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PubMed1999

Isolation, cloning, and expression of an acid phosphatase containing phosphotyrosyl phosphatase activity from Prevotella intermedia.

A novel acid phosphatase containing phosphotyrosyl phosphatase (PTPase) activity, designated PiACP, from Prevotella intermedia ATCC 25611, an anaerobe implicated in progressive periodontal disease, has been purified and characterized. PiACP, a monomer with an apparent molecular mass of 30 kDa, did not require divalent metal cations for activity and was sensitive to orthovanadate but highly resistant to okadaic acid. The enzyme exhibited substantial activity against tyrosine phosphate-containing peptides derived from the epidermal growth factor receptor. On the basis of N-terminal and internal amino acid sequences of purified PiACP, the gene coding for PiACP was isolated and sequenced. The PiACP gene consisted of 792 bp and coded for a basic protein with an M(r) of 29,164. The deduced amino acid sequence exhibited striking similarity (25 to 64%) to those of members of class A bacterial acid phosphatases, including PhoC of Morganella morganii, and involved a conserved phosphatase sequence motif that is shared among several lipid phosphatases and the mammalian glucose-6-phosphatases. The highly conservative motif HCXAGXXR in the active domain of PTPase was not found in PiACP. Mutagenesis of recombinant PiACP showed that His-170 and His-209 were essential for activity. Thus, the class A bacterial acid phosphatases including PiACP may function as atypical PTPases, the biological functions of which remain to be determined.

Acid Phosphatase↗
PubMed1975

Biochemical and cytochemical studies of digestive-absorptive functions of esophagus, cecum, and tequment in Schistosoma mansioni: acid phosphatase and tracer studies.

Acid phosphatase activity was examined, both cytochemically and biochemically, using beta-glycerophosphate (betaGP) and p-nitrophenyl phosphate (NPP) as substrates. The hydrolysis of these substrates differs in pH optimum and sensitivity to some inhibitors. A latent component of the enzyme activity could be demonstrated with betaGP but not with NPP as substrate. These differences suggest the presence of multiple enzymes operative at acid pH in S. mansoni. Cytochemical localization of the sites of hydrolysis of these substrates shows the major activity of the digestive system to be in the posterior portion of the esophagus and in the cecum. The reaction product in the posterior esophagus is found in small dumbbell-shaped vesicles and in the basal infoldings, while in the cecum it occurs on the apical plasmalemma, basal infoldings, and in pleiomorphic vesicles. The electron-dense tracers, ferritin, peroxidase, Thorotrast, and latex beads were all ingested but none was phagocytized. Tracer material was found in some "apparent" vesicles with subsequently were shown by the lanthanum staining technique to be in communication with the extracellular space.

4-Nitrophenylphosphatase↗
PubMed1985

Reactive thiol groups in rat liver acid phosphatase.

Dimeric rat liver acid phosphatase P1 of Mr 92,000 is inactivated by p-chloromercuribenzoate and fluorescein mercuriacetate (FMA). The enzyme is protected against the mercurials by the substrate analogue Pi. The reaction with FMA is accompanied by changes in absorbance at 495 nm and in fluorescence emission at 520 nm that are characteristic of reaction of this compound with thiol groups. Titration of P1 with FMA monitored by spectrophotometry or by fluorimetry indicated that equivalence is reached at an FMA/P1 ratio of 3. Since FMA can act as a bifunctional reagent, it is likely that P1 contains either 3 or 6 reactive thiol groups per molecule. Analysis of FMA inactivation/modification data by a statistical method suggests that of 6 reactive thiol groups, 2 are essential so that there are probably 3 thiol groups per subunit, one of which is located at the active site. If the total thiol number is 3, analysis suggests 1 essential thiol per subunit.

Acid Phosphatase↗
PubMed1991

Cloning, sequence, and developmental expression of a type 5, tartrate-resistant, acid phosphatase of rat bone.

Tartrate-resistant acid phosphatase (TRAP) is a characteristic constituent of osteoclasts and some mononuclear preosteoclasts and, therefore, used as a histochemical and biochemical marker for osteoclasts and bone resorption. We now report the isolation of a 1397-base pair (bp) full-length TRAP/tartrate-resistant acid ATPase (TrATPase) cDNA clone from a neonatal rat calvaria lambda gt11 cDNA library. The cDNA clone consists of a 92-bp untranslated 5'-flank, an open reading frame of 981 bp and a 324-bp untranslated 3'-poly(A)-containing region. The deduced protein sequence of 327 amino acids contains a putative cleavable signal sequence of 21 amino acids. The mature polypeptide of 306 amino acids has a calculated Mr of 34,350 Da and a pI of 9.18, and it contains two potential N-glycosylation sites and the lysosomal targeting sequence DKRFQ. At the protein level, the sequence displays 89-94% homology to TRAP enzymes from human placenta, beef spleen, and uteroferrin and identity to the N terminus of purified rat bone TRAP/TrATPase. An N-terminal amino acid segment is strikingly homologous to the corresponding region in lysosomal and prostatic acid phosphatases. The cDNA recognized a 1.5-kilobase mRNA in long bones and calvaria, and in vitro translation using, as template, mRNA transcribed from the full-length insert yielded an immunoprecipitated product of 34 kDa. In neonatal rats, TRAP/TrATPase mRNA was highly expressed in skeletal tissues, with much lower (less than 10%) levels detected in spleen, thymus, liver, skin, brain, kidney, brain, lung, and heart. In situ hybridization demonstrated specific labeling of osteoclasts at endostal surfaces and bone trabeculae of long bones. Thus, despite the apparent similarity of this osteoclastic TRAP/TrATPase with type 5, tartrate-resistant and purple, acid phosphatases expressed in other mammalian tissues, this gene appears to be preferentially expressed at skeletal sites.

Acid Phosphatase↗
PubMed1990

Biosynthesis, processing, and intracellular transport of lysosomal acid phosphatase in rat hepatocytes.

The biosynthesis, processing, and intracellular transport of lysosomal acid phosphatase was studied using an in vitro cell-free translation system, pulse-chase experiments with primary cultured rat hepatocytes and subcellular fractionation techniques of rat liver after pulse-labeling with [35S]methionine in vivo. The single polypeptide of 45 kDa translated in the cell-free system from membrane-bound polysomal RNAs was converted to the 64 kDa form when the translation was carried out in the presence of microsomal vesicles. Pulse-chase experiments using cultured rat hepatocytes showed that acid phosphatase is initially synthesized as an endo-beta-N-acetylglucosaminidase H (Endo H)-sensitive form of 64 kDa, and processed via an Endo H-sensitive intermediate form of 62 kDa to an Endo H-resistant form with a 67 kDa mass. Phase separation with Triton X-114 showed that both the 64 and 67 kDa forms have hydrophobic properties. Treatment of the cells with chloroquine or tunicamycin, drugs which enhance the secretion of lysosomal hydrolases, had no effect on the normal transport of acid phosphatase to lysosomes. Acid phosphatase did not contain the phosphorylated high mannose type of oligosaccharide chains observed in cathepsin D. Subcellular fractionation experiments in conjunction with pulse-labeling in vivo showed that the acid phosphatase of the 67 kDa form was present in the Golgi heavy fraction (GF3) and the Golgi light fraction (GF1+2) enriched in cis and trans Golgi elements, respectively, at 30 min after the administration of [35S]methionine. Simultaneously, this polypeptide was also found in the lysosomal membrane fraction, thereby indicating that acid phosphatase is delivered to lysosomes in a membrane-bound form, immediately after reaching the trans-Golgi region.(ABSTRACT TRUNCATED AT 250 WORDS)

Acid Phosphatase↗
PubMed1978

Biochemical and immunologic techniques for acid phosphatase measurement in the diagnosis of prostate cancer.

A counter immunoelectrophoresis procedure for the measurement of acid phosphatase is described. Acid phosphatase was purified from human prostate. A monospecific antiserum to the purified enzyme was produced in rabbits. With the specific antiserum and a sensitive chemical staining technique, a counter immunoelectrophoresis assay was developed for detection of serum prostate acid phosphatase. The isoenzymes of serum prostate acid phosphatase were also studied by an isoelectric focusing technique.

Acid Phosphatase↗
PubMed1976

Acid phosphatase localization in the fungus Whetzelinia sclerotiorum.

Acid phosphatase was localized by light and electron microscopy in chains of vacuoles in hyphal tip cells of Whetzelinia sclerotiorum. The enzyme was present in these vacuoles whether or not conditions favored extracellular acid phosphatase secretion. Apical vesicles, microbodies, Woronin bodies, and lipid bodies did not contain acid phosphatase. The implications regarding terminology of organelles in filamentous fungi are discussed with special reference to the fungal spherosome concept.

Acid Phosphatase↗
PubMed1983

Relationship of plasma tartrate resistant acid phosphatase to the bone isoenzyme of serum alkaline phosphatase in hyperparathyroidism.

In 46 patients with primary hyperparathyroidism, in 21 non-dialysed patients with advanced renal failure, and in 52 patients on hemodialysis, a significant positive correlation was found between bone isoenzyme of serum alkaline phosphatase and plasma tartrate resistant acid phosphatase. In primary hyperparathyroidism, a significant positive correlation was found between the radiological degree of osteodystrophy and the biochemical parameters of bone remodelling. After removal of the parathyroid adenoma, only the tartrate-resistant acid phosphatase decreased to normal limits. Plasma tartrate resistant acid phosphatase was most significantly influenced by serum immunoreactive parathyroid hormone levels. In chronic renal failure, bone isoenzyme of serum alkaline phosphatase was most significantly influenced by serum immunoreactive parathyroid hormone levels, by hypocalcemia and by duration of hemodialysis. The results confirm that in hyperparathyroidism the extent of the whole-body rates of bone resorption and formation are approximately equal. The biochemical parameters can be used for serial assessment of the course of the disease but are not specific for diagnosis.

Acid Phosphatase↗
PubMed1985

Serum haptoglobin appearance during neonatal period is associated with acid phosphatase (ACP1) phenotype.

Erythrocyte acid phosphatase (ACP1) is a polymorphic enzyme found in many tissues and acts in vivo as a flavin-mononucleotide phosphatase. We have recently observed a relation between this enzyme and length of gestation. The present study shows that the pattern of appearance of serum haptoglobin during the neonatal period is associated with ACP1 phenotype suggesting some important function of this polymorphic enzyme in human development.

Acid Phosphatase↗
PubMed1978

Problems of reliability in the phenotyping of erythrocyte acid phosphatase in bloodstains.

Erythrocyte acid phosphatase is a useful system for the crime laboratory for both fresh and degraded blood and bloodstains, provided the inherent problems of phenotyping this particular enzyme system are recognized. Because of the great number of variables affecting this enzyme system in vitro, phenotyping should not be attempted unless the complete history of origin and handling of the sample is known.

Acid Phosphatase↗
PubMed1975

Biosynthesis of acid phosphatase of baker's yeast. Characterization of a protoplast-bound fraction containing precursors of the exo-enzyme.

1. Yeast protoplasts, secreting acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum) EC 3.1.3.2) contain a small amount of firmly bound enzyme, even after lysis (Van Rijn, H.J.M., Boer, P. and Steyn-Parvé, E.P. (1972) Biochim. Biophys. Acta 268, 431-441). The major part (70%) of this protoplast-bound acid phosphatase can be solubilized by nonionic detergents, such as Triton X-100. 2. The kinetics of radioactive amino acid incorporation in the solubilized and in the secreted enzyme has been estimated by pulse-chase labelling of secreting protoplasts, followed by fractionation and counting radioactivity in the enzyme band in polyacrylamide gels after electrophoresis at pH 5.0. A precursor-product relationship between the Triton X-100-extractable fraction of the protoplast-bound acid phosphatase and the secreted enzyme is apparent. 3. The solubilized acid phosphatase is essentially indistinguishable from the secreted enzyme with regard to a number of enzymatic properties and its stability towards pH and temperature. Both enzymes also behave alike on polyacrylamide-gel electrophoresis, producing a single acid phosphatase band with glycoprotein character and comparable mobility. 4. A striking difference is seen in isopycnic equilibrium sedimentation in CsCl: the secreted acid phosphatase is homogeneous, with a buoyant density of p equals 1.47 g/cm3, while the Triton X-100-extractable part of the protoplast-bound acid phosphatase is heterogeneous; besides heavier material a major component with buoyant density of p equals 1.37 g/cm3 is always visible.

Acid Phosphatase↗
PubMed1990

A study of the acid phosphatase of Treponema denticola.

This study describes some of the properties of the acid phosphatase of the potential periodontopathogen Treponema denticola. The highest enzyme activity was found in 87 h old cells. Two optimum pHs for enzyme activity were detected, one at pH 4.8 and another at pH 6.2. Divalent cations did not influence the acid phosphatase of T. denticola. The anion F- added in the form of NaF and at a level greater than 20 micrograms/ml F- diminished the activity of the acid phosphatase of intact cells of T. denticola. The addition of 10 micrograms/ml F- as SnF2 induced a statistically significant reduction of acid phosphatase activity. The apparent Km for the acid phosphatase was 7.3 mM with p-nitrophenyl phosphate as substrate. Fluoride appeared to be a noncompetitive inhibitor of the enzyme with an apparent Ki of 0.3 mM. Acid phosphatase may be released partially in osmotic shock fluids. Also, 7-diazonium-1, 3-naphthalene disulfonate, which is incapable of penetrating the bacterial permeability barrier and is known to inactivate enzymes found in the bacterial periplasmic place, suppressed the activity of the acid phosphatase in intact cells of T. denticola.

Acid Phosphatase↗
PubMed1975

Comparative evaluation of serum acid phosphatase, urinary cholesterol, and androgens in diagnosis of prostatic cancer.

Serum acid phosphatase activity, urinary total cholesterol, and ratio of deoxy to oxy urinary 17-ketosteroids were measured in a group of 42 patients with prostatic carcinoma and in a group of 14 age-matched normal healthy individuals. Our purpose was to evaluate whether or not the simultaneous determinations of these tests would increase the rate of detection obtained by the single assay alone. The results of single assay revealed for the following detection rate: 67 per cent (28 of 42 patients) for serum acid phosphatase, 62 per cent for urinary total cholesterol, and 22 per cent for ratio of 17-ketosteroids. A significant increase of detection rate was observed when simultaneous determinations of two assays were performed; 86 per cent for serum acid phosphatase activity and total urinary cholesterol; 74 per cent for serum acid phosphatase and ratio of 17-ketosteroids; and 74 per cent for total urinary cholesterol and ratio of 17-ketosteroids. A detection rate of 88 per cent (37 of 42 patients) was obtained as all three assays were analyzed, though it was not significantly different from a ratio of 86 per cent for simultaneous assays of acid phosphatase and total cholesterol. It was concluded that simultaneous determinations of serum acid phosphatase activity, urinary total cholesterol, and androgens are of values in diagnosis for patients with prostatic neoplasia.

17-Ketosteroids↗
PubMed1981

Appearance of acid phosphatase in neonatal rat substantia gelatinosa.

The onset of acid phosphatase activity was observed in neonatal rat substantia gelatinosa using the Gomori method. Although acid phosphatase activity was not present at birth it appeared during the first day postnatally. By six to ten days postnatally enzyme activity appeared to reach its adult level. The activity was quantified using atomic absorption spectrophotometry which showed that acid phosphatase activity reached its adult level by 6 days postnatally. Acid phosphatase in the substantia gelatinosa is fluoride resistant from its first appearance.

Acid Phosphatase↗
PubMed2001

[Acid phosphatase, ACP (EC 3.1.3.2)].

Acid phosphatase (ACP) is a hydrolytic lysosomal enzyme secreted by a number of cells including blood cells as well as by the prostate, bones, liver and other tissues. Several isozymes of ACP have tissue specificity. The isozymes can be fractionated by electrophoresis into six bands. Prostatic ACP (bands 2-4) is frequently measured for the diagnosis of prostatic disease. Band 5, tartrate resistant ACP (TRACP) consists of two isoforms, bands 5a and 5b. TRACP 5b is considered to be a marker of the osteoclasts and 5a is found in Gaucher's cells, or in the leukocytes of patients with hairy cell leukemia.

Acid Phosphatase↗
PubMed1998

Genetic polymorphism of rabbit (Oryctolagus cuniculus) tissue acid phosphatases (ACP2 and ACP3).

Rabbit (Oryctolagus cuniculus) red cell and tissue acid phosphatases were studied by means of horizontal starch gel electrophoresis and isoelectric focusing followed by enzyme blotting. Red cell acid phosphatase 1 (ACP1) is monomorphic while tissue acid phosphatase 2 (ACP2) is polymorphic in a wild rabbit population, with two alleles: ACP2*1 (0.96) and ACP2*2 (0.04). A third locus homologous of human acid phosphatase 3 (ACP3) is characterized by the presence of three alleles (ACP3*1, ACP3*2 and ACP3*3). ACP3*1 is the most common allele and was detected in all populations, ACP3*2 was found in domestic breeds and in a wild population from Southern France, whereas ACP3*3 is typical of Portuguese wild rabbits. The geographical distribution of ACP3*2 and ACP3*3 is in agreement with the subspecific level of differentiation of the rabbit species in O. cuniculus cuniculus and O. c. algirus. The comparative study of the acid phosphatase activity in red cells of several mammalian species, including humans, suggests that ACP3 activity in erythrocytes exists only in rabbit.

Acid Phosphatase↗
PubMed1986

Monoclonal antibody specific to acid phosphatase isoenzyme 4.

Prostatic acid phosphatase isoenzyme 4 was purified by ion exchange column chromatography, followed by high pressure liquid chromatography. The highly purified enzyme was used to produce monoclonal antibody from immunized BALB/c mice. The antibody was specific to isoenzyme 4, with negligible affinity to isoenzyme 2. The specificity of the monoclonal antibody was evaluated by Western blot analysis and by inhibition of radioimmunoassay. Immunohistochemistry method using the antibody to isoenzyme 2 showed heavy staining on the cell surface in contrast to the even staining throughout the cytoplasm when monoclonal anti-isoenzyme 4 was used. These results reflect the secretory nature of isoenzyme 2 and the non-secretory nature of isoenzyme 4.

Acid Phosphatase↗
PubMed1996

Evolution of cell-surface acid phosphatase of Burkholderia pseudomallei.

Acid phosphatase active fractions were obtained from cell-free extract, outermembrane fraction and culture filtrate of Burkholderia pseudomallei by column chromatography with sepharose 6B and DEAE cellulose. The comparison of the elution patterns of protein, sugar and enzymatic activity among these three components suggested that the enzyme is a glycoprotein evolving from premature proteins through glycosylation and that the enzyme is translocated during glycosylation from the cytoplasm to the outer membrane and finally excreted into the environment. When tunicamycin, a glycosylation inhibitor, was added to the culture, the peaks of sugar and enzymatic activity were lowered concomitantly leaving the protein peak unchanged in the elution pattern of the culture filtrate. The affinity of the bacterial surface to antienzyme sera was demonstrated by immuno-fluorescence microscopy.

Acid Phosphatase↗