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PubMed2001

Analysis of arylsulfatases A and B, acid phosphatase, lactate dehydrogenase, and aspartate transaminase in chronic periapical lesions of endodontic origin.

Attempts were made to detect and measure the activities of arylsulfatases. A&B acid phosphatase, lactate dehydrogenase, and glutamate oxaloacetate transaminase (aspartate transaminase) enzymes in human chronic lesions of endodontic origin. Thirteen periapical lesions of endodontic origin and 11 noninflamed control periapical tissues were obtained. The specimens were carried to the laboratory on liquid nitrogen and kept at -70 degrees C. Samples were thawed, homogenized, and then assayed for enzyme activities. The specific activities of arylsulfatase A (nmol/hr/mg protein) were 55.0+/-10.7 (chronic lesions) vs. 3.4+/-2.2 (controls) (p < 0.01). Arylsulfatase B specific activities (nmol/hr/mg protein) were 50.3+/-6.4 (chronic lesions) vs 91.8+/-18.4 (controls). Total acid phosphatase activities (mU/mg protein) were 45.8+/-6.6 (chronic lesions) vs. 26.8+/-3.1 (controls). Lactate dehydrogenase activities (Berger-Broida units/mg protein) of the chronic periapical lesions were significantly higher than the control group (362+/-63.2) vs. (140+/-46.0) (p < 0.05). There was no significant difference between the specific activities of aspartate transaminase in chronic lesions and the control group (68.0+/-14.5) vs. (53.0+/-10.4) mU/mg protein).

Acid Phosphatase↗
PubMed1979

Prostatic acid phosphatase by radioimmunoassay tumor marker in bone marrow.

Bone marrow acid phosphatase was determined by radioimmunoassay and enzymatic analysis in 95 patients with benign prostatic hypertrophy, 50 patients with disseminated prostatic carcinoma and 36 patients with non-prostatic malignancy. The results indicate superior specificity of the radioimmunoassay. A brief review of the topic and the clinical implications are discussed.

Acid Phosphatase↗
PubMed1975

The red cell acid phosphatase polymorphism in Greek b-thalassemia patients.

Red cell acid phosphatase polymorphism was studied by starch gel electrophoresis in 70 b-thalassemia patients and in 310 healthy Greeks. Our results gave the following gene frequencies; b-thalassemia patients: pa 0.321, pb 0.643, pc 0.036; healthy Greeks: pa 0.302, p b 0.653, pc 0.045. No statistically significant differences were found between the two groups.

Acid Phosphatase↗
PubMed1990

Deoxyribonucleic acid ploidy and the direct assay of prostatic acid phosphatase and prostate specific antigen in fine needle aspiration biopsies as diagnostic methods in prostatic carcinoma.

We used fine needle biopsies from prostatic tumors at routine examinations in 133 patients. Cytological grading was performed with a scoring system. Cellular prostatic acid phosphatase and cellular prostate specific antigen from the aspirates were quantitated. Deoxyribonucleic acid flow cytometry was performed and the tumors were subdivided into diploid, tetraploid and aneuploid groups. Tumor staging was assessed by digital examination. A decrease in the biochemical markers was significantly correlated with the increase in malignancy grade, tumor stage and a shift from diploid to aneuploid tumors. Cellular prostatic acid phosphatase and cellular prostate specific antigen as well as tumor ploidy may contribute to the objective determination of the malignancy potential of the prostatic carcinoma.

Acid Phosphatase↗
PubMed1983

Binding sites of seminal acid phosphatase to Canavalia gladiata DC lectin.

Binding sites of seminal acid phosphatase (AcP) to Canavalia gladiata DC lectin (Can G) were examined. Complex of AcP and Can G produced in a test tube was solubilized with alpha-methyl-D-mannoside and was fractionated with Sephadex G-200. The elution pattern of AcP activity of the complex was similar to that of seminal plasma, suggesting that the reaction of AcP and Can G was reversible. Crossed immuno-affinoelectrophoresis with intermediate gel containing free Can G or immobilized one showed that AcP molecule had two or more binding sites per molecule to Can G. AcP activity of frozen sections of the prostate was inhibited by tartaric acid but not by Can G. However, Can G bound to AcP of the sections could be detected with FITC-labeled anti-Can G. These results indicate that the active site of AcP to Can G is not identical with that to the substrate.

Acid Phosphatase↗
PubMed2006

Tartrate-resistant acid phosphatase 5b (TRACP 5b) as a marker of bone resorption.

Tartrate-resistant acid phosphatase (TRACP) is an enzyme that is expressed in high amounts by bone resorbing osteoclasts, inflammatory macrophages and dendritic cells. Two forms of TRACP circulate in human blood, TRACP 5a derived from macrophages and dendritic cells, and TRACP 5b derived from osteoclasts. Recent data have demonstrated the utility of TRACP 5b as a marker of osteoclast number and bone resorption, and serum TRACP 5a as a marker of inflammatory conditions. This review summarizes the scientific knowledge on the role of TRACP in osteoclastic bone resorption, the mechanism of TRACP 5b generation in osteoclasts and its secretion into the blood circulation, the methodology of measuring TRACP 5b, diagnostic evidence for the use of TRACP 5b as a resorption marker, and characteristics of TRACP 5b compared to other commonly used bone turnover markers.

Acid Phosphatase↗
PubMed2001

Tartrate-resistant acid phosphatase isoform 5b as serum marker for osteoclastic activity.

BACKGROUND: Tartrate-resistant acid phosphatase (AcP) 5b is a marker of osteoclastic activity and bone resorption. Immunoassays for serum TRAcP may lack sensitivity and specificity because of the presence of non-bone isoform 5a. The purpose of this study was to isolate the serum isoforms, quantify their disease-related expressions, and test an improved immunoassay for TRAcP 5b. METHODS: We separated TRAcP isoforms chromatographically from pooled sera of healthy, rheumatoid arthritis (RA) and endstage renal disease (ESRD) subjects. TRAcP isoforms were identified by electrophoresis and quantified by biochemical and immunochemical assays. Serum TRAcP activity in healthy, RA, and ESRD cohorts was assessed at pH 5.5 and 6.1, and compared with bone alkaline phosphatase (BAP) and N-telopeptides of type I collagen (NTx). RESULTS: TRAcP isoforms 5a and 5b were present in all sera; 5b was identical to osteoclastic TRAcP. In serum from healthy subjects, 5a accounted for 87% of the enzyme protein but only 55% of the activity. In RA, both isoforms were increased two- to threefold in protein, but their specific activities were subnormal. In ESRD, only 5b was abnormal, being increased fivefold in protein and threefold in activity. In RA sera, TRAcP activity did not correlate with either BAP or NTx. In ESRD sera, TRAcP activity correlated with BAP and NTx only when measured at pH 6.1. CONCLUSIONS: All sera contained both TRAcP isoforms 5a and 5b, but only 5b was present in bone. TRAcP isoform expression was variable in different diseases. Measurement of TRAcP activity at pH 6.1 improves the specificity of immunoassay for isoform 5b.

Acid Phosphatase↗
PubMed1996

Effect of vanadium compounds on acid phosphatase activity.

The direct effect of different vanadium compounds on acid phosphatase (ACP) activity was investigated. Vanadate and vanadyl but not pervanadate inhibited the wheat germ ACP activity. These vanadium derivatives did not alter the fibroblast Swiss 3T3 soluble fraction ACP activity. Using inhibitors of tyrosine phosphatases (PTPases), the wheat germ ACP was partially characterized as a PTPase. This study suggests that the inhibitory ability of different vanadium derivatives to modulate ACP activity seems to depend on the geometry around the vanadium atom more than on the oxidation state. Our results indicate a correlation between the PTPase activity and the sensitivity to vanadate and vanadyl cation.

3T3 Cells↗
PubMed2004

Properties and expression of human tartrate-resistant acid phosphatase isoform 5a by monocyte-derived cells.

Human serum tartrate-resistant acid phosphatase exists as two enzyme isoforms (TRACP 5a and 5b), derived by differential, post-translational processing of a common gene product. Serum TRACP 5b is from bone-resorbing osteoclasts (OC) and becomes elevated in diseases of increased bone resorption. TRACP 5a is secreted by macrophages (MPhi) and dendritic cells (DC) and is increased in many patients with rheumatoid arthritis. Our purpose was to fully characterize the properties of human TRACP isoforms and to produce an antibody specific to TRACP 5a for use as a biomarker in chronic inflammatory diseases. Partially purified, natural serum TRACP isoforms and recombinant TRACP 5a (rTRACP 5a) were compared with respect to specific activity and subunit structure and presence of sialic acid. Mice were immunized with rTRACP 5a, and resulting hybridomas were screened for monoclonal antibody to serum TRACP 5a. One antibody, 220, was tested for its epitope specificity and use in various immunological techniques. rTRACP 5a had properties identical to serum TRACP 5a. Antibody 220 was specific for the trypsin-sensitive epitope in the loop peptide, present only in TRACP 5a. Antibody 220 was effective for specific immunoprecipitation, immunoassay, and immunoblot of TRACP 5a. Intact TRACP was present in MPhi, DC, and OC. TRACP 5a was the predominant isoform secreted by MPhi and DC, whereas TRACP 5b was the predominant isoform secreted by OC. TRACP isoforms 5a and 5b may have different functions inside and outside of monocyte-derived cells. Antibody 220 is an important resource for studies of the biosynthetic relationship among TRACP isoforms and of the significance of serum TRACP 5a as a marker in diseases of bone metabolism and inflammation.

Acid Phosphatase↗
PubMed1994

Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component.

An acid phosphatase containing a 27-kDa polypeptide component has been identified in Escherichia coli by means of a zymogram technique. The enzyme is secreted in the periplasmic space and is able to hydrolyze several organic phosphate esters, but not diesters, showing preferential activity on p-nitrophenyl phosphate and other phenolic phosphate esters. Production of the enzyme apparently occurs only in cells growing on carbon sources other than glucose.

Acid Phosphatase↗
PubMed1981

A simple immunohistochemical method for the detection of prostatic acid phosphatase.

A simplified immunohistochemical method was developed to identify prostatic cells in paraffin sections for the diagnosis of primary or metastatic prostatic carcinoma. By incubating each section with a specific antiserum, followed by incubation with a specific acid phosphatase isoenzyme of the prostate, the antibody binding site is visualized by staining for acid phosphatase activity in the glandular epithelial cells of the prostate and in the metastatic prostate carcinoma cells that involve the lymph node. The present method is simpler and more specific than the previously described indirect immunoperoxidase method.

Acid Phosphatase↗
PubMed1999

Acid phosphatase polymorphism in European shad (Fish: Clupeids).

Genetic polymorphism of acid phosphatases was investigated in 11 populations of the two European Alosa species using isoelectric focusing after sample treatment with neuraminidase. Two distinct loci, ACP1 and ACP2, were detected being ACP2 polymorphic. The observed genetic diversity between the species at the ACP2 locus supports other studies which indicate that A. alosa is the less polymorphic species of the two. This locus shows a higher geographic than interspecific pattern of differentiation and the ACP*2 allele is essentially confined to the Mediterranean.

Acid Phosphatase↗
PubMed1987

[Optimization of the determination of muscle acid phosphatase in the post-mortem chicken. Study of the stability of enzyme activity during meat storage at 4 degrees C. and -20 degrees C].

A colorimetric quantitative determination of total acid phosphatase in chicken muscle is proposed. Optimal conditions for the use of this enzyme were studied. This method allowed to establish that the muscular acid phosphatase of chicken does not resist to a 30 minutes incubation at 65 degrees C but that its activity is unchanged when the meat is stored at + 4 degrees C for 10 days or at -20 degrees C for 4 months.

Acid Phosphatase↗
PubMed1988

Pseudomonas aeruginosa acid phosphatase contains an anionic site with a trimethyl subsite. Kinetic evidences obtained with alkylammonium ions.

In this work the action of the following compounds upon Ps. aeruginosa acid phosphatase has been studied: 1) alkylammonium compounds; 2) aminoalcohols and aminoacids with different substituents (-H, -CH2OH and -CH3) attached to the nitrogen atom; 3) alcohols analogous to some compounds of the above series, but without the amino group. It was found that the enzyme inhibition was more effective with N-trimethylated compounds than with the triethylated ones. The degree of inhibition depended on the number of methyl groups bound to the nitrogen atom. Taking into account the choline and betaine series the hydroxyl derivatives showed more affinity for the enzyme than the carboxylated ones. In each series the Ki values increased with the decrease of methyl groups bound to the nitrogen atom. The presence of a positively charged nitrogen atom in the molecule of the effector was essential. These results enable us to confirm that in the molecule of Ps. aeruginosa acid phosphatase there exists an anionic site with one subsite with affinity for methyl groups.

Acid Phosphatase↗
PubMed1985

Serum half life of prostatic acid phosphatase.

Traumatic manipulation of the prostate can cause elevated prostatic acid phosphatase (PAP) values. To avoid falsely elevated PAP values after prostatic trauma we studied the serum half life of PAP and the time taken to return to preoperative levels in patients undergoing transurethral resection (TUR-P). Although we observed a broad variation in peak PAP values the half life of PAP is fairly constant at about 1.1-2.6 h. Preoperative values were reached within 30 h. We conclude that PAP determinations can safely be carried out 30 h after prostatic trauma without any risk of falsely elevated PAP values.

Acid Phosphatase↗
PubMed1988

[Purification of prostatic acid phosphatase and prostate specific antigen from human seminal plasma].

Prostatic acid phosphatase (PAP) and prostate specific antigen (PA), which are useful markers of diagnosis for prostatic cancer, have been purified from human seminal plasma. Total of 54.4 mg PAP and 3.0 mg PA were purified from 426.5 ml human seminal plasma. The purified antigens were demonstrated a single band by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), having a molecular weight of about 50,000 and 34,000, respectively. The PAP and PA purified from human seminal plasma were considered similar to that of prostatic tissue immunologically and biochemically.

Acid Phosphatase↗
PubMed1980

Metabolic relationship between invertase and acid phosphatase isoenzymes in Saccharomyces cerevisiae.

Repressed cells of Saccharomyces cerevisiae, subjected to inhibition of both RNA and protein synthesis, showed a pattern of membrane-bound and cytosol acid phosphatase to the external enzyme which seemed to be linked through a precursor-product relationship. Gel exclusion chromatography did not indicate clear differences between the isoenzymes. Moreover, centrifugation experiments in CsCl and precipitation with concanavalin A suggested that there were no acid phosphatase molecules devoid of carbohydrate. Membrane-bound invertase displayed a molecular weight and a carbohydrate to protein ratio smaller than those of the exocellular enzyme. The values of molecular weight and buoyant density of the membrane-bound enzyme were closer to those found for the cytosol invertase. The stability of the level of the soluble invertase detected in the cytoplasm under derepression conditions, or after RNA or protein synthesis inhibition was found to be only apparent and represented the result of an equilibrium between synthesis and degradation.

Acid Phosphatase↗