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At least 595 records · Page 33Linked to original sources
PubMed2002

Can a determination of tartrate-resistant acid phosphatase predict postmenopausal loss of bone mass?

BACKGROUND: A study was carried out over a 24-month interval to determine if an initial measurement of serum tartrate-resistant acid phosphatase would be predictive of bone mass loss quantified by dual-energy X-ray absorptiometry, as total bone mineral content and total bone mineral content corrected for weight. DESIGN: Sixty-two women were studied (at onset: mean age 59.7 +/- 8.9 years, 10.8 +/- 8.8 years since menopause; at conclusion: mean age 61.9 +/- 8.8 and 13.0 +/- 8.7 since menopause). RESULTS: A paired Wilcoxon test showed a small, but significant, increase in weight (P < 0.05) and decrease in height (P < 0.05). Total bone mineral content and total bone mineral content corrected for weight decreased (P < 0.005 and 0.0001, respectively). Serum tartrate-resistant acid phosphatase increased (P < 0.005). Single-regression analysis showed that the per cent bone mass loss observed between the first and second body bone mineral content measurements correlated negatively with the first serum tartrate-resistant acid phosphatase determination (r = -0.62, P < 0.0001). Changes in tartrate-resistant acid phosphatase correlated negatively with changes in total bone mineral content (r = -0.79, P < 0.0001). In a multiple regression analysis of per cent change in bone mass against initially important variables such as age, years since menopause, weight, and tartrate-resistant acid phosphatase, only tartrate-resistant acid phosphatase was significant (P < 0.0001). The sensitivity and specifity of tartrate-resistant acid phosphatase for evaluating bone loss were 86% and 78%, respectively, and the area under the curve was of 0.83 (95% CI 0.71-0.95). CONCLUSION: These results show that a simple measurement of serum tartrate-resistant acid phosphatase can help to predict the potential rate of bone mass loss in women.

Absorptiometry, Photon↗
PubMed1977

Purification and characterization of guinea-pig epidermal acid phosphatase.

Guinea-pig epidermal acid phosphatase has been purified approximately 120-fold by a procedure including acid treatment, CM-cellulose and DEAE-cellulose chromatography, and gel filtration on Sephadex G-100. The enzyme had a pH optimum at 5-0 and the optimal temperature for activity was approximately 50 degrees C. The enzyme was not activated by divalent cations or 2-mercaptoethanol, but it was inhibited by p-chloromercuribenzoate and by fluoride. The km value for p-nitrophenyl phosphate was 1-31x10-4 M, the molecular weight was about 73,000 as determined by Sephadex G-100 gel filtration and the isoelectric point was 6.1. The enzyme hydrolyzed deoxyribonucleoside monophosphates to deoxyribonucleosides.

Acid Phosphatase↗
PubMed1980

Acid phosphatase in eyes with pseudoexfoliation.

We studied the activity of acid phosphatase in the anterior segment of the eye with pseudoexfoliation histochemically and biochemically. Light and electron microscopic histochemistry revealed lead precipitates indicating acid phosphatase activity in pseudoexfoliative materials. Biochemical assay for acid phosphatase was significantly higher in the aqueous humor of eyes with pseudoexfoliation than in that of cataractous eyes without pseudoexfoliation.

Acid Phosphatase↗
PubMed2001

Legionella pneumophila major acid phosphatase and its role in intracellular infection.

Legionella pneumophila is an intracellular pathogen of protozoa and alveolar macrophages. This bacterium contains a gene (pilD) that is involved in both type IV pilus biogenesis and type II protein secretion. We previously demonstrated that the PilD prepilin peptidase is crucial for intracellular infection by L. pneumophila and that the secreted pilD-dependent proteins include a metalloprotease, an acid phosphatase, an esterase/lipase, a phospholipase A, and a p-nitrophenyl phosphorylcholine hydrolase. Since mutants lacking type IV pili, the protease, or the phosphorylcholine hydrolase are not defective for intracellular infection, we sought to determine the significance of the secreted acid phosphatase activity. Three mutants defective in acid phosphatase activity were isolated from a population of mini-Tn10-mutagenized L. pneumophila. Supernatants as well as cell lysates from these mutants contained minimal acid phosphatase activity while possessing normal levels of other pilD-dependent exoproteins. Genetic studies indicated that the gene affected by the transposon insertions encoded a novel bacterial histidine acid phosphatase, which we designated Map for major acid phosphatase. Subsequent inhibitor studies indicated that Map, like its eukaryotic homologs, is a tartrate-sensitive acid phosphatase. The map mutants grew within macrophage-like U937 cells and Hartmannella amoebae to the same degree as did wild-type legionellae, indicating that this acid phosphatase is not essential for L. pneumophila intracellular infection. However, in the course of characterizing our new mutants, we gained evidence for a second pilD-dependent acid phosphatase activity that, unlike Map, is tartrate resistant.

Acid Phosphatase↗
PubMed2005

The SCO2299 gene from Streptomyces coelicolor A3(2) encodes a bifunctional enzyme consisting of an RNase H domain and an acid phosphatase domain.

The SCO2299 gene from Streptomyces coelicolor encodes a single peptide consisting of 497 amino acid residues. Its N-terminal region shows high amino acid sequence similarity to RNase HI, whereas its C-terminal region bears similarity to the CobC protein, which is involved in the synthesis of cobalamin. The SCO2299 gene suppressed a temperature-sensitive growth defect of an Escherichia coli RNase H-deficient strain, and the recombinant SCO2299 protein cleaved an RNA strand of RNA.DNA hybrid in vitro. The N-terminal domain of the SCO2299 protein, when overproduced independently, exhibited RNase H activity at a similar level to the full length protein. On the other hand, the C-terminal domain showed no CobC-like activity but an acid phosphatase activity. The full length protein also exhibited acid phosphatase activity at almost the same level as the C-terminal domain alone. These results indicate that RNase H and acid phosphatase activities of the full length SCO2299 protein depend on its N-terminal and C-terminal domains, respectively. The physiological functions of the SCO2299 gene and the relation between RNase H and acid phosphatase remain to be determined. However, the bifunctional enzyme examined here is a novel style in the Type 1 RNase H family. Additionally, S. coelicolor is the first example of an organism whose genome contains three active RNase H genes.

Acid Phosphatase↗
PubMed1988

Total, tartrate-resistant, and tartrate-inhibited acid phosphatases in serum: biological variations and reference limits.

We studied several factors affecting biological variation in serum acid phosphatases in a population of 1195 apparently healthy subjects four years old or older. We assayed total acid phosphatase activities in the presence of a transphosphorylating agent and using alpha-naphthyl phosphate as substrate. The main factors modifying total and tartrate-resistant acid phosphatases activities in serum are similar to those observed for total and bone alkaline phosphatases activities: age, sex, and hormonal state (puberty or menopause). The tartrate-inhibited acid phosphatase activity is, however, independent of biological variations. Finally, we propose reference limits for total, tartrate-resistant, and tartrate-inhibited acid phosphatases in serum.

Acid Phosphatase↗
PubMed1977

Platelet-derived acid phosphatase isoenzyme in the serum in thrombocythemia.

Acid phosphatase is present in platelets and is released during the clotting process. In thrombocythemic conditions, this may increase serum enzymatic activity. An illustrative case in which the determination of plasma enzymatic activity suggested a platelet origin of elevated serum levels, confirmed by isoenzyme fractionation on disk polyacrylamide gel electrophoresis is presented. It is concluded that in the presence of thrombocytosis a plasma sample is preferable to a serum sample for determination of acid phosphatase activity.

Acid Phosphatase↗
PubMed1984

Clinical assessment of solid phase immunoadsorbent assay of human prostatic acid phosphatase.

A new solid phase immunoenzyme assay for human prostatic acid phosphatase was tested in clinical practice. Clearly elevated levels of prostatic acid phosphatase (PAP) were found with advancing age and even more so in patients with benign prostatic hyperplasia (BPH). In patients with localized carcinoma of the prostate there was no elevation of levels above those observed in patients with BPH. When lymph node metastases were found at staging lymphadenectomy, the preoperative level of prostatic acid phosphatase was elevated in 7 of 12 cases. Good response to hormone treatment of metastatic carcinoma of the prostate was indicated by decrease of PAP-levels to normal. Rising levels often preceded the clinical manifestation of progression.

Acid Phosphatase↗
PubMed1988

Effects of multivalent cations on cell wall-associated Acid phosphatase activity.

Primary cell walls, free from cytoplasmic contamination were prepared from corn (Zea mays L.) roots and potato (Solanum tuberosum) tubers. After EDTA treatment, the bound acid phosphatase activities were measured in the presence of various multivalent cations. Under the conditions of minimized Donnan effect and at pH 4.2, the bound enzyme activity of potato tuber cell walls (PCW) was stimulated by Cu(2+), Mg(2+), Zn(2+), and Mn(2+); unaffected by Ba(2+), Cd(2+), and Pb(2+); and inhibited by Al(3+). The bound acid phosphatase of PCW was stimulated by a low concentration but inhibited by a higher concentration of Hg(2+). On the other hand, in the case of corn root cell walls (CCW), only inhibition of the bound acid phosphatase by Al(3+) and Hg(2+) was observed. Kinetic analyses revealed that PCW acid phosphatase exhibited a negative cooperativity under all employed experimental conditions except in the presence of Mg(2+). In contrast, CCW acid phosphatase showed no cooperative behavior. The presence of Ca(2+) significantly reduced the effects of Hg(2+) or Al(3+), but not Mg(2+), to the bound cell wall acid phosphatases. The salt solubilized (free) acid phosphatases from both PCW and CCW were not affected by the presence of tested cations except for Hg(2+) or Al(3+) which caused a Ca(2+)-insensitive inhibition of the enzymes. The induced stimulation or inhibition of bound acid phosphatases was quantitatively related to cation binding in the cell wall structure.

Journal Article↗
PubMed1979

Combined serum and bone marrow radioimmunoassays for prostatic acid phosphatase.

Combined serum and bone marrow radioimmunoassays for prostatic acid phosphatase provide a unique means for the early diagnosis and more accurate clinical staging of prostatic cancer. The combined screening technique appears to be helpful, particularly in providing a clinical assessment of the presence or absence of early, subclinical lymphatic and bone marrow metastases. Low titer elevations of bone marrow prostatic acid phosphatase by radioimmunoassay have been observed commonly in clinically understaged C prostatic cancer with normal technetium bone scans, indicating the presence of unrecognized stage D disease with bone metastases. The combined screening method also is of distinct clinical value in the early diagnosis of prostatic cancer and in monitoring the effects of specific therapy. In therapeutically responsive patients marked suppression of serum and bone marrow prostatic acid phosphatase is observed regularly with the radioimmunochemical method under study.

Acid Phosphatase↗
PubMed1988

Review of acid phosphatase in the diagnosis and prognosis of prostatic cancers.

Acid phosphatase is a secretory product frequently utilized as a tumor marker for disseminated, late stage (D2) prostatic cancer. In the 40 years since this association has been recognized, this enzyme has been subjected to extensive biochemical and immunological characterizations. These techniques have also been adapted for rapid and specific determinations of the prostatic isoenzyme levels using a variety of techniques. Since acid phosphatase levels do not become significantly elevated until late stage cancer, newer markers such as prostate-specific antigen have been sought which appear earlier and may be more useful for the screening and monitoring of high risk populations. At this time it is appropriate to review the current and future status of acid phosphatase as a diagnostic aid.

Acid Phosphatase↗
PubMed1991

Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase.

The pairing of the half-cysteine residues of human prostatic acid phosphatase was established by proteolytic digestion and analysis of the resulting peptide mixtures by fast atom bombardment mass spectrometry (FAB-MS). An independently derived, full length cDNA clone was used as the basis for the interpretation of the FAB-MS data. The sequence of the native protein is that predicted from the present cDNA sequence, except for the carboxyl-terminal end and some possible post-translational deamidations. Isolated human prostatic acid phosphatase was found to have multiple carboxyl-terminal ends, terminating in Thr, Glu, and Asp, corresponding to residues 349-351 of the 354-residue protein that is predicted from the cDNA sequence after removal of a leader peptide. The protein contains no free sulfhydryl groups. The identical monomer chains of the dimeric native enzyme are found to contain three disulfide bonds, specifically Cys-129 to Cys-340, Cys-183 to Cys-281, and Cys-315 to Cys-319. In view of the conserved positions of cysteines in the homologous human and rat liver lysosomal acid phosphatases, an identical disulfide bonding pattern may be predicted for those proteins. The location of a potential antigenic site was established by selective labeling of proximate tyrosine residues predicted to be on the surface. A conserved RHGXRXP sequence is present in the prostatic, lysosomal, Escherichia coli, and yeast acid phosphatases and is predicted to be of mechanistic significance. In addition, residue Arg-54 is shown to be an active site residue by reaction of the enzyme with phenylglyoxal. Interestingly, this residue is present in a sequence RXRY (R,H) that is also present in lysosomal phosphatase and in recently described protein tyrosine phosphatases.

Acid Phosphatase↗
PubMed1982

Bone marrow and acid phosphatase by counterimmune electrophoresis: pre-treatment and post-treatment correlations.

The value of bone marrow acid phosphatase in the staging of prostatic cancer has been a controversial issue. A number of investigators have concluded that the enzymatic determinations of bone marrow acid phosphatase are inaccurate because of lack of specificity. The introduction of the immune methods for measuring acid phosphatase has revived interest in the role of immune bone marrow acid phosphatase in pre-treatment staging. Fifty-five patients underwent determination of simultaneous immune bone marrow and serum acid phosphatase before any treatment. While positive values did predict a risk for initial and subsequent metastasis they could not be used to dictate against definitive therapy. Positive bone marrow values were paralleled by positive serum values and provided no additional staging information.

Acid Phosphatase↗
PubMed1976

Identification of human seminal acid phosphatase by electrophoresis.

Recent advances in forensic science in the identification of human seminal acid phosphatase are presented, with particular attention to the acrylamide gel electrophoretic method. In that method a difficulty in distinguishing seminal acid phosphatase from certain fecal phosphatases has been observed and an attempt is made here to distinguish the phosphatases from one another experimentally by differential substrate specificity. 4-Methylumbelliferyl phosphate and alpha-naphthyl acid phosphate are used as reaction substrates. Although seminal and vaginal acid phosphatases are differentiated by the modified method, fecal phosphatase is not clearly differentiated from seminal acid phosphatase.

Acid Phosphatase↗
PubMed1981

[The significance of acid phosphatase activity in the cytologic diagnosis of thyroid malignancy (author's transl)].

The activity of acid phosphatase in thyroid cells obtained by aspiration biopsy with thin needle was studied. The results were compared with those, found by a biochemical method in the operation material of the same cases. It has been proved that there is a significant difference between malignant tumours with cytochemically mostly positive acid phosphatase reaction and colloid adenomas with mostly negative reaction. The results obtained by biochemical method showed significant quantitative differences between malignant and benign tumours. The pattern of acid phosphatase subunits (isoenzymes) in the sera of patients with thyroid malignancies were pathologic and similar to those found in mammary cancers. It can be supposed that the behavior of acid phosphatase in thyreocytes depends on same metabolic properties, perhaps on some process characteristic for malignancy, e.g. growth activity. Even this finding of cytochemically positive acid phosphatase reaction cannot be awaited to be quite specific, it has proved as a useful marker signalizing the possibility of malignancy.

Acid Phosphatase↗
PubMed2006

Molecular cloning and expression in insect cells of honeybee venom allergen acid phosphatase (Api m 3).

BACKGROUND: Acid phosphatase (Api m 3) is a major allergen in honeybee (Apis mellifera) venom, and its availability as a recombinant protein may facilitate the development of improved diagnostic tests and immunotherapies. OBJECTIVE: One objective is the determination of the complete primary structure of Api m 3 and to obtain recombinant Api m 3 on the basis of expression in insect cells. Another objective is the quantitative analysis of patient serum IgE antibody reactive to recombinant Api m 3. METHODS: The cloning of Api m 3 from venom gland cDNA and its expression as a full-length protein in eukaryotic insect cells is described. The immunoreactivity of serum IgE antibodies of honeybee venom-sensitized patients to recombinant Api m 3 was determined in an enzyme immunoassay. RESULTS: PCR amplification generated a 1122-bp DNA fragment whose identity as the coding sequence of Api m 3 was verified by several means. Recombinant Api m 3, expressed in Trichoplusia ni cells, showed an expected molecular weight and enzymatic activity at pH 4.5. Analysis of tryptic fragments of purified recombinant Api m 3 by mass spectrometry confirmed its identity. In immunoassays, recombinant Api m 3 is specifically recognized by IgE antibodies of pooled serum in Western blots and by 37% of the individual sera of honeybee venom-sensitized patients in ELISA analysis. CONCLUSION: The availability of recombinant Api m 3 provides a tool for both the development of improved diagnostic tests and the design of safer and more effective immunotherapeutic approaches for honeybee venom allergy. CLINICAL IMPLICATIONS: The recombinant venom allergen Api m 3 is a key element in the search for an optimized component-resolved approach to honeybee venom allergy with regard to both the development of superior diagnostic tests and the improvement of allergen immunotherapy.

Acid Phosphatase↗
PubMed1984

Study of the carbohydrate part of yeast acid phosphatase.

It has been found that the carbohydrate part of acid phosphatase from yeast Saccharomyces cerevisiae consists of 16 N-glycosidically linked carbohydrate chains containing from 14 to about 150 mannose units. The presence of very small amounts of O-glycosidically linked chains was indicated. Acetolysis studies pointed to a high similarity in the structure of acid phosphatase and mannan carbohydrate chains. A new method is described for cross-linking of acid phosphatase specifically via carbohydrate chains. The possibility to cross-link the enzyme subunits intramolecularly is in accordance with the suggestion that carbohydrate chains play a role in subunit associations.

Acid Phosphatase↗
PubMed1981

Presence of "prostatic" acid phosphatase in human neutrophils.

The occurrence of natural substances with antigenic properties similar to those of the prostatic acid phosphatase was examined in one patient with neutrophilic leukemia and increased activity of serum acid phosphatase. The fraction responsible for the increased serum enzyme activity was tartrate sensitive and was identified as isoenzyme 2 by polyacrylamide gel electrophoresis. This isoenzyme originated from the leukocytes but had similar electromobility to that of the prostatic acid phosphatase isoenzyme 2. Immunohistochemical and counterimmunoelectrophoretic studies indicated that this leukocytic isoenzyme was present in the neutrophils and shared antigenic properties with the prostatic isoenzyme 2. Leukocytes from one patient with acute granulocytic leukemia, two patients with polycythemia vera with neutrophilia, and five normal subjects also contained this prostatic acid phosphatase like isoenzyme. Elevated serum "prostatic" acid phosphatase activity, therefore, may be found not only in prostatic cancer but also in granulocytic leukemia and perhaps other diseases.

Acid Phosphatase↗