other evidence which strongly suggests that the phoC locus is coding for the constitutive acid phosphatase was obtained by a similar investigation. Although the phoC and phoE loci are tightly linked, they were separable by meiotic recombination.
Mol Gen Genet 1975 Dec 30
PMID:Genes coding for the structure of the acid phosphatases in Saccharomyces cerevisiae. 76 44

Lipid droplets surrounded by a peripheral membrane closely apposed to an electron-dense layer and containing acid phosphatase activity, similar to the lipolysosomes in hamsters described by Nehemiah and Novikoff (J. Cell Biol. 59: 246a, 1973; Exp. Mol. Pathol. 21:398, 1974), were found in the hepatocytes of patients with Wilson's disease. These organelles account for 1 to 2 per cent of the observed lipid droplets at the stage of the disease when excess fat is present. The occurrence of lipolysosomes in a condition not known to be associated with an acid lipase deficiency suggests that lipolysosomes may represent a nonspecific, alternate route for the mobilization of excess lipid from hepatocytes.
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PMID:Lipolysosomes in human hepatocytes. Ultrastructural and cytochemical studies of patients with Wilson's disease. 114 38

1. Iron, acid phosphatase and N-acetyl-beta-glucosaminidase were assayed in liver biopsies from control subjects and patients with primary and secondary haemochromatosis. 2. The activities of the lysosomal enzymes were significantly higher in liver biopsies from patients with iron overload than in those from other patient groups. 3. Lysosomes from the livers of patients with iron overload were strikingly more fragile than those of control subjects as demonstrated by assays of latent and sedimentable N-acetyl-beta-glucosaminidase. 4. Lysosomal integrity was essentially normal in biopsies from patients with a wide variety of chronic liver diseases. 5. It is suggested that iron accumulation damages lysosomal membrane, releasing acid hydrolases into the cytoplasm and thus initiating cell damage.
Clin Sci Mol Med 1976 Jan
PMID:Acid hydrolase activities and lysosomal integrity in liver biopsies from patients with iron overload. 124 5

A DNA probe is described that can be used for identification of Providencia stuartii by means of filter hybridization assays. The probe, which is a fragment of the P. stuartii phoN gene coding for an acid phosphatase, appeared to be able to recognize only P. stuartii strains in slot-blot hybridization experiments performed with total DNA extracted from 545 strains of 64 different Gram-negative bacterial species, including all the major representatives of the family Enterobacteriaceae. Owing to the problems that may be often encountered for correct identification of P. stuartii at the species level when using commercial identification systems, this probe may result useful for fast and reliable identification of P. stuartii strains for taxonomical, epidemiological and diagnostic studies.
Mol Cell Probes 1992 Oct
PMID:A species-specific DNA probe for Providencia stuartii identification. 147 80

The major phosphate-repressible acid phosphatase (APase) of Saccharomyces cerevisiae, a cell wall glycoprotein, has been extensively used as a reporter protein to analyse successive steps in the yeast secretory pathway. In contrast to other yeast secretory proteins, APase can still be translocated into the endoplasmic reticulum (ER) even when it is made without its signal peptide. This property illustrates the permissiveness of targeting to the ER in yeast. Studies on APase-containing hybrid proteins have provided some of the evidence that specific soluble factors must interact with secretory proteins prior to their translocation across the ER membrane. A systematic analysis of mutations affecting the sequence of the APase signal peptide cleavage site demonstrated that cleavage occurs only when the last amino acid of the signal sequence is small and neutral. This was one of the first studies to verify the requirements for signal peptidase cleavage that had previously only been predicted from statistical analysis. Studies performed either with inhibitors of glycosylation or with mutant APases demonstrated the critical role of core glycosylation for APase folding, which is essential for efficient transport beyond the ER. Following the fate of particular modified APases along the secretory pathway provided insights into some general properties of the secretory apparatus and illustrated the specific requirements for a given protein during its intracellular traffic.
Mol Microbiol 1992 Mar
PMID:Protein-specific features of the general secretion pathway in yeast: the secretion of acid phosphatase. 155 57

Purple acid phosphatase from red kidney bean has been crystallized from ammonium sulfate solutions in the pH range from 3.5 to 5.5. The crystal form is tetragonal bipyramidal and the largest crystals grew up to 2.0 mm long. Systematic absences indicate one of the enantiomorphic space groups P4(1)2(1)2 (92) or P4(3)2(1)2 (96) with cell dimensions a = b = 104.1(1) A and c = 308.7(2) A. The asymmetric unit contains one dimer with Mr of 110,700, determined by ultraviolet-laser desorption mass spectrometry. The crystals, with a salt-free density of 1.12 g/cm3 and a water content of 67%, diffract to 3.5 A.
J Mol Biol 1992 Mar 20
PMID:Crystallization and preliminary crystallographic data of purple acid phosphatase from red kidney bean. 156 Apr 65

The human prostate tumor cell line LNCaP contains an abnormal androgen receptor system with broad steroid binding specificity. Progestagens, estradiol and several antiandrogens compete with androgens for binding to the androgen receptor in the cells to a higher extent than in other androgen sensitive systems. Optimal growth of LNCaP cells is observed after addition of the synthetic androgen R1881 (0.1 nM). In addition, estrogens, progestagens and several antiandrogens do not inhibit androgen responsive growth, but have striking growth stimulatory effects and increase EGF receptor level and acid phosphatase secretion. We have found that the androgen receptor in the LNCaP cells contains a single point mutation changing the sense of codon 868 (Thr to Ala) in the ligand binding domain. Expression vectors containing the normal or mutated androgen receptor sequence were transfected into COS or HeLa cells. Androgens, progestagens, estrogens and several antiandrogens bind the mutated androgen receptor protein and activate the expression of an androgen-regulated reporter gene (GRE-tk-CAT), indicating that the mutation directly affects both binding specificity and the induction of gene expression. Interestingly, the antiandrogen casodex showed antiandrogenic properties in growth studies of LNCaP cells and did not induce reporter gene activity in Hela cells transfected with the mutant receptor. The mutated androgen receptor of LNCaP cells is therefore a useful tool in the elucidation of different levels of action of steroids and antisteroids.
J Steroid Biochem Mol Biol 1992 Mar
PMID:The androgen receptor in LNCaP cells contains a mutation in the ligand binding domain which affects steroid binding characteristics and response to antiandrogens. 156 39

Simultaneous localization of 3H-thymidine incorporation and acid phosphatase (AcP) activity was undertaken by combined radioautography and cytochemistry in the spleen of mice at different ages. The localization of radiolabelled thymidine was used to determine the site of DNA synthesis (cell proliferation), while AcP activity as a marker for cell lysis/death. For EM radioautography (EMRAG), the tissue sections were incubated in a medium containing 3H-thymidine and processed for radioautography, while the lanthanide-based method for the ultrastructural localization of AcP activity was employed. Quantitation of AcP activity was carried out by X-ray microanalysis. In all tissue sections examined, mostly of the labelled nuclei were observed in the hematopoietic cells. Few mitochondria of these cells were labelled. The labeling index was expressed as the percentage of labelled cells over the total number of counted cells. The labeling indices dropped considerably from day one after birth and progressively until the 10th month. The result of AcP activity correlated well with the result of a previous work (Olea, 1991). The localization of radiolabelled thymidine and AcP activity were not hindered by the simultaneous exposure of the same tissue section to 3H-thymidine and AcP cytochemical media. Interestingly enough, the spleen actively participates both in hematopoiesis and erythrophagocytosis. Prominently, it is most active during the early postnatal life. However, their influence declined considerably at the later stage of life (adult stage).
Cell Mol Biol 1992 Apr
PMID:Simultaneous localization of 3H-thymidine incorporation and acid phosphatase activity in mouse spleen: EM radioautography and cytochemistry. 157 40

We have found an open reading frame which is 1.1 kb upstream of PHO84 (which encodes a Pi transporter) and is transcribed from the opposite strand. In Saccharomyces cerevisiae, this gene is distal to the TUB3 locus on the left arm of chromosome XIII and is named GTR1. GTR1 encodes a protein consisting of 310 amino acid residues containing, in its N-terminal region, the characteristic tripartite consensus elements for binding GTP conserved in GTP-binding proteins, except for histidine in place of a widely conserved aspargine residue in element III. Disruption of the GTR1 gene resulted in slow growth at 30 degrees C and no growth at 15 degrees C; other phenotypes resembled those of pho84 mutants and included constitutive synthesis of repressible acid phosphatase, reduced Pi transport activity, and resistance to arsenate. The latter phenotypes were shown to be due to a defect in Pi uptake, and the Gtr1 protein was found to be functionally associated with the Pho84 Pi transporter. Recombination between chromosome V (at the URA3 locus) and chromosome XIII (in the GTR1-PHO84-TUB3 region) by using a plasmid-encoded site-specific recombination system indicated that the order of these genes was telomere-TUB3-PHO84-GTR1-CENXIII.
Mol Cell Biol 1992 Jul
PMID:Putative GTP-binding protein, Gtr1, associated with the function of the Pho84 inorganic phosphate transporter in Saccharomyces cerevisiae. 162 Jan 8


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