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PubMed1992

The value of serum enzymatic acid phosphatase in the staging of localized prostate cancer.

With the development of reliable assays for the measurement of prostate specific antigen (PSA), the use of serum enzymatic acid phosphatase in the staging of disease before radical prostatectomy has been called into question. We evaluated 460 consecutive men who were referred to our institution as candidates for radical prostatectomy. Staging evaluation included digital rectal examination, serum measurements of enzymatic acid phosphatase and PSA, bone scans and, in patients in whom advanced clinical stage was anticipated, computerized tomography, magnetic resonance imaging or transrectal ultrasonography. Of the 460 men 21 (4.6%) had elevations of serum enzymatic acid phosphatase. All 19 men with elevations who were fully evaluated proved to have either positive bone scans, extraprostatic extension of disease, PSA greater than 100 ng./ml., positive lymph nodes or positive seminal vesicles. However, in 17 of the 21 men (81%) with elevated serum enzymatic acid phosphatase advanced disease was detected by either abnormal digital rectal examination or PSA alone. Thus, serum enzymatic acid phosphatase provided unique information in only 4 of the entire study population (0.9%). Recognizing this low yield of unique information, we believe that measurements of serum enzymatic acid phosphatase are no longer mandatory before radical prostatectomy but may provide important confirmatory information in patients in whom advanced disease is suspected.

Acid Phosphatase↗
PubMed1986

Morphometric and cytochemical analysis of lysosomes in rat Peyer's patch follicle epithelium: their reduction in volume fraction and acid phosphatase content in M cells compared to adjacent enterocytes.

M cells are specialized epithelial cells over lymphoid follicles in Peyer's patches which take up viruses, bacteria, and antigenic macromolecules from the intestinal lumen. Unlike ordinary enterocytes which sequester pinocytosed material in lysosomes, M cells transport such material across the epithelium to antigen-processing areas in lymphoid follicle domes, suggesting a difference in lysosomal activity or a different route for movement of endocytic vesicles. Ileal Peyer's patches in rats were examined by electron microscopy to identify lysosomes by acid phosphatase activity. Acid phosphatase was found in dense bodies in enterocytes but not in M cells. Stereological analysis showed the volume fraction occupied by dense bodies in M cells to be 16 times less than in enterocytes (P less than .0005), even though the volume fractions of cytoplasm occupied by mitochondria in M cells and enterocytes were not significantly different. The small volume fraction of dense bodies and the absence of acid phosphatase activity in M cells thus correlate with absence of lysosomal degradation of luminal microorganisms during transport into lymphoid follicles by M cells and may provide not only a complete array of microbial antigens for initiation of immune responses, but also a route through the mucosal barrier for microorganisms which can evade local containment mechanisms.

Acid Phosphatase↗
PubMed1990

Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure.

Tartrate-resistant acid phosphatase type-5 was purified to apparent homogeneity from human osteoclastomas by sequential chromatography on CM-Sepharose, Phenyl-Sepharose, concanavalin A-Sepharose, FPLC Superose-12, and FPLC Mono-S. The purification over the original tissue extract was 1167-fold, with a yield of 16%. An identity in the N-terminal amino acid sequence and Mr was found between this enzyme and two type-5 tartrate-resistant acid phosphatases isolated from hairy cell leukemia spleen. However, they appeared to be different as assessed by amino acid composition. In contrast to a previous report, no evidence was found for two subunits of the tartrate-resistant acid phosphatase.

Acid Phosphatase↗
PubMed1974

Characterization of a dominant, constitutive mutation, PHOO, for the repressible acid phosphatase synthesis in Saccharomyces cerevisiae.

An apparent operator-constitutive mutation was discovered in the repressible acid phosphatase system in Saccharomyces cerevisiae. The site of mutation, designated PHOO, was found to be closely linked to the phoD locus. The mutant allele, PHOO, was semidominant over the wild-type allele and effective for the expression of the phoD gene in cis position. The phoD mutation gave rise to a defective phenotype for the formation of the repressible acid phosphatase. On the other hand, neither the repressible acid phosphatase activity in the cell-free extracts prepared from cells of the temperature-sensitive phoD mutant grown at 25 C, nor that of the revertants from the phoD mutants, could be distinguished from that of the wild-type strain with respect to thermolability and K(m) value for p-nitrophenylphosphate. These results strongly suggest that the phoD gene is not a structural gene, but a regulatory gene exerting positive control for the formation of repressible acid phosphatase. Close similarity between the apparent role of the phoO-PHOD gene cluster and that of the c-GAL4 gene cluster in the galactose system of S. cerevisiae could be inferred.

Acid Phosphatase↗
PubMed1993

Uteroferrin and intracellular tartrate-resistant acid phosphatases are the products of the same gene.

Uteroferrin (Uf) is a purple acid phosphatase with a bi-iron center. It is the major secretory product of the porcine uterus under the influence of progesterone and supplies iron to the developing fetuses during pregnancy. Tartrate-resistant acid phosphatases (TRAP) are clearly similar to Uf in many of their properties but are generally located intracellularly in lysosomes. To determine whether Uf and intracellular TRAP are distinct gene products, cDNA for the TRAP from pig spleen were compared with Uf cDNA. Although no full-length cDNA for the former were isolated, a TRAP cDNA of 1.1 kilobases was identical in nucleotide sequence to a Uf cDNA (1.42 kilobases) in the region of overlap, which included the entire 3'-end of the transcript and most of the open reading frame. TRAP purified from porcine spleen also had an NH2-terminal amino acid sequence that corresponded to that of Uf purified from uterine secretions and was also similar in sequence to intracellular TRAP isolated from tissues of other species, including ones from human osteoclastomas and spleen. Finally, Southern hybridization analysis with two probes specific for exons 1 and 2 of the Uf gene strongly suggested the presence of only a single gene for acid phosphatases of this class in the pig. A similar analysis performed on human DNA with an exon-specific probe for human TRAP was also consistent with a single gene. It is concluded that the difference in trafficking between a secreted TRAP, such as Uf, and TRAP located in lysosomes is not the result of distinctive primary sequence of the polypeptides and that the variability within species ascribed to such enzymes is most likely the result of minor posttranslational changes.

Acid Phosphatase↗
PubMed1974

The development of ribonuclease and acid phosphatase during germination of Pisum arvense.

1. Development of ribonuclease activity in the cotyledons of germinating peas is biphasic, the time of appearance of the two phases depending on the conditions of growth. 2. Acid phosphatase exhibits a single phase of development. 3. Cycloheximide inhibits development of ribonuclease activity in phase II but not in phase I. 4. (14)C-labelled amino acids are not incorporated into ribonuclease isolated during phase I. 5. The buoyant density of ribonuclease isolated during phase I is not affected by imbibition of the seed in 80% deuterium oxide. 6. Acid phosphatase was isolated from the supernatant fraction of the cotyledons of germinating peas and partially purified. 7. Development of acid phosphatase activity during germination is inhibited by treatment of the seed with cycloheximide or actinomycin D. 8. Partial purification of acid phosphatase from peas germinated in the presence of (14)C-labelled amino acids suggests that the enzyme is radioactively labelled. 9. Germination of peas in the presence of 80% deuterium oxide results in an increase in the buoyant density of acid phosphatase. 10. The results suggest that increase in ribonuclease activity during the first 4 days of germination does not result from synthesis of protein de novo, but that the corresponding increase in acid phosphatase activity does result from synthesis de novo.

Acid Phosphatase↗
PubMed1983

Chloramphenicol stimulates acid phosphatase activity in germinating cotton (Gossypium hirsutum) embryos.

Low dosages of chloramphenicol (25-50 micrograms/ml) brought about a 2-4-fold stimulation of acid phosphatase activity in 48 h-germinated cotton (Gossypium hirsutum) embryos. However, at high concentrations of chloramphenicol (100-1000 micrograms/ml), there was a progressive decline in enzyme activity. The stimulatory effect of the drug on acid phosphatase activity was relatively specific, since no significant stimulation of activities of proteinase, deoxyribonuclease, ribonuclease, o-diphenolase and peroxidase was observed in germinating cotton embryos. Chloramphenicol, however, did promote the activities of isocitric lyase and alkaline phosphatase. Sephadex G-200 chromatography of the enzyme fraction revealed high (230 000)- and low (106 000)-molecular-weight multiple forms of acid phosphatase in the chloramphenicol-treated embryos, in contrast with a single molecular form (mol.wt. 106 000) in the untreated embryos. Thus the treatment of cotton embryos with chloramphenicol induced both a qualitative and a quantitative change in the acid phosphatase activity. Chloramphenicol-stimulated acid phosphatase activity was strongly inhibited when Pi was included in the germination medium. However, the control embryos showed less pronounced inhibition of enzyme activity in presence of Pi ions.

Acid Phosphatase↗
PubMed1978

Electron microscopy of peroxidase and acid phosphatase in leprous and uninfected armadillo macrophages: a macrophage subpopulation contains peroxisomes and lacks bacilli.

Lepromatous tissue from armadillos inoculated 24--36 months earlier with Mycobacterium leprae was obtained for electron microscopic studies. Cytochemically stained lepromas revealed a subpopulation of macrophages containing peroxisomes. These peroxidase reactive macrophages were not infected with bacilli. Acid phosphatase was present in macrophages and many of these were infected with bacilli and contained vacuoles and lipid globules. Within the membrane-bound vacuoles, acid phosphatase surrounded bacilli. However, the reaction product ended abruptly at a 15--40 millimicron thick zone of low electron density surrounding intact bacilli. Acid phosphatase was more intensely reactive and localized less precisely in heavily infected and vacuolated macrophages than in lightly and non-infected cells. The effectiveness of this bacillary barrier and the numerous infected macrophages with substantial acid phosphatase argue against the ability of acid phosphatase to protect host cells from leprosy bacilli. Evidence suggests a protective action of peroxidase or the rapid turnover of macrophages within lepromas. Granular and membranous debris were commonly seen within vacuoles of infected macrophages. A portion of the debris was ultrastructurally similar to bacillary matrix and was nonreactive for peroxidase and acid phosphatase. Following homogenization and centrifugation, similar materials banded with bacilli above 60% sucrose. Another portion of the debris was ultrastructurally similar to host lysosomal matrix and was reactive for acid phosphatase. Results support the concept of dual host and parasitic origins of the debris found in phagolysosomes of infected macrophages. Transparent, oval Epon defects remained eccentric to the majority of intact bacilli in centrifuged fractions. Apparently, an intrinsic property of leprosy produced these Epon defects.

Acid Phosphatase↗
PubMed1984

The role of serum prostatic acid phosphatase as a tumor marker in men with advanced adenocarcinoma of the prostate.

Serial serum prostatic acid phosphatase levels were obtained every 4 hours during a 48-hour interval from 10 men with stage D adenocarcinoma of the prostate. No therapeutic or diagnostic manipulations occurred during sample procurement, so that the amount of fluctuation of serum prostatic acid phosphatase levels that can be expected in these patients could be determined. The coefficient of variation for each man ranged from 16.67 to 43.68 per cent, which was significantly higher than the expected 8 per cent coefficient of variation determined with a control sample. The maximum percentage variations above and below the mean were 79 and 50 per cent, respectively. The average percentage variation in all patients was within 50 per cent greater than and 50 per cent less than the mean value of prostatic acid phosphatase. Thus, the usefulness of serum acid phosphatase by radioimmunoassay as a clinical tumor marker is limited by the number of serial assays needed to establish a mean. Based on these findings, certain guidelines are suggested.

Acid Phosphatase↗
PubMed1976

Preparation of specific antisera to Drosophila acid phosphatase without rigorous protein purification.

Extracts from an acid phosphatase CRM- null mutant of Drosophila melanogaster were used to eliminate contaminating antibodies in a nonspecific preparation of anti-acid phosphatase serum. This method of producing specific antisera makes unnecessary the rigorous purification of an antigen prior to immunization attempts in those cases where CRM- null mutants of the antigen are available. Antisera so prepared could be used for a wide variety of purposes.

Acid Phosphatase↗
PubMed1989

Cloning, sequencing, and characterization of the principal acid phosphatase, the phoC+ product, from Zymomonas mobilis.

The Zymomonas mobilis gene encoding acid phosphatase, phoC, has been cloned and sequenced. The gene spans 792 base pairs and encodes an Mr 28,988 polypeptide. This protein was identified as the principal acid phosphatase activity in Z. mobilis by using zymograms and was more active with magnesium ions than with zinc ions. Its promoter region was similar to the -35 "pho box" region of the Escherichia coli pho genes as well as the regulatory sequences for Saccharomyces cerevisiae acid phosphatase (PHO5). A comparison of the gene structure of phoC with that of highly expressed Z. mobilis genes revealed that promoters for all genes were similar in degree of conservation of spacing and identity with the proposed Z. mobilis consensus sequence in the -10 region. The phoC gene contained a 5' transcribed terminus which was AT rich, a weak ribosome-binding site, and less biased codon usage than the highly expressed Z. mobilis genes.

Acid Phosphatase↗
PubMedDate not supplied

Characterization of alkaline and acid phosphatases from skeletal muscles of young and old rats.

Alkaline phosphatase (ALP) and acid phosphatase (ACP) specific activities were measured in gastrocnemius muscles of female Wistar rats ranging in age from 2 to 30 months. ALP activity reached a peak at 12 months, with a subsequent slow decline with age. ACP activity increased sharply up to 12 months of age, followed by a slower elevation up to the age of 30 months. Using histochemical staining techniques and electron microscopy, the presence of ALP was demonstrated in the sarcolemma of gastrocnemius muscles, as well as in some capillaries around muscle fibers. ALP and ACP were isolated further from muscles of young (12 months) and old (30 months) animals by applying ion-exchange chromatography and separation on a Sephadex G-200 column. The purity of ALP was shown on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). From a calibrated Sephadex G-200 column and SDS-PAGE, the molecular mass of ALP was determined as 116 kilodaltons (kDa), a dimer of two 56-kDa monomers. The ACP major peak of the Sephadex G-200 column revealed a molecular mass of 40 kDa. No differences in molecular mass or in amino acid analysis were detected between ALP(s) from young and old animals, indicating that most probably the decline of activity with age is due to some post-translational events, as has been shown in the past for many other enzymes and proteins.

Journal Article↗
PubMedDate not supplied

Action of norepinephrine on free and cryptic acid phosphatase activity in newborn rats.

The distribution of free and cryptic acid phosphatase activity in brain slices and homogenates of newborn rats was investigates with 1-5% Triton X-100. A maximum level of enzyme activity (which implies a loss of latency of lysosomal acid phosphatase was found with 2.5% Triton X-100. The enzyme activity was constantly enhanced 2.5-3 fold by homogenization of brain with 2.5% Triton X-100. Preincubation of brain slices with 0.1 mM norepinephrine for 1 hour increases by 20% the activity of enzyme. Preincubation of supernatant, after homogenization, decreases by 6-8% the total activity and by 8% the activity of samples treated with 2.5% Triton X-100. This latter effect seems to be more efficient on the cryptic (lysosomal) acid phosphatase as suggested by the isoenzymatic pattern. Addition of cyclic AMP to the samples (after homogenization) has no effect on the enzymatic activity.

Acid Phosphatase↗
PubMed1982

Comparison of prostatic and nonprostatic acid phosphatase.

Electrophoresis and ion-exchange column chromatography were used to separate the wide varieties of acid phosphatases with different biological and clinical significance. Band 0 was very strong in ascitic cells with many autophagic vacuoles, indicating a role in autophagic function. Band 1 was a membrane-bound acid phosphatase, seen mainly in the microsomal fraction. Band 3 was the major lysosomal acid phosphatase of all nonprostatic tissues. Bands 2 and 4 were antigenically identical to each other, and were observed in unusually high amounts in the prostate. The different electrophoretic mobility between bands 2 and 4 was due to their carbohydrate content. Band 5 was a characteristic enzyme of the osteoclast. The tartrate-sensitive enzymes included bands 0 through 4. Only band 5 was tartrate resistant. The tartrate-resistant acid phosphatase of erythrocytes was not detected by the electrophoresis method. Clinical applications were seen for both bands 2 and 5. Band 2 was a secretory enzyme, normally secreted into the seminal plasma. Band 2 was absorbed into the blood circulation in some prostatic cancer patients. A small amount of bands 2 and 4 was observed in nonprostatic tissues. The diagnostic value of band 2 resulted from its extremely high concentration in the prostate. Band 5 was not observed in the normal prostate. A high concentration of band 5 was observed in hairy cells, Gaucher cells, and osteoclasts. The serum level of band 5b was an indicator of osteoclastic activity in the bone. Elevation of band 5b in serum was observed in normal children during physiological bone growth, in Gaucher's disease, and in malignancies metastasized to bone.

Acid Phosphatase↗
PubMed2001

The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity.

Recombinant human purple acid phosphatase (recHPAP) provides a convenient experimental system for assessing the relationship between molecular structure and enzymatic activity in mammalian purple acid phosphatases (PAPs). recHPAP is a monomeric protein with properties similar to those of uteroferrin (Uf) and other PAPs isolated as single polypeptide chains, but its properties differ significantly from those of bovine spleen PAP (BSPAP) and other PAPs isolated as proteolytically "clipped" forms. Incubation of recHPAP with trypsin results in proteolytic cleavage in an exposed region near the active site. The product is a tightly associated two-subunit protein whose collective spectroscopic and kinetics properties resemble those of BSPAP. These results demonstrate that the differences in spectroscopic and kinetics properties previously reported for mammalian PAPs are the result of proteolytic cleavage. Mass spectrometry shows that a three-residue segment, D-V-K, within the loop region is excised by trypsin. This finding suggests that important interactions between residues in the excised loop and one or more of the groups that participate in catalysis are lost or altered upon proteolytic cleavage. Analysis of available structural data indicates that the most important such interaction is that between Asp 146 in the exposed loop and active-site residues Asn 91 and His 92. Loss of this interaction should result in both an increase in the Lewis acidity of the Fe(II) ion and an increase in the nucleophilicity of the Fe(III)-bound hydroxide ion. Proteolytic cleavage thus constitutes a potential physiological mechanism for regulating the activity of PAP in vivo.

Acid Phosphatase↗
PubMed1996

Gene cloning and cellular localization of a membrane-bound acid phosphatase of Leishmania mexicana.

In a previous publication, we described the purification of a membrane-bound acid phosphatase of Leishmania mexicana as a heterogeneously N-glycosylated protein of an apparent molecular mass of 70000-72000 expressed in both the promastigote and the amastigote stage of the parasite [19]. Screening of a genomic DNA library of L. mexicana with degenerate oligonucleotides designed according to the NH2-terminus of the protein led to the cloning of the lmmbap gene, which is present in one copy per haploid genome. The open reading frame predicts a protein of 516 amino acids composed of a signal sequence, a large hydrophilic region, a trans-membrane alpha-helix and a short cytoplasmic tail. The sequence of the hydrophilic region is homologous to acid phosphatases from other organisms. While in wild-type promastigotes, the acid phosphatase is located in the endosomal/lysosomal compartment between the flagellar pocket and the nucleus, overexpression leads to its abundant exposure on the cell surface. In cells transfected with a construct lacking the region corresponding to the trans-membrane and the cytoplasmic parts, the resulting altered acid phosphatase is efficiently secreted into the culture medium. The potential of this system for studies on membrane trafficking in kinetoplastid organisms is discussed.

Acid Phosphatase↗
PubMed1988

Clinical behavior of prostatic specific antigen and prostatic acid phosphatase: a comparative study.

We assayed prostatic specific antigen and prostatic acid phosphatase serum levels in 1,383 patients using a double antibody radioimmunoassay (RIA) 125I. Establishing the upper normal limit in 10 ng/ml for prostatic specific antigen and 2.5 ng/ml for prostatic acid phosphatase, the false positive results were only 1.9 and 5.1% in men with nonprostatic benign or malignant pathology and 0 and 2.2% in women, respectively. We detected false positive levels in 3.5 and 4.7% of the patients with noncomplicated benign prostatic hypertrophy, 64.8 and 19.2% in complicated benign prostatic hypertrophy, 24 and 16% in acute prostatitis and 3.3% in chronic prostatitis for both tumoral markers. The sensibility in patients with prostate cancer was 87.2 and 64.1%, respectively, and there was better correlation with prostatic specific antigen than prostatic acid phosphatase levels on tumoral spread and histologic grading. Finally, the clinical efficacy was higher with prostatic specific antigen and it did not increase with the quantification of both tumoral markers.

Acid Phosphatase↗
PubMed2000

Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities.

The appA gene that was previously shown to code for an acid phosphatase instead codes for a bifunctional enzyme exhibiting both acid phosphatase and phytase activities. The purified enzyme with a molecular mass of 44,708 Da was further separated by chromatofocusing into two isoforms of identical size with isoelectric points of 6.5 and 6.3. The isoforms had identical pH optima of 4.5 and were stable at pH values from 2 to 10. The temperature optimum for both phytase isoforms was 60 degrees C. When heated at different pH values the enzyme showed the greatest thermal resistance at pH 3. The pH 6.5 isoform exhibited K(m) and Vmax values of 0.79 mM and 3165 U.mg-1 of protein for phytase activity and 5.5 mM and 712 U.mg-1 of protein for acid phosphatase, respectively. The pH 6.3 isoform exhibited slightly lower K(m) and Vmax values. The enzyme exhibited similar properties to the phytase purified by Greiner et al. (1993), except the specific activity of the enzyme was at least 3.5-fold less than that previously reported, and the N-terminal amino acid sequence was different. The Bradford assay, which was used by Greiner et al. (1993) for determination of enzyme concentration was, in our hands, underestimating protein concentration by a factor of 14. Phytase production using the T7 polymerase expression system was enhanced by selection of a mutant able to grow in a chemically defined medium with lactose as the carbon source and inducer. Using this strain in fed-batch fermentation, phytase production was increased to over 600 U.mL-1. The properties of the phytase including the low pH optimum, protease resistance, and high activity, demonstrates that the enzyme is a good candidate for industrial production as a feed enzyme.

6-Phytase↗