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PubMed1976

On the geographical variability of the red cell PGM1 and acid phosphatase gene frequencies.

Based on the hitherto published population data of the human red cell PGM1 and acid phosphatase polymorphisms, the geographical distributions of their gene frequencies were analyzed. As far as the acid phosphatase alleles are concerned, a marked geographical gradient was found as the Pa and Pb alleles showed significant correlations with the mean annual temperatures of the various human biotopes (Pa:r = -0.706; Pb:r = +0.812). Against that, the world distribution of the PGM1 alleles did not show a comparable correlation (PGM1 1:R = +0.063; PGM2 1:R = -0.063). The possible reasons for the distribution pattern of the acid phosphatase alleles are discussed.

Acid Phosphatase↗
PubMed1981

Acid phosphatase localization in PAS-bodies of Gonyaulax.

Periodic acid-Schiff staining, acid phosphatase localization, and yellow autofluorescence have been correlated with the PAS-body of Gonyaulax polyedra for the first time. PAS- staining and acid phosphatase activity are both correlated with the PAS-body of Gonyaulax tamarensis. These results that the PAS-body of these marine dinoflagellate algae functions in subcellular digestion.

Acid Phosphatase↗
PubMed1978

Bone marrow acid phosphatase by radioimmunoassay.

A double-antibody radioimmunoassay was developed and utilized to measure prostatic acid phosphatase in bone marrow aspirates. One hundred-eighteen patients with carcinoma of the prostate in various clinical stages, and fifty with benign prostatic hyperplasia were studied. In patients with carcinoma, levels of prostatic acid phosphatase in bone marrow aspirates were found to correlate well with increasing clinical stage of the disease. Determination of bone marrow prostatic acid phosphatase by radioimmunoassay may be a valuable adjunct to clinicopathologic staging of prostatic carcinoma.

Acid Phosphatase↗
PubMed2003

Effects of several low-molecular weight organic acids and phosphate on the adsorption of acid phosphatase by soil colloids and minerals.

Adsorption of acid phosphatase on goethite, kaolinite and two colloids from the soils in central and south China in the presence of organic acids and phosphate was studied. With the increase of anion concentration, the ability in decreasing enzyme adsorption followed the sequence: phosphate>tartrate>oxalate>acetate. Acetate showed promotive effect on enzyme adsorption at lower anion concentrations whereas oxalate, tartrate and phosphate compete effectively with enzyme in a broad range of anion concentration. The adsorption isotherms of enzyme in most of the anionic systems studied conformed to the Langmuir equation. Phosphate reduced the affinity of enzyme on goethite more significantly than the other anions. However, tartrate decreased the affinity of enzyme on soil colloids and kaolinite to a greater extent than phosphate, oxalate and acetate. This observation suggested that the impact of anions on enzyme adsorption varies with anionic type and the surface characteristics of soil components. The influence of the addition order of ligand on enzyme adsorption was found greater in tartrate and phosphate systems. In general, simultaneous introduction of ligand and enzyme into the system had the lowest enzyme adsorption, showing more competition between ligand and enzyme molecules in this system. Data from this work indicated that the status and activity of enzyme in certain soil microenvironments especially the rhizosphere where various organic and inorganic ligands are active can be altered and may be completely different from the bulk soil.

Acid Phosphatase↗
PubMed2000

Acid phosphatase, genetic polymorphism and cardiovascular risk factors in a pediatric population.

BACKGROUND: Although the clinical expression of cardiovascular disease usually occurs in adulthood, it is unanimously accepted that atherosclerosis begins in the pediatric age. Because of the early onset of the disease, it is of great importance to screen for major risk factors since pre-school age, especially in risk families. Recent investigations have shown a great interest not only in studying the classic risk factors, but also in the evaluation of oxidative stress and the main antioxidant defense systems. The major cause of this interest is the knowledge of the deleterious effect of reactive oxygen species on lipids, the endothelial membrane of arteries and, finally, on the occurrence of cardiovascular disease. POPULATION AND METHODS: 51 children of both genders, aged 9-12 years, randomly selected from a rural community, were observed. A possible association between low molecular acid phosphatase genetic polymorphism of the erythrocyte and the prooxidant status markers (epinephrine oxidase and low molecular protein phosphotyrosine phosphatase from the erythrocyte), some enzymatic systems of the body antioxidant defense (transmembranar reductase of ferricyanide and metahemoglobin reductase) and finally some intermediate phenotypes of cardiovascular disease (lipid profile and blood pressure) were studied. RESULTS: The study of prooxidant status markers and antioxidant enzymes shows significant differences for acid phosphatase and epinephrine oxidase activities in relation to low molecular acid phosphatase genetic polymorphism, the highest values observed being in those homozygous to the B allele (p < 0.05). The inter-relation study between variables showed, among other things, a significant inverse correlation between acid phosphatase and transmembrane reductase and a direct correlation between apolipoprotein B, acid phosphatase and metahemoglobin reductase. A positive family history for cardiovascular disease also showed a direct and significant correlation to total cholesterol, LDL-cholesterol and apolipoprotein B. CONCLUSIONS: The polymorphic variants of low molecular acid phosphatase and protein phosphotyrosine phosphatase with greater activity are strongly associated, not with the classic parameters of cardiovascular risk factors, but with oxidative stress indicators, such as low molecular protein phosphotyrosine phosphatase and epinephrine oxidase. Family history indicators of cardiovascular risk are clearly associated, since early ages, to some conventional risk factors, such as lipid profile and blood pressure.

Acid Phosphatase↗
PubMed1987

Selective inactivation of an extra-cytoplasmic acid phosphatase of yeast-like cells of Sporothrix schenckii by sodium fluoride.

Suspensions of intact, yeast-like cells of Sporothrix schenckii exhibited an acid phosphatase (EC 3.1.3.2) activity against p-nitrophenyl phosphate of about 5 IU (g dry wt)-1, without recourse to membrane perturbation. This extra-cytoplasmic acid phosphatase was reversibly and competitively inhibited by orthophosphate (Ki = 2 mM at pH 5) but unaffected by L(+)-tartrate (in contradistinction to some of the cytoplasmic acid phosphatases of the same organism). Inactivation by NaF of the extra-cytoplasmic isoenzyme was irreversible and followed first order kinetics; sensitivity to NaF was decreased by the presence of citrate, phosphate or substrate. Neither Km (0.3 mM at pH 5) nor Vmax for this enzyme in acetate buffer was greatly affected by pH in the range 3-5 but the first order rate constant for inactivation by NaF was strongly dependent on pH (maximum at pH 3.5). Crude cell-free extracts of yeast cells had nine electrophoretically distinct acid phosphatase activity bands and, on the basis of the pattern of inhibitors, the extra-cytoplasmic activity was identified as Y-I, an isoenzyme that barely penetrates standard polyacrylamide gel electropherograms. Additional evidence for the assignment came from selective inactivation of this isoenzyme by short treatments of intact cells with NaF under conditions that did not allow penetration of the plasma membrane by the inhibitor and did not kill the cells.

Acid Phosphatase↗
PubMed1982

A single domain of human prostatic acid phosphatase shows antibody-mediated restoration of catalytic activity.

By limited proteolysis with mouse submaxillaris protease, human prostatic acid phosphatase (EC 3.1.3.2) was cleaved into three fragments, Sp1, Sp2, and Sp3, which individually had no enzymatic activity. One of the fragments, Sp3, regained enzymatic activity after interaction with rabbit antibody to prostatic acid phosphatase. The Sp3 fragment was purified and characterized as to its molecular weight, amino acid composition, and carbohydrate content. The Sp3 fragment behaved like the parent molecule in L(+)-tartrate affinity and in trapping of a phosphoryl intermediate. The same Sp3 fragment also bears the most prominent antigenic determinants. This evidence suggest that Sp3 is the enzymatically active domain of prostatic acid phosphatase.

Acid Phosphatase↗
PubMed1980

Purification and partial characterization of an acid phosphatase (EC 3.1.3.2) produced by Propionibacterium acnes.

A strain of Propionibacterium acnes (type I; Marples & McGinley, 1974), isolated from a blackhead acne lesion, produced an acid phosphatase which was present in the culture supernatant in the late-exponential and early-stationary phases of growth. This acid phosphatase was purified more than 45 000-fold (4.5% yeild). The purified enzyme gave two protein bands on sodium dodecyl sulphate-polyacrylamide gel electrophoresis corresponding to molecular weights of 155 000 and 87 100. The enzyme had a single peak of activity on Sephadex G-100, with a molecular weight corresponding to 93 000. The highly purified acid phosphatase had an optimum activity at pH 5.8, was stable from pH 4.0 to 5.5 and was totally inactivated after 30 min at 55 degrees C. The enzyme did not show an absolute requirement for metal ions, but was stimulated by Mg2+, Ca2+, Zn2+ and K+ at concentrations between 0.1 and 1 mM. The acid phosphatase was active against a number of monophosphate esters.

Acid Phosphatase↗
PubMed1981

[Improved diagnostic evaluation of prostatic neoplasms using radioimmunoassay for prostatic acid phosphatase].

Better diagnosis of prostatic cancer by RIA of serum prostatic acid phosphatase? The results of serum determination of RIA prostatic acid phosphatase (PAP) and enzymatic serum phosphatase were compared in 267 patients with the clinical diagnosis to reveal the diagnostic value of the RIA-PAP in prostatic carcinomata. In 33 of the investigated patients (12.4%) we found elevated values of the PAP over the normal range of 0--5 ng/ml. In these 33 patients with pathologic PAP-values those with adenomata and in adenomata intracapsulated prostatic cancers had normal serum values measured enzymatically. There was no correlation between PAP-RIA results and the stage of the prostatic carcinoma. In nearly 20% we found better information by RIA-PAP than enzymatic laboratory tests, but combined with a digital investigation.

Acid Phosphatase↗
PubMed1989

Vanadate monomers and dimers both inhibit the human prostatic acid phosphatase.

A combination of enzyme kinetics and 51V NMR spectroscopy was used to identify the species of vanadate that inhibits acid phosphatases. Monomeric vanadate was shown to inhibit wheat germ and potato acid phosphatases. At pH 5.5, the vanadate dimer inhibits the human prostatic acid phosphatase whereas at pH 7.0 it is the vanadate monomer that inhibits this enzyme. The pH-dependent shift in the affinity of the prostatic phosphatase for vanadate is presumably due to deprotonation of an amino acid side chain in or near the binding site resulting in a conformational change in the protein. pH may be a subtle effector of the insulin-like vanadate activity in biological systems and may explain some of the differences in selectivity observed with the protein phosphatases.

Acid Phosphatase↗
PubMed1991

Purification and characterization of a membrane-bound acid phosphatase of Leishmania mexicana.

As defined by the reaction with monoclonal antibodies, Leishmania mexicana promastigotes contain two acid phosphatases which together comprise about 90% of the cellular activity. A first enzyme recognized by monoclonal antibody AP4 is largely membrane-bound. The protein has an apparent molecular weight of 70,000-72,000, carries about seven N-linked glycan chains and is present in approximately 16,000 copies per cell. The protein is also expressed in the amastigote stage. A second enzyme reactive with monoclonal antibody AP3, that also recognizes lipophosphoglycan and a secreted acid phosphatase, is mainly found in the soluble fraction of promastigote lysates. It is suggested that this enzyme is the precursor of the secreted protein. The N-terminal sequences of the phosphatase recognized by AP4 and the secreted enzyme are similar but not identical. AP4 does not cross-react with phosphatase activity of Leishmania major or Leishmania donovani promastigotes, while AP3 recognizes part of the cellular and all of the secreted phosphatase activity of L. donovani promastigotes but not that of L. major which does not release an acid phosphatase into the culture medium.

Acid Phosphatase↗
PubMed1985

Steroid hormone regulation of prostatic acid phosphatase expression in cultured human prostatic carcinoma cells.

We have investigated the modulation of prostatic acid phosphatase expression in the human prostatic cancer cell line LNCaP in response to the natural androgens testosterone and dihydrotestosterone, the female sex steroid estradiol and the synthetic androgen R1881 (methyltrienolone). Testosterone and dihydrotestosterone at 1 microgram/ml enhance the acid phosphatase synthesis by a factor of 3.5, while a hundred-fold lower concentration of the synthetic androgen R1881 induces an almost five-fold increase in the expression of this enzyme. The stimulation by all androgens tested and estradiol was dose-dependent. The synthetic glucocorticoid triamcinolone acetonide does not modulate the prostatic acid phosphatase expression in LNCaP cells, neither alone nor in combination with R1881.

Acid Phosphatase↗
PubMed1985

Properties of an acid phosphatase from Legionella micdadei which blocks superoxide anion production by human neutrophils.

The high-speed supernatant (100,000 g, 1 h) obtained after centrifuging a suspension of Legionella micdadei that had been freeze-thawed and sonicated contained (i) considerable acid phosphatase activity when assayed using 4-methylumbelliferyl phosphate (MUP) as the substrate, and a factor that blocked superoxide anion production by human neutrophils stimulated with f-Met-Leu-Phe. Chromatography of the extract on a hydroxylapatite column resolved two acids phosphatases (designated ACP1 and ACP2). Subsequent chromatography of ACP2 on a Sephadex G-150 column revealed coincident elution of phosphatase activity and neutrophil blocking activity. When heated at 45 degrees C for various periods of time, the phosphatase activity of the acid phosphatase preparation was lost at the same rate as the ability of the preparation to block superoxide anion production by neutrophils. Furthermore, preincubation of neutrophils and acid phosphatase together in the presence of a heteropolymolybdate complex that inhibits the phosphatase eliminated the effect of the L. micdadei phosphatase on neutrophil superoxide anion production. ACP2 had the following properties: pH optimum, 6.0; Km for MUP, 3.8 mM; isoelectric point, 4.5; substrate specificity, MUP greater than ADP greater than phosphoenolpyruvate greater than phosphothreonine greater than phosphoserine greater than phosphotyrosine; molecular weight (estimated by sucrose density gradient centrifugation and gel filtration chromatography), 71,000-86,000. These results indicate that a cell-associated phosphatase may play a role in the virulence of L. micdadei.

Acid Phosphatase↗
PubMed1980

Localized secretion of acid phosphatase reflects the pattern of cell surface growth in Saccharomyces cerevisiae.

Secretion of cell wall-bound acid phosphatase by Saccharomyces cerevisiae occurs along a restricted portion of the cell surface. Acid phosphatase activity produced during derepressed synthesis on a phosphate-limited growth medium is detected with an enzyme-specific stain and is localized initially to the bud portion of a dividing cell. After two to three generations of phosphate-limited growth, most of the cells can be stained; if further phosphatase synthesis is repressed by growth in excess phosphate, dividing cells are produced in which the parent but not the bud can be stained. Budding growth is interrupted in alpha-mating-type cells by a pheromone (alpha-factor) secreted by the opposite mating type; cell surface growth continues in the presence of alpha-factor and produces a characteristic cell tip. When acid phosphatase synthesis is initiated during alpha-factor treatment, only the cell tip can br stained; when phosphate synthesis is repressed during alpha-factor treatment, the cell body but not the tip can be stained. A mixture of derepressed alpha cells and phosphatase-negative alpha cells form zygotes in which mainly one parent cell surface can be stained. The cell cycle mutant, cdc 24 (Hartwell, L.H. 1971. Exp. Cell Res. 69:265-276), fails to bud and, instead, expands symmetrically as a sphere at a nonpermissive temperature (37 degrees C). This mutant does not form a cell tip during alpha-factor treatment at 37 degrees C, and although acid phosphatade secretion occurs at this temperature, it is not localized. These results suggest that secretion reflects a polar mode of yeast cell- surface growth, and that this organization requires the cdc 24 gene product.

Acid Phosphatase↗
PubMed1997

Characterization of the amsI gene product as a low molecular weight acid phosphatase controlling exopolysaccharide synthesis of Erwinia amylovora.

The ams region, responsible for amylovoran synthesis of the fireblight pathogen Erwinia amylovora, contains the gene amsI encoding a 144 amino acid protein with homology to mammalian low molecular weight acid phosphatases [Bugert and Geider (1995) Mol. Microbiol. 15, 917-9331. A DNA fragment with amsI was cloned under the control of the lac promoter on a high copy number plasmid. The gene product of amsl is about 17 kDa in a protein expression system and had the enzymatic activity of an acid phosphatase. This is the first report about a low molecular weight acid phosphatase activity in prokaryotes. As part of the large ams transcript, expression of amsI was affected by the activator proteins RcsA and RcsB. Overexpression of amsI in E. amylovora caused a strong increase of acid phosphatase activity, but additionally a strong reduction in EPS synthesis, phenotypically similar to a mutation in the gene. The gene product may participate in changes of phosphorylation required for the biosynthesis of EPS such as recycling the lipid carrier diphosphate to the monophosphate form.

Acid Phosphatase↗
PubMed1992

Differential increase in activity of acid phosphatase induced by phosphate starvation in Tetrahymena.

We have studied the effects of phosphate starvation on the levels and distributions of activities of acid phosphatase and beta-hexosaminidase in cultures of Tetrahymena thermophila. The cells were grown in synthetic nutrient medium and refed every day with fresh medium. After 4 days of growth in the complete medium, the cultures were divided into two portions. One received complete medium and the other phosphate-free, but otherwise complete, medium. Population densities and activities of acid phosphatase and beta-hexosaminidase in cells plus medium and in cell-free samples were determined in aliquots removed every day before medium replacement. In cultures having complete medium the enzyme levels remained fairly constant; in the phosphate-starved cultures both total and extracellular activities of acid phosphatase increased sixfold. beta-Hexosaminidase levels remained essentially unaltered in both cases. These results indicate that phosphate starvation can induce differential increase in acid phosphatase activity in cultures of Tetrahymena. Somewhat less than 50% of the total activities of both enzymes are found in the cell-free extracellular fluid at any time.

Acid Phosphatase↗