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PubMed2000

Tartrate-resistant acid phosphatase 5b: a novel serum marker of bone resorption.

Human serum contains two forms of tartrate-resistant acid phosphatase (TRAP), 5a and 5b. Of these, 5a contains sialic acid and 5b does not. We show here that antigenic properties and pH optimum of TRAP purified from human osteoclasts are identical to those of serum TRAP 5b and completely different from those of serum TRAP 5a, suggesting that 5b would be derived from osteoclasts and 5a from some other source. We developed a novel immunoassay specific for 5b using a monoclonal antibody O1A as capture antibody. O1A did not bind acid phosphatase derived from platelets and erythrocytes. Western analysis showed that O1A was specific for TRAP in both human bone and serum. We measured bound TRAP activity at pH 6.1, where 5b is highly active and 5a almost completely inactive. The immunoassay detected more than 90% of the initial TRAP 5b activity after 8-h incubation of serum samples at 25 degrees C and after 3 days incubation at 4 degrees C. Serum TRAP 5b activity decreased significantly after 6 months of hormone replacement therapy (HRT) of postmenopausal women compared with the change observed in postmenopausal women receiving placebo (p < 0.0001). Instead, no significant differences were observed between the changes in the placebo and HRT groups in total serum TRAP amount. These results show that serum TRAP 5b is a specific and sensitive marker for monitoring antiresorptive treatment. Instead, total serum TRAP cannot be used for that purpose. These findings may turn out to be a significant improvement in using serum TRAP as a resorption marker.

Acid Phosphatase↗

PubMed1978

Quantitative determination endogenous acid phosphatase activity in vaginal washings.

Vaginal washings obtained in 98 patients were analyzed for acid phosphatase activity. A history of recent sexual intercourse was also obtained. Acid phosphatase values of less than 50 IU (obtained by the alpha naphthol phosphate method) correlated with abstinence from sexual intercourse for more than 30 hours, whereas values greater than 50 IU correlated with sexual intercourse in a period up to and including 30 hours (P less than 0.05). The presence or absence of sperm was found to correlate poorly with the time since intercourse.

Acid Phosphatase↗

PubMed1979

Testicular acid phosphatases of the mouse. Characterization after chromatographic fractionation.

The testicular homogenate of adult mice was eluted by DEAE-cellulose chromatography. Four peaks of acid phosphatase were identified. The pooled samples of each peak were used to determine substrate specificity, pH-optima, modifier characteristics, thermal stability, and Km-values. The results obtained suggest that each peak may represent a separate and distinct type of acid phosphatase. These observations are very similar to those previously obtained with the rat testis. The acid phosphatase activities in the mouse seem, however, to differ biochemically to some extent from those in the rat.

Acid Phosphatase↗

PubMed1979

Cytological events in allo-stimulated lymphocytes triggered by exposure to stimulatory alloantigens. II. Changes in the areal density of cytoplasmic vacuoles and in the subcellular localization of acid phosphatase.

H-2b lymphocytes were sensitized against H-2d alloantigens by lymphocyte culture reaction and incubated with H-2d mastocytoma cells. The interaction between lymphoid cells and mastocytoma cells was stopped by fixation with glutaraldehyde. The areal density of the cytoplasmic vacuoles as well as the subcellular localization of acid phosphatase in lymphocytes were examined by electron microscopy. Two populations of lymphocytes were observed, small lymphocytes with heterochromatic nuclei and larger lymphocytes (lymphoblasts) with euchromatic nuclei. Only the lymphoblasts showed change following interaction with target cells. The vacuole area in percent of cytoplasmic area (vacuole areal density) of sensitized lymphoblasts increased during the first 30 minutes and from the third to fourth hour of interaction with target cells. Acid phosphatase staining was observed in the Golgi apparatus of the lymphoblasts after 30 minutes of interaction. Multivesicular bodies showed acid phosphatase staining within 20 minutes of interaction with target cells. After 20 minutes of interaction, phagosomes containing myelin figures were formed. These phagosomes also showed acid phosphatase staining and during the next hours of interaction their number increased over the number of multivesicular bodies.

Acid Phosphatase↗

PubMed1979

Acid phosphatase in normal human blood cells: characterization by isoelectric focusing in polyacrylamide gel.

Using the high resolution technique of isoelectric focusing in polyacrylamide gel, isoenzymatic components could be discerned in acid phosphatase extracted from normal human lymphocytes, granulocytes, monocytes, and platelets. For each cell type, distinctive isoenzymatic patterns of acid phosphatase activity could be observed. These studies provide further evidence that various types of cellular differentiation are associated with differences in isoenzymatic components of acid phosphatase.

Acid Phosphatase↗

PubMedDate not supplied

Lymphocyte lysosomal acid phosphatase in patients with carcinoma of the larynx.

The activity of lysosomal acid phosphatase in the peripheral blood lymphocytes was determined by using the method of Barka and Anderson in 20 men with carcinoma of the larynx, untreated. The results were compared with those in 20 healthy subjects. In the patients a statistically significant decrease of the lymphocyte count exhibiting enzyme-positive lysosomal granules was noted but the number of the lymphocytes with granular and diffuse or only diffuse type of cytochemical reaction was significantly increased. The lack of significant differences in the total lymphocyte count between patients and controls suggests the possibility of lysosome disruption and subsequent release of enzymes into the cytoplasm in the patients studied. The anomalies of the enzyme-positive lymphocyte lysosomal equipment are discussed in the light of the data on immunologic alterations in cancer patients, and of those suggesting that acid phosphatase may serve as marker of T cells.

Acid Phosphatase↗

PubMed2003

Development of immunoassays for type-5 tartrate-resistant acid phosphatase in human serum.

BACKGROUND: Tartrate-resistant acid phosphatase (TRAP) is known as a marker of bone resorption. The purpose of this study was the development of a sensitive and specific immunoassay for TRAP. METHODS: We have developed two types of immunoassays, enzyme-linked immunosorbent assay (ELISA) and immunoselective enzyme immunoassay (ISEA) using monoclonal antibodies to recombinant TRAP, for determination of TRAP in human serum. To evaluate assay performance, recovery and dilution tests were performed. Further, we determined serum TRAP levels of patients with secondary hyperparathyroidism at different pH conditions. RESULTS: The detected ranges of ELISA and ISEA were between 0.08 and 5 microg/l and between 0.063 and 4 U/l. Different concentrations of TRAP added were recovered on average at 98.0% in ELISA and 102.9% in ISEA. In the serial dilution test, serum TRAP levels were on average at 101.6% and 109.6% of the expected values in ELISA and ISEA, respectively. The serum TRAP levels of patients with secondary hyperparathyroidism were significantly higher than those of normal controls in ELISA and ISEA. Similar TRAP levels were obtained in the conditions at pH 5.5 and 6.1 in ISEA. CONCLUSION: The present findings suggest that our assay methods are applicable for clinical tests, and strengthen the idea that serum TRAP is useful as a marker for bone resorption.

Acid Phosphatase↗

PubMed1970

Senescense: association of synthesis of Acid phosphatase with banana ripening.

During ripening of banana (Musa sapientum L., var. Gros Michel or Valery) acid phosphatase activity increases 13-to 26-fold in the precipitate and 2- to 4-fold in the supernatant fraction of tissue homogenates. These increases are closely correlated with the onset and peak of the climacteric. The precipitate enzyme may be extracted with Triton X-100, CaCl(2) or NaCl; about 80% of it is in a 500g precipitate. Studies on effect of tonicity of the grinding medium indicate that the precipitate enzyme is desorbed from membrane or cell wall surfaces, and is not released as a result of lysis of membranes. The development of acid phosphatase during aging of tissue slices is the same as in intact fruit. Short term studies of tissue slices with cycloheximide and actinomycin D indicate that the increase in activity is owed to new enzyme synthesis, which is dependent upon synthesis of RNA. The possible effects of the increase in acid phosphatase on ripening are discussed.

Journal Article↗

PubMed1980

Fine structural and histochemical studies on salivary glands of Peripatoides novae-zealandiae (Onychophora) with special reference to acid phosphatase distribution.

The Onychophora feed on small arthropods and produce saliva when ingesting prey. Although saliva undoubtedly helps to liquefy the food its constituents have not yet been fully described. The salivary glands, two long tubes of glandularepithelium, are known to secrete a powerful protease, however, besides other enzymes and mucus. In Peripatoides novae-zealandiae there are protein-secreting cells of three types, referred to here as columnar, cuboidal and modified cells, and mucus cells. The anterior two-thirds of the gland show most cell diversity, while the posterior regionconsists mainly of columnar cells. These are the most numerous elements overall and they probably secrete salivary protease. In thick resin sections the granules of all protein-secreting cells stain strongly with methylene blue. Those of columnar cells are markedly uneven in size and accumulate distally, eventually filling the cytoplasm. More proximal Golgi regions may be discernible. Mucus cells are all of one type and their secretion droplets are stained lightly by methylene blue. The electron microscope shows that distal microvilli, desmosomes and septate junctions are common to all gland cells. In columnar cells, secretory material is contributed by Golgi complexes and by rough endoplasmic reticulum. Early secretory vacuoles containing dense material are seen in the concavity of Golgi regions. They are precursors to larger condensing vacuoles whose contents have a more flocculent appearance, and which may attain 3--4 micrometers in diameter. These evolve into secretory granules, usually of uneven texture, which are up to 2.5 micrometers in diameter. Histochemical tests for acid phosphatase show moderate amounts of enzyme throughout the gland. In whole mounts and sections the strongest reaction is in a band of cuboidal cells along the anterior median border. Columnar cells show a diffuse cytoplasmic reaction towards the base and sometimes distal to the nucleus, and mucus cells may also react strongly round the nucleus. Cytoplasm near the lumen shows little reaction. The secretory granules do not appear to contain active enzyme. Under the electron microscope a positive reaction for acid phosphatase is seen in lysosomal derivatives near the base and lateral periphery of gland cells. These bodies are probably outophagic vacuoles and they may contain membranous whorls and possibly old secretion granules. Acid phosphatase is involved also in the eleboration of new secretory granules in both columnar and mucus cells. Dense reaction products is found in a system of interconnected tubules and cisternae near the innermost face of the Golgi complex, which is interpreted as GERL. Acid phosphatase is present in the peripheral zone of adjacent early secretory vacuoles, and interconnections occur between GERL and secretory vacuoles. It is suggested that GERL tubules containing the enzyme may fuse with early secretory vacuoles and release acid phosphatase at their periphery...

Acid Phosphatase↗

PubMed1981

The effect of starvation, restricted feed intake and refeeding on acid phosphatase activity of the hypothalamus and frontal cerebral cortex of the rat.

Acid phosphatase (EC: 3.1.3.2) activity at the hypothalamus and frontal cerebral cortex has been studied in male rats maintained on different dietary regimes. The enzyme activity in the cerebral cortex did not undergo any observable changes in any of the experimental groups. Enzyme activity in the hypothalamus, rose after food deprivation in both acutely and chronically starved rats, while the enzyme activity returned to physiological levels in refed animals. The hypothalamus neuroendocrine role and a possible interregional heterogeneity for acid phosphatase in rat brain might explain the two enzymic activity patterns observed in the present experiment.

Acid Phosphatase↗

PubMed1995

Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site.

Kidney bean purple acid phosphatase (KBPAP) is an Fe(III)-Zn(II) metalloenzyme resembling the mammalian Fe(III)-Fe(II) purple acid phosphatases. The structure of the homodimeric 111-kilodalton KBPAP was determined at a resolution of 2.9 angstroms. The enzyme contains two domains in each subunit. The active site is located in the carboxyl-terminal domain at the carboxy end of two sandwiched beta alpha beta alpha beta motifs. The two metal ions are 3.1 angstroms apart and bridged monodentately by Asp164. The iron is further coordinated by Tyr167, His325, and Asp135, and the zinc by His286, His323, and Asn201. The active-site structure is consistent with previous proposals regarding the mechanism of phosphate ester hydrolysis involving nucleophilic attack on the phosphate group by an Fe(III)-coordinated hydroxide ion.

Acid Phosphatase↗

PubMed2006

Cloning, purification and crystallization of Bacillus anthracis class C acid phosphatase.

Cloning, expression, purification and crystallization studies of a recombinant class C acid phosphatase from the Category A pathogen Bacillus anthracis are reported. Large diffraction-quality crystals were grown in the presence of HEPES and Jeffamine ED-2001 at pH 7.0. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.4, b = 90.1, c = 104.2 angstroms. The asymmetric unit is predicted to contain two protein molecules with a solvent content of 38%. Two native data sets were collected from the same crystal before and after flash-annealing. The first data set had a mosaicity of 1.6 degrees and a high-resolution limit of 1.8 angstroms. After flash-annealing, the apparent mosaicity decreased to 0.9 degrees and the high-resolution limit of usable data increased to 1.6 angstroms. This crystal form is currently being used to determine the structure of B. anthracis class C acid phosphatase with experimental phasing techniques.

Acid Phosphatase↗

PubMed2003

Involvement of upstream stimulatory factors 1 and 2 in RANKL-induced transcription of tartrate-resistant acid phosphatase gene during osteoclast differentiation.

Tartrate-resistant acid phosphatase (TRAP) plays an important role in bone resorption. TRAP expression in osteoclasts is regulated by receptor activator of NF-kappaB (RANKL), a potent activator of osteoclast differentiation. However, the molecular mechanism underlying the RANKL-induced TRAP expression remains unknown. Here we show that two regions in the mouse TRAP promoter (one at -1858 to -1239 and the other at -1239 to -1039, relative to the translation start site) are implicated in RANKL-induced TRAP transcription in RAW264.7 cells. A detailed characterization of the region at -1239 to -1039 identifies a 12-bp sequence, AGCCACGTGGTG, that specifically binds nuclear proteins from RAW264.7 cells and primary bone marrow macrophages (BMMs) in an electrophoretic mobility shift assay (EMSA). Moreover, the binding is significantly enhanced in EMSA with nuclear extracts from RANKL-treated RAW264.7 cells and BMMs, suggesting that the 12-bp sequence may be involved in RANKL-induced TRAP transcription. Various assays reveal that nuclear proteins binding to the 12-bp sequence are upstream stimulatory factors (USF) 1 and 2. Importantly, mutation of the USF-binding site partially blocks RANKL-induced TRAP transcription in RAW264.7 cells, confirming that USF1 and USF2 are functionally involved in RANKL-induced TRAP transcription. In summary, our data show that USF1 and USF2 play a functional role in RANKL-dependent TRAP expression during osteoclast differentiation.

Acid Phosphatase↗

PubMed1986

A histochemical study of rat salivary gland acid phosphatase.

Male Sprague-Dawley rats received 4 mg pilocarpine/100 g body wt intraperitoneally or physiological saline as control and were killed at various intervals. Acid phosphatase was reacted on frozen sections from soft palate, parotid and submandibular glands using sodium-alpha-naphthyl acid phosphate as substrate. Various inhibitors were added to the incubation medium. The strongest acid phosphatase activity was in the parotid gland acinar and proximal secretory duct cells; the mucous minor glands of the palate were completely negative. Activity was found in the acinar cells, proximal secretory duct cells, granular and striated duct and excretory duct cells. Pilocarpine injection slightly reduced the activity up to 6 h after injection. Cupric chloride added to the incubation medium lowered the overall activity. Fluoride and molybdate inhibited the acid phosphatase reaction in all structures. Tartrate inhibited the reaction in all structures except the submandibular striated duct cells. The tartrate-resistant activity may be a Na+K+-dependent ATPase involved in re-absorbing water and electrolytes from the primary saliva.

Acid Phosphatase↗

PubMed1990

[Elastase and acid phosphatase activity in bronchoalveolar lavage fluid during chronic bronchitis].

The dynamics of acid phosphatase and granulocytic elastase activities in bronchoalveolar washings of 40 patients with chronic catarrhal bronchitis was studied. In case of effective cure, the activities of these enzymes were increased shortly on the 10-13 days from beginning of the cure. In order to study the nature of this enzymes, the additional researches were conducted. These researches demonstrated that the macrophages were the source of the acid phosphatase, and the neutrophils--elastase. The transitory increase of the activity of both enzymes is favourable prognostical sign of disease's course.

Acid Phosphatase↗

PubMed1992

Changes in enzyme expression related to differentiation and regulatory factors: the acid phosphatase of osteoclasts and other macrophages.

Human tartrate-resistant Type 5 acid phosphatase is a unique isoenzyme encoded by a gene located on chromosome 19. It is a member of a widely-distributed and structurally highly-conserved group of iron-containing proteins. It is normally expressed in certain tissue macrophages, notably osteoclasts and alveolar macrophages, but is virtually absent from the precursor monocytes. Factors which enhance or inhibit expression of this specific isoenzyme can be studied in monocytes and osteoclasts cultured in vitro. This provides opportunities to develop the use of Type 5 acid phosphatase as a reporter of pathophysiological events and an essential, though not sufficient, role in bone resorption by osteoclasts has been established by such studies.

Acid Phosphatase↗

PubMed1985

Cytochemical examination of acid phosphatase and beta-glucuronidase enzymes in low-grade B cell non-Hodgkin's lymphomas.

The differential diagnostic significance of acid phosphatase and beta-glucuronidase were studied in 77 cases of low-grade B cell non-Hodgkin's lymphomas. In most cases the results of cytochemical enzyme studies performed on malignant cells of the bone marrow were evaluated. B cell chronic lymphocytic leukaemia, centrocytic and centroblastic/centrocytic lymphomas were characterized by a weak or a negative acid phosphatase and beta-glucuronidase activity. Stronger positivity was observed in immunocytoma and in Waldenström's macroglobulinaemia, while the highest activity was found in multiple myeloma. Hairy cell leukaemia of B cell origin showed intensive tartrate-resistant acid phosphatase activity. The cytochemical examination of these lysosomal enzymes may be useful in the diagnosis of low-grade malignant lymphomas of B cell origin by completing other methods.

Acid Phosphatase↗

PubMed1981

Comparison of prostatic acid phosphatase assays.

A prospective study compared five different assays for serum prostatic acid phosphatase in the detection of carcinoma of the prostate gland. The assays included two radioimmunoassay procedures, one counterimmunoelectrophoresis procedure, and an enzymatic procedure using alpha-naphthol phosphate substrate with and without sodium tartrate inhibition. The patients' hospital records were reviewed, as were all available surgical histology slides. The patients were divided into four groups: prostatic carcinoma, benign prostatic hypertrophy, other carcinomas (besides prostatic carcinoma), and no related disease states (that would be expected to give elevated acid phosphatase levels). The results were analyzed with respect to sensitivity, specificity, predictive value of a positive result, predictive value of a negative result, and efficiency of the assays.

Acid Phosphatase↗