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PubMed1988

Localization of acid phosphatase in lamellar bodies of tannic acid treated alveolar type II cells.

Acid phosphatase was demonstrated in well preserved lamellar bodies of rats' alveolar type II cells. The highly ordered lamellar organization was preserved by using tannic acid in the tissue procession protocol. Acid phosphatase reaction products were observed in the amorphous regions of the lamellar bodies adjacent to the limiting membranes and in the central core regions. No reaction product was observed in the lamellar areas. 85% +/- 5% of the lamellar bodies were positively reactive, unrelated to their size. Multivesicular bodies were only partially reactive (approx. 50%), except for those attached to lamellar bodies which all had reaction product.

Acid Phosphatase↗
PubMedDate not supplied

Rhythmic changes of some lysosomal hydrolases activity from rat liver. Rhythmic changes of acid phosphatase synthesis.

The activity of acid phosphatase (E.C.3.1.3.2.), arylsulfatase (E.C.3.1.1.23.), beta-galactosidase (E.C.3.1.1.23.), and beta-acetylglucosaminidase (E.C.3.2.1.30.) in rat liver homogenates of 4.5 month-old male rats is presented in this paper. The degradation processes are observed in rat liver homogenate after incubation. The activity of acid phosphatase and beta-acetylglucosaminidase increases, the activity in one of beta-galactosidase is constant, and arylsulfatase decreases during the time of incubation. Furthermore, the maxima of the enzyme activities shift during the incubation in the time of a day. Gel filtration of acid phosphatase on the Sephadex G-150 Superfine and DEAE-cellulose columns determinate the mutual content of acid phosphatase subunits to isoenzymes I and II in various points of a day. The greatest content of acid phosphatase subunits versus both the isoenzymes content is at 02(24), and the greatest content of isoenzyme II versus the content of isoenzymes I appears at 07(12). From these data it is clear that the period of the isoenzyme II synthesis from the subunit amounts to 5 h, while 10 h are necessary to create the isoenzyme I originated from isoenzyme II. The comparison of acid phosphatase activity before and after the homogenate filtration on the Sephadex column indicates the increase of this enzyme activity after its separation from the other proteins and other components.

Acid Phosphatase↗
PubMed1990

A possible genetic component of obesity in childhood. Observations on acid phosphatase polymorphism.

Phenotypes of acid phosphatase with low enzymatic activity (ACP1 A and BA) are correlated with the highest degree of body mass increase observed in a sample of obese children. Since acid phosphatase probably functions as a flavin-mononucleotide phosphatase, differential modulation of flavo-enzyme activity and energy metabolism due to acid phosphatase genetic variability may explain the observed association.

Acid Phosphatase↗
PubMed1989

Purification and characterization of human bone tartrate-resistant acid phosphatase.

Tartrate-resistant acid phosphatase (TRAP) is a histochemical marker for osteoclasts, the multinucleated bone resorbing cell. This type 5 acid phosphatase has been purified 500-fold from human bone by three chromatographic steps: cation exchange, gel filtration, and HPLC cation exchange. Like most other TRAPs isolated, it is a basic glycoprotein of a molecular weight about 33,000. Its pH optimum Km, and Vmax for p-nitrophenyl phosphate are 5.7, 0.8 mM, and 12 units/mg, respectively. Human bone TRAP hydrolyzes aryl phosphates, nucleoside di- and triphosphates, pyrophosphate, and phosphoproteins. It is activated by mild reducing agents but inhibited by molybdate, fluoride, arsenate, phosphate, and dithionite. Its activity is not inhibited by tartrate, a feature that distinguishes it from other acid phosphatases. Sodium etridonate, the bisphosphonate used clinically to reduce bone resorption, is a relatively poor inhibitor of bone TRAP. Human bone TRAP is immunologically related to the porcine uterine secretory TRAP, uteroferrin. Monospecific rabbit antibodies to the bone TRAP have been immunopurified by using affinity chromatography with uteroferrin immobilized on Sepharose and can be used to detect low amounts of the enzyme in a simple dot-blot assay.

Acid Phosphatase↗
PubMed1994

3-Phosphohistidine/6-phospholysine phosphatase from rat brain as acid phosphatase.

A phosphatase hydrolyzing 3-phosphohistidine and 6-phospholysine was purified from rat brain cytosol to 90% homogeneity on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. One milligram of protein of the purified phosphatase released inorganic phosphate from 3-phosphohistidine, 6-phospholysine, AMP, GMP, and p-nitrophenyl phosphate at velocities of 6.5, 15.6, 15.0, 6.9, and 8.3 mumol/min, respectively. However, the purified enzyme could not hydrolyze N omega-phosphoarginine and phosphocreatine, which are substrates for phosphoamidase [EC 3.9.1.1]. The molecular masses of the holoenzyme and the subunit were 94 and 50 kDa, respectively, and the sedimentation coefficient of the native enzyme was 6.3 s, indicating that it was a dimeric enzyme of identical subunits. The enzyme functioned well under acidic conditions, and 50% of the activity was inhibited by 30 microM tartrate, 4 microM vanadate, 20 microM molybdate, 4 microM VCl3, or 13 microM MoCl5. These results indicate that the present hydrolase belongs to the acid phosphatase group [EC 3.1.3.2].

Acid Phosphatase↗
PubMed1981

Clinical evaluation of immunological methods for detection for serum prostatic acid phosphatase.

Evaluation of serum acid phosphatase by 3 immunochemical methods (radioimmunoassay, counterimmunoelectrophoresis and immunoenzymoassay) was done in 3 groups of patients. In 42 patients wit stage D prostatic carcinoma a comparison of serum acid phosphatase determination by colorimetric assay and the 3 immunochemical methods in samples obtained before and after initiation of therapy showed an excellent correlation among the assays. Presently, we see no advantage of the immunochemical methods over the colorimetric assay in this group of patients. Among 100 patients studied in a blind fashion to detect those with unsuspected prostatic carcinoma no such cases were found. In the last group of patients with localized prostatic carcinoma staged surgically by pelvic lymphadenectomy the only elevations of serum acid phosphatase were observed in patients with extraprostatic involvement.

Acid Phosphatase↗
PubMed1979

Purification and partial characterization of two acid phosphatases from rat bone.

Acid phosphatase activity in homogenized tibiae and femora of suckling rats was extracted with 0.3M KCl and 0.1% Triton X-100. A high-speed supernatant was treated with protamine sulfate, dialyzed, and chromatographed on CM-52 cellulose. All of the acid phosphatase activity was eluted with a sodium acetate buffer and combined ionic strength-pH gradient into two peaks (E1 and E2). Both enzyme peaks were further purified with Sephadex G-200, which resulted in 700- and 1000-fold purification for E2 and E1, respectively. A total of 220 units (mumoles substrate/min) of E2 with a specific activity of 160 units/mg protein has been obtained in one run by this procedure. E1 has a high molecular weight (greater than 100,000) and shows preference for monophosphate ester substrates, is markedly inhibited by tartrate, and has a pH optimum near 5. E2 has a lower molecular weight (greater than 40,000) and shows negligible activity with monophosphate esters [except with p-nitrophenyl phosphate (p-NPP)], but high activity with ADP and ATP. E2 is unaffected by tartrate and shows a pH optimum near 6. Both enzymes are competitively inhibited by inorganic phosphate, and E2, but not E1, is markedly inhibited by p-chloromercuribenzoate. With p-NPP as substrate, E1 and E2 have distinctly different values for Km. E1 appears similar to the high molecular weight acid phosphatases of soft tissues. However, E2 appears to differ from the low molecular weight phosphatases in soft tissues with regard to substrate specificity.

Acid Phosphatase↗
PubMed1989

Targeting of lysosomal acid phosphatase with altered carbohydrate.

Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes, where it is converted into a soluble protein by a limited proteolysis (Waheed et al., 1988, EMBO J. 7, 2351-2358). Transport of human lysosomal acid phosphatase in heterologous BHK-21 cells was examined under conditions that impair mannose-6-phosphate receptor-dependent transport, N-glycosylation or processing of N-linked oligosaccharides. Targeting of lysosomal acid phosphatase to lysosomes was neither affected by antibodies blocking the mannose-6-phosphate/IGF II receptor, nor by NH4Cl, which inhibited the mannose-6-phosphate receptor-dependent targeting of soluble lysosomal enzymes. 1-Deoxynojirimycin, 1-deoxymannojirimycin and swainsonine inhibited processing of N-linked oligosaccharides in lysosomal acid phosphatase without significantly affecting its transport. Tunicamycin inhibited N-glycosylation of lysosomal acid phosphatase. The non-glycosylated lysosomal acid phosphatase polypeptides accumulated within light membranes and were not transported to dense lysosomes. These results indicate that transport of lysosomal acid phosphatase is independent of mannose-6-phosphate receptors, does not involve an acid pH-dependent step and does not require processing of N-linked oligosaccharides. N-glycosylation appears to be necessary to achieve a transport competent form of lysosomal acid phosphatase.

1-Deoxynojirimycin↗
PubMed1985

[Cancer of the prostate: prostatic acid phosphatases. Biochemical properties and assay].

The first data on acidic phosphatase were published in the beginning of the 20th century. The applications to prostatic carcinoma were performed by Gutman in 1936. The enzyme is a glycoprotein which action mechanism is similar to a histidine-phosphatase. Acidic phosphatase has been found in numerous tissues and blood-stream cells. Its structure is dimeric and glycans average 10% of the M.W. The enzyme has been assayed in serum, using numerous substrates in the presence of specific inhibitors. The best results were obtained with thymolphthalein phosphate. Improvements were done by assays in bone marrow and by the introduction of immunological technics which lead to a better appreciation of tumoral invasion.

Acid Phosphatase↗
PubMed1978

Disturbance of the machinery for the gene expression by acidic pH in the repressible acid phosphatase system of Saccharomyces cerevisiae.

When the pH of growth medium containing a limited amount of inorganic phosphate is kept below 3.0, cells of Saccharomyces cerevisiae produce repressible alkaline phosphatase but no repressible acid phosphatase. The same cells produce acid phosphatase immediately on shifting the medium pH to 4.0 or above. Like intact cells, spheroplasts prepared from cells grown at pH 3.0 or 4.5 in medium with a limited amount of inorganic phosphate in suspension begin production of acid phosphatase immediately after pH shift from below 3.0 to 4.0 whereas sheroplasts from cells grown in inorganic phosphate-rich medium showed a prolonged lag period (3 h). The enzyme formation on the pH shift was sensitive to cycloheximide. No significant differences could be detected in cellular growth or in incorporation of 3H-L-lysine or 14C-adenine between cells cultivated at pH 3.0 and 4.5. These results along with the fact that the expression of structural genes of repressible acid and alkaline phosphatases is controlled by a common genetic regulatory system, at least in part, indicate that the genetic regulatory system operates to express the structural genes even at low pH, though the expression of repressible acid phosphatase is interrupted. Coupled experiments of temperature and pH shifts with the temperature-sensitive mutants of the regulatory genes suggest that the acidic pH affects the function of the cytoplasmic products of those genes in the expression of the structural gene. Based on these observations, a revised model involving the simultaneous functioning of the regulatory factors was suggested for the genetic regulation of repressible acid phosphatase synthesis.

Acid Phosphatase↗
PubMed1987

Prospective comparison between serum monoclonal prostate specific antigen and acid phosphatase measurements in metastatic prostatic cancer.

Prostate specific antigen, prostatic acid phosphatase antigen and acid phosphatase activity were measured on 175 serum samples serially collected from 80 patients with metastatic stage D adenocarcinoma of the prostate. Prostate specific antigen and prostatic acid phosphatase antigen concentrations were measured with a monoclonal radioimmunometric assay, and acid phosphatase activity was measured enzymatically. The over-all frequency of abnormal levels of prostate specific antigen (76 per cent) was significantly greater than abnormal prostatic acid phosphatase antigen (60 per cent) and acid phosphatase activity (49 per cent) results (p less than 0.001). These differences were greater among the subset of patients in clinical remission. Levels greater than 10 times normal were observed in 68 per cent of prostate specific antigen, 43 per cent of prostatic acid phosphatase antigen and 31 per cent of acid phosphatase activity measurements (p less than 0.001). Three or more serial prostate specific antigen measurements in 17 patients demonstrated excellent correlation with independently assessed clinical disease activity. These results suggest that prostate specific antigen is a more sensitive and potentially more useful tumor marker than acid phosphatase measurements in patients with metastatic prostatic carcinoma.

Acid Phosphatase↗
PubMedDate not supplied

[Alkaline and acid phosphatase activity in the dynamics of ectopic osteogenesis].

Activities of marker enzymes of osteoblasts (alkaline phosphatase), osteoclasts (tartrate-resistant isoform of acid phosphatase), and macrophages (tartrate-sensitive isoform of acid phosphatase) in bone tissue forming after osteoinduction on the basis of demineralized bone matrix were under study. Early (1 week) stages of osteosynthesis were characterized by low activity of alkaline phosphatase, acid phosphatase being represented by the tartrate-sensitive isoform. Two-three weeks later alkaline phosphatase activity grew and the tartrate-resistant isoform of acid phosphatase appeared. By the fourth-sixth weeks of osteogenesis alkaline phosphatase activity stabilized at a certain level and acid phosphatase activity still grew at the expense of the tartrate-resistant isoform. Conformity of the enzymologic data to changes in cellular populations in ectopic osteogenesis is discussed.

Acid Phosphatase↗
PubMed1980

[Determination of acid phosphatase in prostatic carcinoma].

Serum acid phosphatase activity is the most commonly measured biochemical marker for diagnosing prostatic cancer and monitoring responses of such patients to therapy. Increased total serum acid phosphatase activity has been detected in the serum of up to 75% of patients with advanced disease (Stage D) which has metastasized to the bone, whereas in early stages (Stage A and B) as few as 10% may have increased total serum acid enzyme phosphatase values that can be detected by conventional biochemical assays. Serum acid phosphatase is believed to be comprised of specific molecular variants (isoenzymes) from sources throughout the body. Unfortunately, biochemical tests may lack specificity and sensitivity for the prostatic acid phosphatase, which is, thought to enter the serum in early stages of prostatic cancer. This situation prompted the development of immunologic assays for the determination prostatic acid phosphatase (radioimmunoassays, enzyme-immunoassays) which, it is hoped, combine the specificity achieved with immunologic reagents and techniques with the sensitivity made available through the use of radioisotopes or spectrophotometers.

Acid Phosphatase↗
PubMed2005

Differential expression of monomeric and proteolytically processed forms of tartrate-resistant acid phosphatase in rat tissues.

Purple acid phosphatase (PAP), also known as tartrate-resistant acid phosphatase (TRAP), uteroferrin or type 5 acid phosphatase (Acp5) is synthesized as an N-glycosylated monomeric latent precursor, which can be processed by limited proteolysis to a disulfide-linked two-subunit form with increased enzyme activity. In this study, we disclosed that the proteolytically processed two-subunit form constitutes the major PAP/TRAP variant in monocytic cells in spleen, thymus, liver and colon. In addition significant expression of the monomeric PAP/TRAP, indicating a non-enzymatic function, was detected in epithelial cells of colon, lung and kidney. Interestingly, proteolytic processing alone did not activate the enzyme but rendered the enzyme more susceptible to activation by reductants. Thus, beside limited proteolysis, the subcellular redox state could also be a determinant of enzyme action in vivo. The co-localization of PAP/TRAP and the cysteine protease cathepsin L could suggest a role for cathepsin L in the in vivo proteolytic processing of PAP/TRAP in monocytic cells.

Acid Phosphatase↗
PubMed2000

Biology of tartrate-resistant acid phosphatase.

Tartrate-resistant acid phosphatase (TRAP) is a member of the ubiquitously expressed enzyme family of the acid phosphatases. Nearly 30 years ago, TRAP became known to hematologists as cytochemical marker enzyme of hairy cell leukemia. Physiologically, TRAP is primarily a cytochemical marker of macrophages, osteoclasts and dendritic cells. TRAP is localized intracellularly in the lysosomal compartment. Recent data suggest also secretion of TRAP by some cell types, in particular by osteoclasts. Human, mouse and rat TRAP are biochemically well characterized. While the complete genomic sequence of TRAP has been elucidated, only limited information on the genetic details of the gene and its regulation is available. It appears that the intracellular iron content is involved in the regulation of the enzyme. The physiological substrates for this enzyme have not been identified yet and consequently the functional role of TRAP remains completely unknown, though some hypotheses have been forwarded, e.g. involvement in bone resorption and iron homeostasis (transport, metabolism). Taken together, research on the biology of TRAP has been intensive and has led to considerable progress on a number of fronts, including the cloning of the gene. Further studies are, however, still required to determine the role of TRAP in vivo.

Acid Phosphatase↗
PubMed1976

Saliva acid phosphatases: genetic studies.

Acid phosphatases from human saliva have been demonstrated by the zymogram technique. Six phenotypes were found. Family and population studies suggested that the phenotypes are the product of two loci, Sap-A with three alleles A, A' and O, and Sap-B with two alleles B and O.

Acid Phosphatase↗