PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “ACID PHOSPHATASE”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 127 records · Page 7Linked to original sources
PubMed1981

Cytochemistry and biochemistry of acid phosphatases. III. Inhibition experiments of lysosomal and secretory acid phosphatases of the rat ventral prostate.

Biochemical and cytochemical inhibition experiments of rat prostatic acid phosphatase were performed using enzymes separated on isoelectric focusing (IEF) gels, and thin sections of the rat ventral prostate. Various inhibitors, including L (+) tartrate, mercuric ions and sodium fluoride were applied to electrofocused enzymes which were subsequently stained for acid phosphatase activity. Enzymes focused on IEF gels at pH 7.9 and 8.1, respectively, were inhibited with 1.8 x 10-3 M tartrate, while the enzyme activities with isoelectric points (pl) of 5.6 and 7.15, respectively, were only slightly inhibited by this compound. Using 10-3M mercuric ions, enzymes with pl of 5.6 and 7.15 were inhibited while the enzymes with pl of 7.9 and 8.1 were still active. The biochemical procedures were adapted to chopper sections of perfused-fixed ventral prostate of the rat. Preincubation of the sections with 2.4 x 10-3M mercuric chloride blocked the secretory enzyme and most of the lysosomal enzyme and resulted in an artificial staining of the Golgi apparatus and other cytoplasmic organelles. Nuclear precipitates however were prevented. L (+) tartrate could not be used at the ultrastructural level since it developed false positive results by the formation of lead tartrate. The results indicate that no selective inhibition of either secretory or lysosomal acid phosphatase can be achieved at the ultrastructural level using metal salts or tartrate, respectively.

Acid Phosphatase↗
PubMed1989

Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase.

The cDNAs encoding human prostatic acid phosphatase were cloned and characterized. The mRNAs contain 3' noncoding regions of heterogeneous sizes 646, 1887 or 1913 nucleotides. A dimer and a monomer of the conserved Alu-repeats are present in the longer 3' noncoding sequences. The complete sequence of 354 amino acids for the mature enzyme was determined by sequencing both cDNA and protein. Human prostatic and lysosomal acid phosphatases exhibit 50% sequence homology, including five Cys residues and two putative N-linked glycosylation sites. The Acp-3 gene coding for human prostatic acid phosphatase was mapped onto chromosome 3 in this investigation. The Acp-2 gene coding for lysosomal acid phosphatase has previously been located on chromosome 11, while the Acp-1 gene coding for red blood cell acid phosphatase is on chromosome 2.

Acid Phosphatase↗
PubMed1985

Cytochemistry and biochemistry of acid phosphatases. VI: Immunoelectron microscopic studies on human prostatic and leukocytic acid phosphatases.

Using different antisera against secretory and lysosomal prostatic acid phosphatases, the localization of the respective antigens was studied in the human prostate at the ultrastructural level. Secretory acid phosphatase was confined exclusively to the secretory vacuoles of the glandular cells. Discharge of the secretory material occurs in a merocrine type of secretion. The identical antigen could be localized in the primary and secondary granules of neutrophil and eosinophil granulocytes separated from human peripheral blood. The antiserum used was also cross-reactive with the canine prostate, where a very distinct immunoreaction was observed with the secretory granules of the glandular cells. The antibodies directed against lysosomal acid phosphatases prepared from prostatic homogenates consistently gave a positive immunoreaction with dense bodies, lipofuscin, and secretory granules. The respective antigens were present also in neutrophil and eosinophil granulocytes. These findings do not identify the existence of a prostate-specific acid phosphatase, which does not exist. The secretory form of the isoenzymes, however, is clearly distinct from the lysosomal form, both of which are present in granulocytes. Therefore the origin of acid phosphatases elevated in peripheral blood in cases of metastatic prostatic cancer could be either the carcinomatous cells or leukocytes destroyed during the process of metastasis.

Acid Phosphatase↗
PubMed2001

Alkaline fixation-resistant acid phosphatases in human tissues: histochemical evidence for a new type of acid phosphatase in endothelial, endometrial and neuronal sites.

The effect of pH during formalin fixation on acid phosphatases in human tissues was studied. Lysosomal-type acid phosphatase was sensitive to alkaline fixation, being completely inactive after fixation at pH 9.0. Prostatic and tartrate-resistant osteoclastic/macrophagic types were alkaline fixation-resistant, as was an acid phosphatase localized in endothelium, endometrial stromal cells and intestinal nerves. The latter activity was further separable into fluoride- and tartrate-sensitive beta-glycerophosphatase and fluoride-sensitive, tartrate-resistant alpha-naphthyl phosphatase. The activities appeared to represent either different, tightly associated enzymes or separate activity centres of a single enzyme. Alkaline fixation-resistant alpha-naphthyl phosphatase at endothelial, endometrial and neuronal sites was also well demonstrated in unfixed or neutral formalin-fixed sections as tartrate-resistant activity similar to classical tartrate-resistant acid phosphatase, but these phosphatases appear to be antigenically different. Alkaline fixation-resistant acid phosphatase showed a restricted tissue distribution both in endothelium (mainly in vessels of abdominal organs) and at neuronal sites (only in intestinal nerves). Alkaline fixation-resistant acid phosphatase appears to represent a previously unknown or uncharacterized enzyme activity whose chemical properties could not be classified as any previously known type of acid or other phosphatases.

Acid Phosphatase↗
PubMed1975

[Genetico-biochemical study of acid phosphatases in Saccharomyces cerevisiae yeast. V. Genetic control of regulation of acid phosphatase II synthesis].

Regulation of exocellular enzyme acid phosphatase 2 synthesis is studied. 21 mutants with consitutive synthesis of this enzyme are obtained by UV-irradiation. All mutants were recessive and were distributed among 3 complementation groups ACP80, ACP81, ACP82. Two groups, ACP80 and ACP81 corresponded to two different genes, which showed no linkage with ACP1, ACP2 and PHO1 genes. The type of synthesis of acid phosphatase 2 in strains acp1 acp80, acp1 acp81, acp2 acp80, acp2 acp81 is determined, and a conclusion is made about the participation of ACP2 gene in the regulation of acid phosphatase 2 synthesis. It is shown that some mutations in PHO1 gene, which block the activity of acid phosphatase 1, influence the activity and regulation of acid phosphatase 2.

Acid Phosphatase↗
PubMed1983

Acid phosphatases of the human placenta, characterization and immunological comparison with prostatic acid phosphatase.

Four different acid phosphatases, denoted A1, A2, B and C, were separated from human placental homogenates. The enzymes A1, A2 and B were separated from enzyme C by binding to concanavalin A-Sepharose. Although the A1, A2 and B enzymes were all strongly inhibited by L-tartrate, only the A1 enzyme bound by affinity chromatography to L-tartrate-Sepharose. The A2 and B enzymes were separated on DEAE-cellulose. A1, A2 and B had molecular weights about 95,000. Enzyme B had high KM, whereas enzymes A1 and A2 had low KM. The enzymes A1 and A2 bound to antibodies raised against prostatic acid phosphatase, whereas the enzymes B and C did not.

Acid Phosphatase↗
PubMed1976

Production of specific antibody to purified prostatic acid phosphatase.

Prostatic acid phosphatase may well be a prime antigenic protein in prostatic tissue and fluid. Extraction of the enzyme in highly purified form from prostatic fluid and benign hypertrophic prostatic tissue provides a unique antigen capable of inducing a prompt and specific antibody response in the goat and rabbit as amnifested by immunodiffusion, immunoelectrophoresis, and immunofluorescence techniques. In prostatic cancer patients with elevated serum acid phosphatase levels it is possible to detect humoral circulating PAP antigen by standard immunoelectrophoretic methods and to confirm the existence of the enzyme by radioautography, L-tartrate inhibition, and the Gomori or Burstone staining procedures. Preliminary indirect prostatic immunofluorescence studies consistently demonstrated characteristic fluorescent foci in the paranuclear areas of benign prostatic epithelial cells, the presumed area of synthesis of prostatic acid phosphatase. Consideration has been given to the possibility of the development of a radioimmunoassay for prostatic acid phosphataase utilizing a heterolologous antiserum to the enzyme extracted from human prostatic fluid.

Acid Phosphatase↗
PubMed1990

Alkaline phosphatase and phosphoamino acid phosphatases in normal and cancerous tissues of the human larynx.

The activities of alkaline phosphatase and phosphoamino acid phosphatases were measured in normal and cancerous regions of the human larynx. For each larynx, alkaline phosphatase and phosphotyrosine phosphatase activities were higher in the tumor than in the corresponding normal tissue. Phosphothreonine and phosphoserine phosphatase activities were relatively low and there were no consistent trends. The increased alkaline phosphatase activity in the tumors supports histological observations that ossification of cartilage seems to occur at the site of invasion; the phosphatase acting on phosphotyrosine could serve as a regulator of cell differentiation during tumorigenesis.

Adult↗
PubMed2000

Secretion of an acid phosphatase (SapM) by Mycobacterium tuberculosis that is similar to eukaryotic acid phosphatases.

Mycobacterium tuberculosis secretes a large number of polypeptides with broad biological and immunological functions. We describe here the characterization of a 28-kDa acid phosphatase of M. tuberculosis (SapM) localized to the culture filtrate. The mature protein demonstrated biochemical characteristics similar to those of the bacterial nonspecific acid phosphatases. However, SapM yielded significant sequence homology to fungal acid phosphatases and not those of bacteria. Thus, SapM may represent a new class of bacterial nonspecific acid phosphatases.

Acid Phosphatase↗
PubMed1984

Multiple acid phosphatases in avian pectoral muscle--the postmicrosomal supernatant acid phosphatase is elevated in avian dystrophic muscle.

There are at least three forms of acid phosphatase in avian pectoralis muscle differing in molecular weight, subcellular location, and response to various substrates and inhibitors. These enzymes are separated by differential sedimentation into postmicrosomal supernatant, lysosomal, and microsomal activities with apparent molecular weights in Triton X-100 of 68,000, 198,000, and 365,000, respectively. All of the enzymes show acid pH optima (pH approximately 5), but the postmicrosomal supernatant form is distinctly different from the other two forms in its resistance to most common phosphatase inhibitors and in its reduced activity against several organic phosphates. Quantitation of these three forms of acid phosphatase in normal and dystrophic avian pectoralis muscle shows that the postmicrosomal supernatant form is significantly elevated in dystrophic muscle; at 33 days ex ovo, 84% of the increased acid phosphatase activity in dystrophic muscle can be attributed to the postmicrosomal supernatant form. The microsomal form is only slightly elevated; the level of the lysosomal form is not altered.

Acid Phosphatase↗
PubMed1975

[Genetic-biochemical study of acid phosphatases from Saccharomyces cerevisiae yeasts. IV. Genetic control of acid phosphatase II activity].

Genetic control of exocellular acid phosphatase of yeast Saccharomyces cerevisiae (acph 2) is studied. 64 mutants with the impaired activity of acid phosphatase have been obtained by UV-irradiation. All the mutations have been distributed among 4 genes: ACP1, ACP2, ACP3, ACP4 using functional and recombinational tests for allelism. It is shown that mutations in genes ACP1--ACP3 are recessive, but in the gene ACP4--dominant. The gene ACP4 is found to be located 0.41+/-0.064 in strains from centromere and to have no linkage with ACP1. Possible functions of genes studied are under discussion.

Acid Phosphatase↗
PubMed2005

N-glycosylation influences the latency and catalytic properties of mammalian purple acid phosphatase.

Purple acid phosphatase (PAP), also known as tartrate-resistant acid phosphatase or uteroferrin, contains two potential consensus N-glycosylation sites at Asn(97) and Asn(128). In this study, endogenous rat bone PAP was found to possess similar N-glycan structures as rat recombinant PAP heterologously expressed in baculovirus-infected Sf9 insect cells. PAP from Sf9 cells was shown to contain two N-linked oligosaccharides, whereas PAP expressed by mammalian CHO-K1 cells was less extensively glycosylated. The extent of N-glycosylation affected the catalytic properties of the enzyme, as N97Q and N128Q mutants, containing a single oligosaccharide chain, exhibited a lower substrate affinity and catalytic activity compared to those of the fully glycosylated PAP in the native, monomeric state. The differences in substrate affinity and catalytic activity were abolished and partially restored, respectively, by proteolytic cleavage in the loop domain, indicating that the extent of N-glycosylation influences the interaction of the repressive loop domain with catalytically important residues.

Acid Phosphatase↗
PubMed1987

Effect of prolactin and androgens on the prostate of bonnet monkeys, Macaca radiata: I. Nucleic acids, phosphatases, and citric acid.

The effects of prolactin (PRL), bromocriptine (Br), testosterone propionate (TP), dihydrotestosterone (DHT), and the combinations of these androgens with PRL/Br on the growth and secretory activities of cranial and caudal prostates were studied in castrated mature monkeys, Macaca radiata. Castration decreased the body weight, organ weights, nucleic acids (DNA and RNA), phosphatases, and citric acid of cranial and caudal prostates. PRL did not alter the body weight but increased the organ weights, nucleic acids, phosphatase activities, and citric acid. Br given alone decreased the body weight and the secretory activities of prostates but caused no significant alteration in the nucleic acids. TP/DHT replacement brought back the body weight and prostatic nucleic acids to normal. It enhanced the weights, phosphatase activities, and citric acid contents of cranial and caudal prostates. PRL + TP/DHT enhanced the body weight, organ weight, and secretory activities. Br + TP/DHT decreased the body weight and secretory products of prostate but it did not produce any alteration in the organ weight and RNA content. These results suggest that PRL plays a specific stimulatory influence on monkey prostate.

Androgens↗
PubMed1990

Prostatic acid phosphatase in serum of patients with prostatic cancer is a specific phosphotyrosine acid phosphatase.

We developed an assay to measure at acid pH the phosphotyrosine phosphatase activity in sera from patients with prostatic cancer. The method used quantifies the inorganic phosphate liberated from phosphotyrosine after incubation with serum, followed by the deproteinization of the reaction mixture. A high acid phosphatase (EC 3.1.3.2) activity towards phosphotyrosine was observed in all sera from patients with increased activity of prostatic acid phosphatase. This activity represented 96% of prostatic acid phosphatase and 77% of total acid phosphatase activities. Moreover, it was correlated (r = 0.91) with the amount of serum prostatic acid phosphatase determined by radioimmunoassay. When serum acid phosphatase activity was measured on several phosphorylated substrates, preferential hydrolysis was demonstrated for those in which the phosphate group was esterified on an aromatic ring rather than those presenting an aliphatic chain. Among phosphoamino acids, only phosphotyrosine was a good substrate, with little or no activity observed with phosphoserine and phosphothreonine. Human seminal plasma and partially purified prostatic acid phosphatase, tested for their activity on some of these substrates, gave similar results. On the other hand, sera from patients with above-normal alkaline phosphatase activity and no prostatic disease showed little or no activity on phosphotyrosine at both acid and alkaline pH values. Evidence is presented that the prostatic acid phosphatase in serum is a specific phosphotyrosine acid phosphatase.

Acid Phosphatase↗
PubMed1991

Purification, characterization, and subcellular localization of an acid phosphatase from black mustard cell-suspension cultures: comparison with phosphoenolpyruvate phosphatase.

An acid phosphatase from Brassica nigra (black mustard) leaf petiole cell-suspension cultures has been purified 1633-fold to a final specific activity of 1225 (mumols orthophosphate produced/min)/mg protein and near homogeneity. The native protein was a glycosylated monomer having a molecular mass of 60 kDa and a pI of 4.5. The enzyme displayed a broad pH optimum of about pH 5.6 and was heat stable. The final preparation hydrolyzed a wide variety of phosphate esters. The highest specificity constants were obtained with 3-phosphoglycerate, 2,3-diphosphoglycerate, PPi, and phosphoenolpyruvate (PEP). The enzyme was activated 1.4-fold by 4 mM Mg2+ or Mn2+, but was strongly inhibited by Mo, Pi, F, and several phosphorylated compounds. Subcellular localization experiments revealed that this nonspecific acid phosphatase is probably a secreted enzyme, localized in the cell wall. By contrast, B. nigra PEP phosphatase appeared to be localized in the cell vacuole. Peptide mapping via CNBr fragmentation was employed to investigate the structural relatedness of the two phosphatases. Their respective CNBr cleavage patterns were dissimilar, suggesting that B. nigra acid and PEP phosphatases are distinct polypeptides. Putative metabolic functions of these two phosphatases are discussed in relation to the biochemical adaptations of B. nigra cell-suspension cultures to nutritional phosphate deprivation.

Acid Phosphatase↗
PubMed1981

Immunohistochemistry of acid phosphatase in the human prostate: normal and pathologic. Cytochemistry and biochemistry of acid phosphatases II.

Three different antisera against human prostatic acid phosphatase were used for direct and indirect immunohistochemical demonstration of acid phosphatase in paraffin sections of infantile and adult normal, hyperplastic and carcinomatous prostatic tissue. All antisera were prepared in rabbits. Antiserum A was prepared from highly purified acid phosphatase extracted from autopsy specimens. Antiserum B was a concentrate of a commercial antiserum used in radioimmunoassay and was prepared from purified extracts of human seminal fluid. Antiserum C was a peroxidase-conjugated antiserum prepared from purified extracts of human seminal fluid. The specificity of the three antisera was compared using different immunohistochemical methods and tissues. It was comparably high in all three antisera which gave only slightly different staining results in prostatic tissue. The staining results in prostatic carcinoma were only dependent on the titer of the respective antiserum. Carcinomas with a cribriform growth pattern showed variable staining, but always had a positive immunoreactions, provided the titer of the antiserum was sufficiently high. Striking differences were observed in metaplastic, atrophic and hyperplastic prostatic epithelium. The most intense reaction was observed in atrophic glands: it was much less intense in hyperplastic and normal epithelium and negative or slightly positive in metaplastic epithelium.

Acid Phosphatase↗