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PubMed1965

The deceptive acid phosphatases.

Determination of the prostatic acid phosphatase is, theoretically, a specific test for carcinoma of the prostate, but the present laboratory techniques have produced too many false positives and false negatives to be dependable. There may be inhibitors or enzymes that interfere with these tests. Until more exact enzymes are discovered, the present acid phosphatases should not be depended upon as a criterion for the type of surgical operation in carcinoma of the prostate, nor, without biopsy, should they be taken as an indication of prostatic malignant disease.

Acid Phosphatase↗
PubMed1986

Cytochemical localization of acid phosphatase in Leishmania mexicana amazonensis.

Acid phosphatase was cytochemically detected at the ultrastructural level in infective and non-infective promastigotes and in amastigotes of the parasitic protozoan Leishmania mexicana amazonensis. Cerium chloride was used as the capture agent of the phosphate liberated during the hydrolysis of the substrate (Na-beta-glycerophosphate). Reaction product, indicative of enzyme activity, was seen in the outer face of the plasma membrane of many, but not all, infective and noninfective promastigote forms. No reaction product was seen in the plasma membrane of amastigote forms. Reaction product was seen in the endoplasmic reticulum, in the Golgi complex, in vesicles located close to the flagellar pocket and in cytoplasmic structures which may represent lysosomes. No reaction product was seen when the substrate was omitted from or sodium fluoride was added to the incubation medium. The possible role played by the acid phosphatase present in the plasma membrane of Leishmania parasites is discussed.

Acid Phosphatase↗
PubMed1991

[Histochemistry of acid phosphatase in small intestine mucosa in experimental coccidiosis in suckling piglets].

The activity of acid phosphatase (phosphohydrolase of orthophosphate monoesters; EC. 3.1.3.2) was evaluated densitometrically in the mucosa of duodenum, jejunum and ileum of 22 conventional piglets which were experimentally infected by oocysts of the coccidiae Isospora suis (infection dose of 200,000 oocysts) on day one after parturition (DAP). The activity of the studied hydrolase was investigated in the infected piglets during days two to ten after infection (DAI) in the intestinal mucosa (enterocytes) and in goblet cells. The density of the reaction product of acid phosphatase was simultaneously determined in the same mucosal cells of different sections of the small intestine in five control conventional piglets at the age of 2-14 days. In the small intestine mucosa of control piglets the activity of acid phosphatase was demonstrated to be located especially in the supranuclear zone of enterocytes. As for goblet cells, the reaction product of acid phosphatase is distributed in all zones (supra-, para-, infranuclear zones); the lowest density of this enzyme was found in the infranuclear zone. The activity of acid phosphatase is also localized in intestinal crypts: in their cells the enzyme concentration is decreasing from duodenum to caudal sections. Important changes were revealed, in comparison with the control data, in the development of the activity of acid phosphatase in the intestinal mucosa cells in the experimentally infected piglets. In the period of investigation (DAI 2-10) there were two stages of the development of the density of the enzyme reaction product. The first stage can be characterized by an increase, the other by a decrease in the level of acid phosphatase activity. Enterocytes are influenced in both stages, but the decrease in the density of the reaction product of acid phosphatase was observed only in absorption cells, and not in goblet cells. The increase in the activity of acid phosphatase occurs in the periods of DAI 4 and 9-10. Enzymatic deviations occur mainly in the absorption cells of the mucosa of duodenum and middle jejunum; in the cells of posterior jejunum and ileum an increase in the density of the reaction product of acid phosphatase was also demonstrated, but at the lower quantitative level (especially on DAI 4). The decrease in the activity of acid phosphatase has a protracted development and it takes place on DAI 5 to 8.(ABSTRACT TRUNCATED AT 400 WORDS)

Acid Phosphatase↗
PubMed1985

An enzyme-amplified monoclonal immunoenzymometric assay for prostatic acid phosphatase.

An immunoassay for prostatic acid phosphatase is described in which a high degree of specificity for the prostatic isoenzyme, obtained by the use of monoclonal antibodies, is combined with great sensitivity, made possible by enzyme-amplified measurement of the combination of the isoenzyme with its antibody. The increase in sensitivity thus achieved is of the order of 170 times that of conventional methods of measurement. The advantages of the enzyme-amplified method have been shown to be particularly useful in detecting and monitoring small abnormalities of prostatic acid phosphatase levels in patients with prostatic cancer.

Acid Phosphatase↗
PubMed1979

Sézary syndrome. Tartrate-resistant acid phosphatase in the neoplastic cells.

Tartrate-resistant acid phosphatase has been known to be of diagnostic value in hairy cell leukemia. However, occasionally neoplastic cells of other varieties of lymphoproliferative disorders may contain tartrate-resistant acid phosphatase. The authors have studied four patients with Sézary syndrome who had typical cutaneous lesions with extensive lymphoid infiltrates and circulating atypical E-rosetting lymphoid cells. The abnormal Sézary cells accounted for 23-69% of the peripheral mononuclear cells and often showed convoluted or folded nuclei. These cells in all four patients were strongly positive for acid phosphatase resistant to tartaric acid inhibition. Enzymatic cytochemical studies for acid phosphatase with and without tartrate may be helpful in the differential diagnosis of cutaneous T-cell lymphomas from variants of chronic dermatitis.

Acid Phosphatase↗
PubMed2004

Characterization and properties of acid phosphatases with phytase activity produced by Aspergillus caespitosus.

High levels of thermostable acid phosphatases were produced by Aspergillus caespitosus in culture media supplemented with xylan birchwood or agricultural residues, as carbon sources. The optimal culture conditions for production of phosphatases were 40 degrees C and pH 6.0. Extra- and intra-cellular acid phosphatases were purified by chromatography on DEAE-cellulose, followed by concanavalin A-Sepharose affinity separation. Both extra- and intra-cellular enzymes were glycoproteins showing 63.0 and 58.3% of carbohydrate content respectively. Molecular masses estimated on Sepharose CL-6B column were 186 and 190+/-15 kDa, and 84 and 74+/-5 kDa according to SDS/PAGE, for extra- and intra-cellular acid phosphatases respectively. Taken together, these results suggest that both native enzymes were homodimers. Optimum temperature and pH for both phosphatase activities were 80 degrees C and 5.5 respectively. The extra- and intra-cellular acid phosphatases were stable for more than 60 min at 60 degrees C. The extracellular acid phosphatase was slightly inhibited by NaF, in contrast with the significant inhibition of the intracellular form. KH(2)PO(4) inhibited both activities equally. Both extra- and intracellular acid phosphatases were tartarate-resistant. Among several phosphorylated substrates used, the extracellular enzyme preferentially hydrolysed p-nitrophenyl phosphate. Kinetic parameters calculated for the hydrolysis of p-nitrophenyl phosphate by extracellular acid phosphatase were h (Hill coefficient)=1.2, K(0.5)=0.082 mM and V(max)=4.43 units/mg, whereas the intracellular enzyme exhibited Michaelian kinetics with K(m)=0.029 mM and V(max)=0.082 unit/mg. Phytase activity was also observed for both the enzymes, suggesting that they could be useful for biotechnological applications.

6-Phytase↗
PubMed1986

Phosphatase cytochemistry with cerium as trapping agent. Verification of acid phosphatase and glucose-6-phosphatase reactive sites.

Lead is prevalently replaced by cerium as trapping agent in phosphatase cytochemistry to prevent non-specific precipitation. Recently, substrate specific but artefactual lead precipitates have been described in the nuclear envelope (NE) and rough endoplasmic reticulum (RER) due to a local matrix effect. In the present study a verification was carried out of the localization of acid phosphatase and glucose-6-phosphatase in the NE and RER of rat peritoneal macrophages and hepatocytes respectively with cerium. It appeared that precipitates of cerium phosphate in NE and RER of peritoneal macrophages do not represent sites of acid phosphatase activity but are due to the matrix effect. However, in rat hepatocytes these organelles demonstrate true reactive sites for glucose-6-phosphatase.

Acid Phosphatase↗
PubMed1984

Kinetic analysis of chemical reactions coupled to an enzymic step. Application to acid phosphatase assay with Fast Red.

Acid phosphatase assay with alpha-naphthyl phosphate as substrate and the use of diazonium salt (Fast Red TR) for chromophore formation was kinetically analysed as a system of two chemical reactions coupled to an enzymic reaction. This system follows a mechanism defined as enzymic-chemical-chemical (EzCC). The accumulation of chromophore with reaction time presented a marked lag period, which was only dependent on the rate constants of the chemical reactions and was independent of the enzymic step. The specific rate constants of each chemical step were determined in 3.8-5.0 pH and 10-35 degrees C temperature ranges. Thermodynamic parameters of the chemical steps were also obtained. Measurement of acid phosphatase activity can be carried out in the pH range 3.8-5.0 (4.8 was optimal pH) without the need to eliminate the lag period.

Acid Phosphatase↗
PubMed1984

Monoclonal antibody-based radioimmunoassay compared with conventional enzyme immunoassay in the detection of prostatic acid phosphatase.

Determination of serum prostatic acid phosphatase by a monoclonal antibody-based radioimmunoassay (RIA) was compared to a polyclonal antibody-based enzyme immunoassay (EIA) to study the clinical value of both test systems. The 97.5 percentile of 48 patients with histologically proven benign prostatic hyperplasia (BPH) was chosen as the normal range. The classification of 38 patients with prostatic carcinoma (CaP) stage pT1-3N0-3M0 was performed by radical prostatectomy and/or pelvic lymph node dissection. Elevated prostatic acid phosphatase (PAP) serum concentrations were observed in 1 of 26 patients with CaP stage pT1-3N0M0 by the EIA and in 7 of 12 patients with CaP stage pT1-3N1-3M0 in both assays. Distant metastases observed in 15 patients lead to elevated PAP serum concentrations in 12 patients by the RIA and in 13 patients by the EIA. The correlation coefficient of both test systems was 0.97. These data indicate that the determination of PAP by a monoclonal antibody-based RIA is of no advantage compared to polyclonal antibody-based EIA, though both test systems are suitable for the follow-up of patients with CaP. Early recognition of CaP, however, is not possible by these two test systems. Elevated serum concentrations of PAP in both assays indicated metastatic disease. These findings should be considered if a curative treatment of CaP is planned.

Acid Phosphatase↗
PubMed1990

Development of an immunoassay for human serum osteoclastic tartrate-resistant acid phosphatase.

A tartrate-resistant acid phosphatase (TrACP), which has been suggested to be very similar to the osteoclastic TrACP, was partially purified from the spleen of a patient with hairy cell leukemia. The purification procedure consisted of carboxymethyl-Sepharose, phosphocellulose, Sephacryl S-200, and phenyl-Sepharose chromatographies. Polyclonal antibodies were generated in guinea pigs with a titer of at least 1:6000. Immunohistochemical staining of fetal rat tibia with the antisera revealed that only the lysosomes of osteoclasts, but not osteoblasts, were stained. An enzyme-linked immunosorbent assay (ELISA) was developed with the antisera. There was no cross-reactivity with 1) partially purified acid phosphatases (ACPs) from normal human and beef spleens, 2) ACPs in extracts of human osteoblastic cells, 3) purified bovine bone matrix TrACP, or 4) commercial prostatic ACP. However, extracts of giant cell bone tumors, containing large amounts of bona fide osteoclasts, showed large amounts of cross-reactive material, which diluted in parallel with the partially purified hairy cell leukemic TrACP in the ELISA. Commercial serum band 5b TrACP also displaced in parallel with the partially purified hairy cell leukemic TrACP. Immunoblotting studies revealed that the antiserum, but not nonimmune guinea pig serum, reacted with the homogeneous hairy cell leukemia splenic band 5 TrACPs, which were recently purified by our laboratory. Preliminary application of the ELISA to sera of patients with metabolic bone diseases revealed that normal healthy individuals had measurable amounts of the immunoreactive material, and patients with Paget's disease or hyperparathyroidism, who should have high bone turnover, had elevated levels of this immunoreactive material in their sera. In contrast, the level of serum osteoclastic TrACP in a patient with an acute lymphatic leukemia was normal. In summary, 1) we have shown that hairy cell leukemia splenic TrACP shares significant immunological similarity with the osteoclastic TrACP and with the serum band 5b TrACP, and 2) the ELISA holds promise for a sensitive and specific assay for bone resorption.

Acid Phosphatase↗
PubMed1976

A labile acid phosphatase isozyme associated with the surface of vegetative Dictyostelium discoideum cells.

A minor acid phosphatase isozyme (acid phosphatase I) of vegetative Dictyostelium discoideum amebae has been shown to be associated exclusively with the external surface of the plasma membrane. The isozyme is not present in phagocytic vacuoles isolated with latex beads. The isozyme disappears from cells removed from nutrient medium and does not reappear during differentiation. When inhibitors of protein synthesis (e.g. cycloheximide, chloral hydrate, concanavalin A) are added to cells growing in nutrient medium, acid phosphatase I is rapidly lost. It appears that the level of protein synthesis need only be moderately reduced (less than 25%) to induce loss of enzyme activity. Treatment with inhibitors of DNA and RNA synthesis for up to 2 h had no effect on isozyme activity. It is postulated that the cells are able to "sense" (through the reduction in levels of protein synthesis) when external conditions become unfavorable, and immediately respond by reducing the activity of enzymes involved in maintaining contact with the extracellular environment. The closed system thought necessary for differentiation would then be created.

Acid Phosphatase↗
PubMed1979

Photoreceptor membrane breakdown in the spider Dinopis: localisation of acid phosphatases.

The ultrastructural localisation of acid phosphatases (AcPhs) during the normal daily breakdown of rhabdomere membrane in Dinopis has been examined using beta-glycerophosphate and p-nitrophenyl phosphate as substrates. Results are related to the classification of organelles in the receptors given by Blest, Powell and Kao (1978). Weak and infrequent reactions are obtained in multivesicular bodies (mvbs) and multilamellar bodies (mlbs) derived from them. Residual bodies (rbs) begin to react strongly as they lyse. Source of AcPhs is endoplasmic reticulum which has barely differentiated towards the GERL configuration; it becomes reactive as it is incorporated into secondary lysosomes. GERL tubules, Y-bodies and vesicles respond erratically and weakly, and are also incorporated into rbs. No evidence was found for a significant participation of Golgi bodies in these processes, and acid phosphatase cytochemistry fails to reveal a topographical relationship between GERL in these cells and Golgi saccules. Coated vesicle clusters found in the predawn receptive segments are AcPh-negative; this implies that their previous identification as GERL-derived "Nebenkerne" carrying hydrolytic enzymes to newly-formed mvbs (Blest, Kao and Powell, 1978) is dubious. Isolation bodies and autophagic vacuoles enclosing other organelles in pathological receptors give strong reactions while adjacent secondary lysosomes derived from rhabdomere membrane and associated GERL give weak ones. It is concluded that rhabdomere-derived rb lysis is more tightly regulated than other autophagic processes, and it is suggested that a high degree of control is necessary in a receptor which may repeat the autophagy of a large mass of transductive membrane at least 60--100 times in the course of its working life.

Acid Phosphatase↗
PubMed1986

Bile salt related secretion of acid phosphatase in rat bile.

The biliary excretion of bile salts, lysosomal acid phosphatase, and total proteins were studied in rats under different experimental conditions: during bile salt loss through a bile fistula and after loading with exogenous sodium taurocholate. The experimental models were suitable to demonstrate that variations in the excretion of bile salts were associated with those of acid phosphatase output. During bile salt depletion, acid phosphatase output showed a decrease parallel to that of bile salts. Following a single i.v. injection of sodium taurocholate and during its i.v. infusion, a rapid increase of acid phosphatase excretion in bile was seen. The patterns of enzyme outputs observed after administration of sodium taurocholate suggested a bulk discharge in bile of lysosomal contents. The profiles of protein output were similar to those of acid phosphatase suggesting an association between the secretory mechanism of these bile constituents. In contrast to sodium taurocholate, 4-methylumbelliferone, which also increases canalicular bile flow, did not produce changes in the excretory patterns of the bile components studied. Therefore, the results suggested a bile salt related secretion of acid phosphatase in the rat, which may involve protein secretion in bile.

Acid Phosphatase↗
PubMed1990

Alterations to N-linked oligosaccharides which affect intracellular transport rates and regulated secretion but not sorting of lysosomal acid phosphatase in Dictyostelium discoideum.

The importance of N-linked oligosaccharides and their associated modifications in the transport, sorting, and secretion of lysosomal acid phosphatase was investigated using three mutant Dictyostelium cell lines. These mutants synthesize altered N-linked oligosaccharides with the following properties: (i) in strain HL244 carbohydrate side chains lack mannose 6-sulfate residues, (ii) in strain M31 the side chains retain the two alpha-1,3-linked glucose residues resulting in less sulfate and methylphosphate modifications, and (iii) in strain HL243 the nonglucosylated branches are missing three of the outer mannose sugars and the oligosaccharides contain fewer sulfate and phosphate modifications. Lysosomal enzymes in both HL243 and HL244 are also missing a shared epitope termed common antigen-1 (CA-1), which consists in part of mannose 6-sulfate moieties. No increases were observed in the secretion of radiolabeled acid phosphatase or acid phosphatase activity during growth in any of the mutant cell lines, suggesting that the enzyme was correctly sorted to lysosomes. In support of this, Percoll gradient fractionations and indirect immunofluorescence microscopy indicated that acid phosphatase was transported to lysosomes in all cell lines. However, radiolabel pulse chase protocols indicated that newly synthesized acid phosphatase was transported out of the endoplasmic reticulum (ER) and into lysosomes at a two- to threefold slower rate in HL243 and at a sixfold slower rate in M31. The rate of transport of acid phosphatase from the ER to the Golgi was reduced only twofold in M31 as determined by digestion of newly synthesized enzyme with endoglycosidose H. This suggests that certain alterations in carbohydrate structure may only slightly affect transport of the enzyme from the ER to the Golgi but these alterations may greatly delay transport from the Golgi or post-Golgi compartments to lysosomes. Finally all three mutants secreted acid phosphatase at significantly lower rates than the wild-type strain when growing cells were placed in a buffered salt solution (conditions which stimulate the secretion of mature lysosomally localized enzymes). In contrast, alpha-mannosidase was secreted with similar kinetics from the mutant and wild-type strains. Together, these results suggest that the mechanism(s) operating to sort acid phosphatase in Dictyostelium can tolerate a wide range of changes in N-linked oligosaccharides including a reduction in phosphate and the absence of CA-1 and sulfate, while in contrast, these same alterations can profoundly influence the rate of transport of acid phosphatase from the ER and post-ER compartments to lysosomes as well as the secr

Acetylglucosaminidase↗
PubMed1984

A histochemical comparison of acid phosphatase activity in human BPH and rat ventral prostate.

Acid phosphatase activity and its sensitivity to formalin inhibition were compared histochemically in cryostat sections of human BPH and rat ventral prostate. While the glandular epithelium in both human and young adult rat ventral prostate exhibits positive acid phosphatase activity, the intensity of the reaction is greater in human tissue. Moreover, human prostatic tissue remains acid phosphatase positive following 24 hours immersion in formalin, whereas the enzyme reaction in young adult rat ventral prostate disappears after 5 hours of formalin treatment. Unlike both human and young adult rat ventral prostate, sites of acid phosphatase activity in aged rat ventral prostate are not homogeneously distributed throughout the glandular epithelium but, rather, appear as large clumps, which persist after 5 hours of formalin treatment. Procedures used for the histochemical demonstration of formalin-resistant human prostatic acid phosphatase are not, therefore, directly applicable to rat ventral prostate.

Acid Phosphatase↗
PubMed1979

Polymorphism of acid phosphatase in chicken leucocytes.

Three individual variants of acid phosphatase in chicken leucocytes were found by means of starch gel electrophoresis. The phenotype in leucocytes showed the same appearance as polymorphic forms of liver acid phosphatase in the same bird. The study of the Hardy-Weinberg distribution of the phenotypes of acid phosphatase in leucocytes also indicated that they are controlled by the same pair of codominant autosomal alleles as the phenotypes in the liver. Acid phosphatase is polymorphic in all six strains of chickens studied.

Acid Phosphatase↗
PubMed1983

Prostatic acid phosphatase in serum and bone marrow in patients with prostatic carcinoma.

Sixty-two per cent of 61 patients with prostatic carcinoma showed elevated levels of serum acid phosphatase, analysed by radioimmunoassay (RIA). Enzymatically determined serum acid phosphatase was raised in only 38% of the same patients. Bone marrow acid phosphatase determined by RIA was raised in 41%. In untreated metastatic patients with prostatic carcinoma, radioimmunologically determined serum acid phosphatase was elevated in 12 of 13 patients, whereas bone marrow acid phosphatase (RIA) and enzymatically determined serum prostatic acid phosphatase were increased only in about half of the patients. In a control group the upper reference limit of bone marrow acid phosphatase determined by RIA was significantly raised above that obtained by serum analyses. This indicates that nonprostatic acid phosphatases (possibly from bone marrow cells) cross-react with prostatic acid phosphatase in an unpredictable way, even when using a specific radioimmunoassay. In patients with metastatic carcinoma of the prostate, the results of bone marrow acid phosphatase determinations, analysed by RIA, seem to lack diagnostic and/or prognostic information additional to that obtainable by serum acid phosphatase (RIA) analysis.

Acid Phosphatase↗
PubMed1995

Single-step purification of prostatic acid phosphatase: immunoaffinity chromatography with a monoclonal antibody.

BACKGROUND: Prostatic acid phosphatase (PAP) is an important protein which should be studied further as a tumor marker or as a biologically functional molecule. The purpose of the study was to establish a simple and reliable method to obtain highly pure PAP. METHODS: Spleen cells from mice immunized with prostatic epithelial cells prepared from benign prostatic hyperplasia tissue were fused with myeloma cells X63Ag8-653. Hybrid cells of interest were selected using the indirect immunofluorescence method with unfixed frozen tissue sections. One clone of the hybrid cell lines was established which secreted the monoclonal antibody specifically reactive to prostatic acid phosphatase. Using this monoclonal antibody, we purified the antigen from human prostatic tissue by means of single-step immunoaffinity chromatography. RESULTS: SDS-PAGE profiling under reducing conditions indicated that the protein recognized by this antibody consisted of several components of molecular weight 41,000-45,000. Partial amino acid sequence analysis of this protein indicated that these components involved a heterogeneously modified single polypeptide, and that this antigen is identical to human prostatic acid phosphatase. CONCLUSIONS: This single-step method saves the time needed to purify prostatic acid phosphatase and requires only half a day for the whole procedure. Moreover, the purity of the isolated protein was extremely high. This method seems to be useful not only for purifying prostatic acid phosphatase but also for purifying other proteins from the prostate gland and for analysis of antigenic macromolecules.

Acid Phosphatase↗