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PubMed1971

Hydrolytic and alcoholytic dephosphorylation of nucleotides by acid phosphatase in the presence of ethanol.

The effect of ethanol on the activity of acid phosphatase from wheat germ was studied, by using ribonucleoside monophosphates as the enzyme substrates. The nucleotides were effectively degraded to the corresponding nucleosides in the presence of ethanol at all concentrations tested, including a 96% (v/v) solution. However, the nucleotide dephosphorylation was accompanied by the liberation of orthophosphate only when the concentration of ethanol in the assay mixture did not exceed 15%. No inorganic phosphate was liberated when ethanol was present at higher concentrations. Instead, monoethyl phosphate was formed in quantities expected for orthophosphate. The results are explained in terms of phosphatase-catalysed alcoholysis.

Acid Phosphatase↗
PubMed1982

ACP1GUA-1--a low-activity variant of human erythrocyte acid phosphatase: association with increased glutathione reductase activity.

ACP1GUA-1, a variant of human erythrocyte acid phosphatase, exists as a polymorphism (allele frequency of .132) in the Guaymi Indians of Central America. This variant has an electrophoretic mobility similar to the common B- and C-type variants, but individuals of the ACP1GUA-1 phenotype have a level of enzyme activity only 27% of the activity expected for the ACP1C variant. The GUA-1 variant is more thermostable than is the B variant, and the order of responsiveness to the modulation of activity by purine analogs and folate is always (B)-(A)-(GUA-1). Thus, the GUA-1 variant is a low-activity variant with C-like regulatory properties. Erythrocytes from individuals of the ACP1GUA-1 phenotype have increased basal levels of glutathione reductase, and a larger fraction of the glutathione reductase protein is present as the holoenzyme, indicating increased levels of flavin adenine dinucleotide in the erythrocytes of these individuals. This is consistent with the suggestion that ACP1 has a physiological function as a flavin mononucleotide phosphatase.

Acid Phosphatase↗
PubMed1982

Acid phosphatase polypeptides in Saccharomyces cerevisiae are encoded by a differentially regulated multigene family.

Two clones from a lambda phage collection containing yeast genes regulated by inorganic phosphate were shown by low-stringency hybridization to select three mRNAs that direct the in vitro synthesis of repressible acid phosphatase (EC 3.1.3.2) polypeptides p60, p58, and p56. By higher stringency hybridization one yeast fragment [8 kilobases (kb)] selects p60 mRNA and the other (5 kb) selects p56 mRNA. These EcoRI digestion fragments were subcloned in yeast transformation vectors and hybridization selection assignments were confirmed by measuring enzyme and mRNA levels in transformants. Enzyme and mRNA levels in (8-kb) high copy number transformants grown in high inorganic phosphate medium revealed a hitherto undetected acid phosphatase protein, P57, which is believed to correspond to the constitutive enzyme encoded by PHO3. The identify of the 8-kb fragment purported to contain the PHO5/PHO3 genes was confirmed by genetic mapping of an integrated copy of this fragment. The site of integration of the 5-kb fragment was demonstrated to be unlinked to the PHO5/PHO3 genes.

Acid Phosphatase↗
PubMed1989

Effect of vanadate on protein phosphorylation and on acid phosphatase activity in the canine prostate.

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)

Acid Phosphatase↗
PubMed1985

Regulation of repressible acid phosphatase gene transcription in Saccharomyces cerevisiae.

We examined the genetic system responsible for transcriptional regulation of repressible acid phosphatase (APase; orthophosphoric-monoester phosphohydrolase [acid optimum, EC 3.1.3.2]) in Saccharomyces cerevisiae at the molecular level by analysis of previously isolated and genetically well-defined regulatory gene mutants known to affect APase expression. These mutants identify numerous positive- (PHO4, PHO2, PHO81) and negative-acting (PHO80, PHO85) regulatory loci dispersed throughout the yeast genome. We showed that the interplay of these positive and negative regulatory genes occurs before or during APase gene transcription and that their functions are all indispensible for normal regulation of mRNA synthesis. Biochemical evidence suggests that the regulatory gene products they encode are expressed constitutively. More detailed investigation of APase synthesis is a conditional PHO80(Ts) mutant indicated that neither PHO4 nor any other protein factor necessary for APase mRNA synthesis is transcriptionally regulated by PHO80. Moreover, in the absence of PHO80, the corepressor, presumed to be a metabolite of Pi, did not inhibit their function in the transcriptional activation of APase.

Acid Phosphatase↗
PubMed1979

Correlation between the rosette test with neuraminidase-treated sheep red blood cells and acid phosphatase activity in lymphocytes from patients with lymphoproliferative disease.

In 14 adult patients suffering from lymphoproliferative diseases, the relation between numbers of lymphocytes determined by the rosette test (nSE) with neuraminidase-treated sheep red blood cells and numbers of lymphocytes giving a positive reaction for acid phosphatase was determined. Statistical analysis of multiple test results in the patients (n = 38) showed highly positive correlation between the two markers. A similar positive correlation in the course of cytostatic treatment was observed in selected patients with type T and B cell lymphoma. The results indicate that determination of acid phosphatase activity can serve as an additional marker of T lymphocytes in groups of patients with lymphoproliferative disease.

Acid Phosphatase↗
PubMed1999

High bilirubin levels interfere with serum tartrate-resistant acid phosphatase determination: relevance as a marker of bone resorption in jaundiced patients.

Serum tartrate-resistant acid phosphatase (TRAcP) activity is considered to be a biochemical marker of bone resorption. Recently, a lack of specificity of collagen-related markers for assessing bone turnover has been observed in patients with chronic liver disease. Thus, it could be of great interest to determine serum TRAcP activity in such patients. However, nonspecificity of the analytical reaction could occur when hemolyzed, lipemic, or icteric specimens are analyzed. Therefore, we have studied the interference caused by bilirubin in the measurement of serum TRAcP activity using the Hillmann method. The interference was assessed in two pools of serum containing different bilirubin concentrations but with similar total AcP levels. Mixing proportional parts of the two pools, 10 samples were also obtained. Serum activities of total AcP and TRAcP, and the concentration of bilirubin were measured in the 10 samples. Both the actual and the expected values obtained by theoretical calculations were compared. Serum bilirubin values of 2.4 mg/dl showed a negative interference of 15% in the determination of serum TRAcP activity, whereas values of bilirubin higher than 10 mg/dl interfered totally with the measurement of serum TRAcP. Bilirubin did not interfere with the total AcP determination. This study clearly shows the interference of bilirubin in the determination of serum TRAcP. This finding should be considered when bone metabolism disorders are evaluated in jaundiced patients.

Acid Phosphatase↗
PubMed1982

Influence of procaine HCl on larval development, adult lifespan and acid phosphatase activity in Musca domestica L.

By treating larvae of Musca domestica L. with 4 x 10(-4%) procaine HCl we could shorten larval development, decrease larval mortality and increase number of adult offspring. A high concentration of procaine HCl (0.4%) caused a prolongation of the larval development, a lower pupal weight and a decreased number of adult offspring, which are, in our opinion, indications of a toxic effect. The effects of procaine HCl on ageing and acid phosphatase activity are not so clear. The distribution of subpopulations in a population and the correlation with acid phosphatase activity during adult lifespan are discussed.

Acid Phosphatase↗
PubMed2005

The membrane-bound histidine acid phosphatase TbMBAP1 is essential for endocytosis and membrane recycling in Trypanosoma brucei.

In the parasitic protozoan Trypanosoma brucei, endocytosis and exocytosis occur exclusively at an invagination of the plasma membrane around the base of the flagellum, called the flagellar pocket, which actively communicates by vesicular membrane flow with cisternal/tubulovesicular endosomes. The division of the cell surface into three morphologically distinct sub-domains and the rapid plasma membrane turnover establishes T. brucei as an interesting model for investigations on the sorting and recycling of membrane proteins. In this study we show that the type I membrane protein TbMBAP1, an L-(+)-tartrate-sensitive acid phosphatase, is present in all endosomal membranes but is virtually absent from the lysosome membrane (where this type of protein is mainly found in other organisms) and is not detectable at the cell surface. The endosomal localization of TbMBAP1 is a function of protein abundance. Moderate overexpression (three- to fourfold) leads to an increased appearance within the flagellar pocket membrane. At higher levels the protein is found in the flagellum, and routing to the pellicular plasma membrane is observed at levels 10- to 25-fold above that of wild type. In other organisms L-(+)-tartrate-sensitive acid phosphatases appear to be dispensable but TbMBAP1 is essential, as shown by RNA interference, which causes growth arrest followed by cell death. Comparison of the phenotype of TbMBAP1-depleted cells with that of cells in which endocytosis or exocytosis has been specifically inhibited by RNAi against clathrin of RAB11, reveals that TbMBAP1 is essential for both incoming and recycling membrane traffic. During differentiation of the organism from bloodstream to insect stage, TbMBAP1 is down-regulated and differentially modified in parallel with a 10-fold decrease in the rate of endocytosis.

Acid Phosphatase↗
PubMed1983

[Action of estradiol and progesterone on alkaline and acid phosphatase activity in the sheep uterus].

The effect was studied of 20 and 60 micrograms/kg body mass of estradiol and of the combination of 60 micrograms/kg estradiol and 1 mg/kg progesterone on the character and changes in the activity of alkaline and acid phosphatase in the endo- and myometrium of the uterus and the peripheral blood in sheep. The hormones were applied singly, i/m to 18 entire and castrated year-old female sheep. The enzyme in entire females treated with 60 micrograms/kg estradiol lowered its activity, while the enzyme in those treated with the combination raised it. The treatment of castrated females with estradiol at the rate of 60 micrograms/kg raised the activity of both alkaline and acid phosphatase in the endometrium. The activity of these enzymes in the myometrium of intact animals at estradiol and combined treatment dropped. It did not show a dependable rise in the myomentrium of castrated females when treated with both estradiol and estradiol and progesterone. Following treatment with 20 and 60 micrograms/kg body mass of estradiol with castrated, and with 60 micrograms/kg of estradiol with intacts the activity of both enzymes in the blood serum rose.

Acid Phosphatase↗
PubMed1978

An acid phosphatase locus expressed in mouse kidney (Apk) and its genetic location on chromosome 10.

A genetic locus controlling the electrophoretic mobility of an acid phosphatase in mouse kidney is described. This locus, called acid phosphatase-kidney (Apk), is not expressed in erythrocytes, liver, spleen, heart, lung, brain, skeletal muscle, stomach, or testes. The product of Apk hydrolyzes the substrate naphthol AS-MX phosphoric acid but is not active on alpha-naphthylphosphate or 4-methylumbelliferylphosphate. It is not inactivated by 50 C for 1 hr, nor is its electrophoretic mobility altered by incubation with neuraminidase. The locus is invariant among 31 inbred strains (Apka), with a variant allele (Apkm) observed only in Mus musculus molossinus. Codominant expression was observed in F1 hybrids of M. m. molossinus and inbred strains. Apk was mapped on Chr 10, near the neurological mutant waltzer (v).

Acid Phosphatase↗
PubMed2001

Lactobacillus plantarum phytase activity is due to non-specific acid phosphatase.

Microbial phytases suitable for food fermentations could be obtained from lactic acid bacteria isolated from natural vegetable fermentations. Phytase activity was evaluated for six lactic acid bacteria cultures. Although the highest activity was found for Lactobacillus plantarum, the phytase activity was very low. Further characterization of the enzyme with phytate-degrading activity showed a molecular weight of 52 kDa and an optimum activity at pH 5.5 and 65 degrees C. Enzyme activity was due to a non-specific acid phosphatase which had a higher hydrolysis rate with monophosphorylated compounds such as acetyl phosphate that could explain the low phytase activity.

6-Phytase↗
PubMedDate not supplied

Acid phosphatase activity and fresh tissue weights of accessory sex organs in adult male rats following pituitary transplantation.

The effect of female pituitary transplantation under renal capsule of castrated adult male rats on accessory sex organs was studied either in presence or in absence of testosterone. Acid phosphatase activity in prostate and seminal vesicle was estimated apart from recording the fresh tissue weights of prostate, seminal vesicle, coagulating and preputial glands. Prolactin secreted from grafted pituitary significantly increased the fresh tissue weights of all sex accessories except seminal vesicle. Testosterone treatment in presence of pituitary graft stimulated the acid phosphatase activity of prostate and seminal vesicle. Prolactin in absence of testosterone could not change the enzymatic activity of prostate and seminal vesicle. The results indicate that prolactin can act directly on prostate, coagulating glands and preputial glands. Accessory sex organs also require the presence of androgens as well as prolactin to maintain the functions of sex accessories in adult male rats.

Acid Phosphatase↗
PubMed1998

Identification of a novel human phosphatidic acid phosphatase type 2 isoform.

Two human isoforms of membrane associated phosphatidic acid phosphatase have been described (PAP-2a and -2b), and both enzymes have been shown to have broad substrate specificity and wide tissue distribution [Kai et al., J. Biol. Chem. 272 (1997) 24572-24578]. With this report we describe a third isoform, PAP-2c, that we found by searching the database of expressed sequence tags (dbEST) with PAP-2a and PAP-2b sequences. Key structural features described previously in PAP-2a and -2b, including the glycosylation site, putative transmembrane domains, and the proposed catalytic site, are conserved in the novel phosphatase. The kinetics of the three enzymes were compared using as substrates phosphatidic acid, lysophosphatidic acid, and N-oleoyl ethanolamine phosphatidic acid. Km values for each of the substrates, respectively, were (in microM) PAP-2a: 98, 170, 116; PAP-2b: 100, 110, 56; and PAP-2c: 150, 340, 138. Expression of PAP-2c mRNA is more restricted than the two previously described isoforms.

Amino Acid Sequence↗
PubMed1983

The nucleotide sequence of the yeast PHO5 gene: a putative precursor of repressible acid phosphatase contains a signal peptide.

The nucleotide sequence of the PHO5 gene of the yeast, Saccharomyces cerevisiae, which encodes repressible acid phosphatase (APase) was determined. Comparison of N-terminal amino acid sequence deduced from the nucleotide sequence with that of the purified repressible APase revealed the existence of a putative signal peptide in the precursor protein. The signal peptide was shown to contain 17 amino acid residues and its structural features were quite similar to those of higher eukaryotic and prokaryotic signal peptides. The nucleotide sequence of 5' and 3' noncoding flanking regions of the PHO5 gene are also discussed.

Acid Phosphatase↗
PubMed2006

Endocytosis of tartrate-resistant acid phosphatase by osteoblast-like cells is followed by inactivation of the enzyme.

Tartrate-resistant acid phosphatase (TRACP) is generally used as a marker of osteoclasts. Yet, other bone-associated cells, such as osteoblasts and osteocytes, may also express activity of this enzyme. Osteoblasts containing TRACP activity are seen particularly in the vicinity of areas of bone resorption, suggesting that osteoclasts somehow induce TRACP activity in osteoblasts. In a recent study, we found that osteoblast-like cells appeared to have the capacity to endocytose TRACP released by osteoclast precursors. In the present study, we investigated the endocytosis of TRACP in more detail as well as the fate of the endocytosed enzyme. We found that incubation of osteoblast-like cells with TRACP-coated beads resulted in attachment of a high number of beads to the cells. After culturing osteoblast-like cells with medium conditioned by blood monocytes that contain TRACP, activity of the enzyme was found in the cells. Following replacement of the medium by normal medium that did not contain TRACP, a decrease in the level of TRACP activity in osteoblast-like cells occurred. Our data strongly suggest that osteoblast-like cells recognize TRACP released by osteoclast precursors and that upon endocytosis inactivation of the enzyme occurs. We propose that uptake of the enzyme is important for the control of enzyme activity, thereby preventing degradation of matrix constituents.

Acid Phosphatase↗
PubMed1982

Enzyme immunoassay for tartrate-resistant acid phosphatase.

An immunochemical method for quantitative analysis of the tartrate-resistant acid phosphatase (EC 3.1.3.2), band 5, is presented. This method involves precipitation of the enzyme from the serum by the antibody specific to band 5 and by sheep anti-rabbit immunoglobulin, followed by analysis of the enzyme activity in the precipitate. The precipitation procedure eliminates the interferences of the tartrate-sensitive phosphatase of all tissues, of the tartrate-resistant phosphatase of erythrocytes, and of unknown substances that interfere with the colorimetric method. We compare the present method with previously described colorimetric and electrophoretic methods.

Acid Phosphatase↗

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