Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ACID PHOSPHATASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,765 records · Page 98Linked to original sources
PubMed1986

Acute and chronic retention of urine: relevance of raised serum prostatic acid phosphatase levels. A prospective study.

A prospective study of serum prostatic acid phosphatase (PAP) levels in benign prostatic disease is reported. In 12 patients with acute retention the initial PAP level when compared with the level twenty-four hours after catheterization showed a significant fall (p less than 0.02). The initial PAP level was raised above the upper limit of normal in 7 patients (in 3 markedly so, of whom 2 had subsequent histologic evidence of prostatic infarction). In 10 patients with chronic retention there was a significant rise in the PAP level twenty-four hours after catheterization, but in only 1 case did this exceed the normal range. We discuss the significance of a raised PAP level in patients with acute retention and suggest that it may indicate a group of patients in whom the etiology of acute retention is spontaneous prostatic infarction and subsequently may require different management.

Acid Phosphatase↗
PubMed1998

Characterization of high- and low-molecular weight zinc-dependent acid phosphatases in bovine liver.

We have purified two forms of Zn2+-dependent acid phosphatase (Zn2+-APase) from bovine liver, both of which require Zn2+ to hydrolyze the substrate p-nitrophenyl phosphate in an acidic environment. The apparent molecular weights of these two forms of Zn2+-APase were estimated to be about 100,000 and 62,000 by gel filtration, and about 44,000 and 31,000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, respectively. The low-molecular weight (LMW) Zn2+-APase catalyzed the hydrolysis of myo-inositol-1-phosphate in the presence of 3 mM Mg2+ at physiological pH, but the high-molecular weight (HMW) enzyme did not. The LMW-Zn2+-APase of bovine liver was recognized by polyclonal antibodies developed against the Zn2+-APase of bovine brain, but the HMW-Zn2+-APase was not.

Acid Phosphatase↗
PubMed1986

Cytochemical localization of acid phosphatase in the hindbrain of dysraphic mice.

The cytochemical localization of acid phosphatase (AP) was studied at the ultrastructural level in the abnormal neuroepithelium of dysraphic loop-tail (Lp/Lp) embryos between 9 and 12 days of gestation. At 9-11 days, normal and abnormal embryos showed a positive AP reaction throughout the thickness of the neuroepithelium, i.e., in apical, intermediate, and basal zones, although many cells were unreactive. The reaction is sensitive to sodium fluoride and occurs in saccules and vesicles associated with the Golgi complex, as well as in vacuoles of varying size containing flocculent and particulate material. Gap-junctional vesicles, which are known to occur in increased numbers in abnormal brains, were AP-negative. By 12 days of gestation, the reaction in normal embryos was localized in the midventral marginal layer, where some cell processes were filled with reaction product; in abnormal embryos, these AP-positive processes were not observed. The results indicate that perturbations in lysosomal activity may not be fundamentally involved in the etiology of dysraphism in this mutant.

Acid Phosphatase↗
PubMed1988

Characterization of secretion pattern of human prostatic acid phosphatase: a reassessment.

The daily variation of serum levels of prostatic acid phosphatase (PAP) determined by the Roy enzymatic method was investigated in 10 patients with metastatic prostatic cancer and in 10 patients without prostatic disease. Duplicate serum samples were obtained from all patients on the same day at 8 AM, 12 PM, 4 PM, and 8 PM. Statistical analysis of the mean PAP levels at the four sampling times in both groups of patients demonstrated no evidence of circadian or diurnal rhythmic variation. Prostate cancer patients did show significantly greater variability in daily PAP than patients without prostatic disease, although a distinct pattern of secretion was not observed in either group. These results underscore the potential inaccuracy of the use of single determination of serum PAP as a parameter of response in patients with metastatic prostatic cancer and in the staging of patients with clinically localized prostatic malignancy. Evaluation of trends of PAP levels over time, however, continues to play a major role in the assessment and management of patients with prostatic carcinoma.

Acid Phosphatase↗
PubMed1981

Acid phosphatase activity in the cytosol fraction of the breast cancer tissue.

Acid phosphatase activity was studied in the cytosol fraction of breast cancer tissue. Serum, plasma, and extracts of leukocyte and platelet were used for reference. The breast cancer tissue fraction had an electrophoretic mobility intermediate to leukocyte-derived bands 2 and 4 and corresponding to the platelet-derived band 3. The enzymes derived from platelet and breast cancer tissue were both inhibited by L-tartrate and showed a similar pattern for preferred substrates. By contrast, the breast cancer tissue-derived enzyme was different from the enzyme fraction responsible for the elevated serum enzyme activity in some patients with disseminated breast cancer. The two fractions could be distinguished by electrophoretic mobility and tartrate sensitivity. These findings substantiate our previous report, which suggested that the fraction responsible for elevated serum enzyme activity in the course of breast cancer is not derived from cancer tissue. It is proposed that the osteolysis, resulting from bone metastases, may be responsible for elevated serum enzyme activity in this disease.

Acid Phosphatase↗
PubMed1986

Monocyte-associated acid phosphatase isoenzyme profiles as determined in acute myeloid leukaemia cells.

The acid phosphatase (acP) isoenzymes from the blast cells of 102 cases of acute myeloid leukaemia were separated by isoelectric focusing on horizontal polyacrylamide gels. The cases were classified on the basis of the FAB cooperative group criteria. Several single bands were combined into groups (I-IV). An increase in the number of acP isoenzymes was noted which paralleled the assumed maturation along the granulocytic cell lineage from FAB M1 to FAB M3 and along the monocytic cell lineage from FAB M4 to FAB M5. One isoenzyme which was resistant to tartrate inhibition was found in 40% of the monocytic variants FAB M4 and M5, but not in the nonmonocytic cases FAB M1-M3 and M6. This particular isoenzyme, which has been described as being characteristic for hairy cell leukaemia, also appears to be a marker of the monocyte/macrophage system and the respective neoplastic counterparts. The FAB M4 and M5 patients expressed a characteristic profile of group I isoenzymes which allows for the discrimination between monocytic and nonmonocytic cells.

Acid Phosphatase↗
PubMed1983

Molecular weight differences in acid phosphatases of stem homogenates from L and S flax genotrophs.

Anionic acid phosphatase (AP) isozymes in stem homogenates of flax genotrophs L and S were examined electrophoretically. The banding pattern was similar in both genotrophs. Relative mobility (Rm) was faster in each band of L than in the corresponding band of S. These Rm shifts did not result from differences in the sample concentration or from differential rates of development. AP activity was the same in both genotrophs. The banding pattern of F1 hybrids resembled the parental pattern. No multiple banding was observed in any of the F1 bands. The Rm in the F1 hybrids showed a dominance of L. Plots of loge (Rm) against gel concentration were constructed. While the Y intercepts of the plots indicated some differences in free electrophoretic mobility, molecular conformation was the major factor underlying both the Rm differences between bands and the Rm shifts between L and S, for corresponding bands. Estimates of apparent molecular weight (MW) for the different bands ranged from 25,000 to 250,000, with a strong possibility that some bands were oligomeric forms of others. Apparent MW was, on average, 17% higher in S than L.

Acid Phosphatase↗
PubMed1999

Effect of ethanol on the activity and conformation of Penaeus penicillatus acid phosphatase.

The effect of ethanol on the activity of Penaeus penicillatus acid phosphatase has been studied. The results show that ethanol significantly inhibits enzyme activity as a non-competitive inhibitor, with Ki 8.75%. The conformational changes of the enzyme molecule induced by ethanol were followed using fluorescence emission, ultraviolet difference and circular dichroism (CD) spectra. Increasing the ethanol concentration caused the fluorescence emission intensity of the enzyme to increase. The ultraviolet difference spectra of the enzyme denatured with ethanol had two negative peaks at 220 and 278 nm, and a positive peak at 240 nm. Increasing the ethanol concentration produced a small shoulder peak at 287 nm in addition to the increases in the negative magnitudes of the 220 and 278 nm peaks. The changes of the fluorescence and ultraviolet difference spectra reflected the changes of the microenvironments of the tryptophan and tyrosine residues of the enzyme. The CD spectrum changes of the enzyme show that the secondary structure of the enzyme also changed. The results suggest that ethanol is a non-competitive inhibitor and the conformational integrity of the enzyme is essential for its activity.

Acid Phosphatase↗
PubMed1986

Ultrastructural localization of acid phosphatase in the hindbrain of the mouse embryo.

The distribution of acid phosphatase (AP) in neuroepithelial cells in the embryonic hindbrain of the C57BL mouse was determined by means of ultrastructural cytochemistry. Fixed tissues were incubated in Gomori medium containing Na-beta-glycerophosphate as substrate and were post-fixed in osmium tetroxide, routinely dehydrated, and embedded in Epon. At 8.5-11 days, the reaction occurred in apical, intermediate, and basal zones of the neuroepithelium, although many cells were unreactive. In AP-positive cells, reaction product could be seen in saccules and vesicles associated with the Golgi complex, in large ill-defined vacuoles resembling autolysosomes, and in smaller membrane-bound bodies. By 12 days, most cells were unreactive, but a densely concentrated reaction product filled some cell processes in the midventral marginal layer. In all regions studied, the AP reaction was sensitive to sodium fluoride. Treatment with saponin and Triton-X did not affect the pattern or extent of the reaction. The results indicate that a change occurs in the nature of the AP reaction coincidental with differentiation between the eleventh and twelfth day, and that ultrastructural cytochemistry provides a means for further analysis of modifications in the distribution of AP during even earlier stages of neural development.

Acid Phosphatase↗
PubMed1997

HLA-DR2 phenotype and plasma lysozyme, beta-glucuronidase and acid phosphatase levels in pulmonary tuberculosis.

SETTING: Tuberculosis Research Centre, Indian Council of Medical Research, Madras, India. OBJECTIVE: To elucidate the role of HLA-Class II genes/gene products on phagocyte enzymes such as lysozyme, beta-glucuronidase and acid phosphatase in the plasma of pulmonary tuberculosis patients. DESIGN: Serological determination of HLA-DR and -DQ antigens was carried out in 54 active and 84 inactive pulmonary tuberculosis (quiescent) patients and 36 healthy control subjects. The levels of lysozyme, beta-glucuronidase and acid phosphatase were measured in the plasma of tuberculosis patients and control subjects. RESULTS: Increased lysozyme levels were observed in active pulmonary tuberculosis patients. beta-glucuronidase activity was higher in inactive-TB than in active-TB patients and control subjects. HLA-DR2 positive patients showed a lower lysozyme level than -DR2 negative patients. CONCLUSION: Increase in the plasma lysozyme level in active TB reveals the active stage of the disease. Further, increase in the activity of beta-glucuronidase in inactive-TB patients reveals the quiescent stage of the disease. The low level of lysozyme in HLA-DR2 positive patients may also be one of the possible factors involved in susceptibility to tuberculosis.

Acid Phosphatase↗
PubMed1987

Immunochemical characterization of human red cell acid phosphatase isozymes.

An immunological study was performed on human red cell acid phosphatase (ACP1) isozymes encoded by different alleles, each of which is expressed as an electrophoretically fast (f) isozyme and a slow (s) isozyme. These isozymes reacted as two immunochemically different groups. Allele-specific reactions were not detected between either the f isozymes or the s isozymes. Quantitation of ACP1 isozymes in red cells by crossed immunoelectrophoresis revealed a phenotype-dependent variation in the concentration of isozyme protein. A simple gene dosage effect was indicated and the ordering of the ACP1 alleles (ACP1*A less than ACP1*B less than ACP1*C less than ACP1*E) was identical to that found for enzyme activity levels. Also, an allele effect on the proportion between s and f isozymes (s/f) was observed; the ordering here was ACP1*B less than ACP1*A less than ACP1*C, which is the same as that reported for the susceptibility to modulation with purines. These variations in isozyme protein levels appear to account for the phenotypic differences in the intensity of the isozyme bands, when activity-stained after electrophoresis, and in the red cell enzyme activity levels. Investigation of two carriers of a Null allele showed no evidence of an aberrant protein product, and half-normal concentrations of enzyme protein were observed in the red cells of these individuals.

Acid Phosphatase↗
PubMed2001

Protein kinase C pathway is involved in regulating the secretion of prostatic acid phosphatase in human prostate cancer cells.

The stimulated secretion of prostatic acid phosphatase (PAcP) has been known to be a hallmark of androgen action on human prostate epithelial cells for the last five decades. The molecular mechanism of androgen action on PAcP secretion, however, has remained mostly unknown. We investigated the molecular mechanism that promotes PAcP secretion in LNCaP human prostate carcinoma cells which express PAcP and are androgen-responsive. Treatment with 12-o-tetradecanoyl phorbol-13-acetate (TPA), a protein kinase C (PKC) activator, resulted in an increased secretion of PAcP in a dose- and time-dependent fashion. 4Alpha-phorbol, a biologically inactive isomer of TPA, had no effect. This TPA stimulation of PAcP secretion was observed 2 h after exposure, while TPA did not have a significant effect on the mRNA level even with a 6 h treatment. A23187 calcium ionophore, known to mobilize cellular calcium which is a co-factor of PKC, also activated PAcP secretion. This TPA stimulation of PAcP secretion was more potent than the conventional stimulating agent 5alpha-dihydrotestosterone (DHT) at the same concentration of 50 nM. Furthermore, the action of TPA and DHT on PAcP secretion was blocked by five different PKC inhibitors. Results also showed that DHT, as well as TPA, could rapidly modulate PKC activity. Therefore, PKC can regulate PAcP secretion, and may also be involved in DHT action on PAcP secretion.

Acid Phosphatase↗
PubMed1996

Epitope enhancement for immunohistochemical demonstration of tartrate-resistant acid phosphatase.

We have developed a monoclonal antibody (9C5) for immunohistochemical localization of tartrate-resistant acid phosphatase (TRAcP). This antibody reacts with a denatured epitope of TRAcP and requires enhancement methods to promote antigenicity in paraffin-embedded tissues. We used this antibody to systematically examine proteolytic digestion and heat denaturation conditions for epitope enhancement in both paraffin sections and fixed smears. The goal was to increase the sensitivity of the immunohistochemical stain for TRAcP. Optimal conditions for proteolytic digestion were established. Denaturation in a conventional boiling water bath was compared to microwave irradiation in several commonly used solutions. Immunohistochemistry was compared directly to TRAcP cytochemistry in fixed smears from hairy cell leukemia specimens to gauge the level of sensitivity of our improved method. Attempts were made to "retrieve" the 9C5 epitope from overfixed tissues and aged smears. Maximal immunoreactivity of TRAcP was achieved by microwave irradiation in a citrate or Tris buffer of pH 6.0-8.0 without the need for a subsequent protease digestion step. With this method of epitope enhancement, immunohistochemistry with antibody 9C5 was as sensitive as direct cytochemical staining of TRAcP activity. However, once a tissue specimen had been overfixed or a smear stored for a year or more, the 9C5 epitope was no longer retrievable. The key element in epitope enhancement for 9C5 immunohistochemistry is heat denaturation of the target epitope. Immunohistochemistry of TRAcP in paraffin sections would be a great asset to the study of specialized forms of the monocyte/macrophage lineage and to the process of macrophage activation. It would also provide another means for more precise evaluation of residual disease in bone marrow of patients treated for hairy cell leukemia.

Acid Phosphatase↗
PubMed1991

Evaluation of prostate-specific antigen and prostatic acid phosphatase in untreated prostatic carcinoma and benign prostatic hyperplasia.

Prostate specific acid phosphatase (PAP) (Abbott, solid-phase enzyme immunoassay) and prostate specific antigen (PSA) (Hybritech, immunoradiometric assay) were determined in 162 newly diagnosed prostatic carcinoma patients, 187 patients with benign prostatic hyperplasia (BPH) and 127 controls. The upper limit of normal in controls for PAP was 2.2 micrograms/l and for PSA 5.0 micrograms/l. In the BPH group PAP was raised in 21%, for PSA in 41%. When the cut-off level of PSA was raised to 10.0 micrograms/l, 20% of BPH patients had an increased level. PSA was superior to PAP for the detection of prostatic cancer in all stages. Of the 162 patients with prostatic carcinoma, 88 had localised diseases and 74 had metastatic spread. PSA and PAP levels increased with each advancing clinical stage. PAP was elevated in 35% of the patients with cancer confined to the prostate. PSA in 69%. (PSA level 10.0 micrograms/l: 57%). In those patients with metastatic spread PAP was elevated in 77% compared with 96% for PSA. (PSA level 10.0 micrograms/l: 92%). The combined use of PSA and PAP does not give a greater accuracy in the screening of prostate cancer when compared with the sole use of PSA. PAP was elevated in only 4 patients when PSA was normal. In the BPH group there was no proven effect of micturition, frequency or residual urine on the SPA level. However, in this group infection may cause a rise in the PSA level.

Acid Phosphatase↗
PubMed1995

17 beta-estradiol suppresses gene expression of tartrate-resistant acid phosphatase and carbonic anhydrase II in ovariectomized rats.

Tartrate-resistant acid phosphatase (TRACP) and carbonic anhydrase II (CA II) are key enzymes responsible for osteoclastic bone resorption. In this study, we proposed that estrogen loss in postmenopausal osteoporosis may enhance gene expression of TRACP and CA II, and subsequently increase osteoclastic bone resorption. We have, therefore, used the ovariectomized rat model of postmenopausal bone loss to investigate changes at the gene transcriptional level in osteoclastic bone-resorbing enzymes in ovariectomized (OVX) rats, sham ovariectomized (S-OVX) rats, and estrogen-treated ovariectomized (E-OVX) rats. We have demonstrated for the first time that ovariectomy in rats enhances gene expression of TRACP, and CA II. The mRNA levels in OVX were approximately three- and four-fold higher, respectively, than those in S-OVX. Enhancement was observed 1 week after ovariectomy and transcripts remain high during the experimental period of 8 weeks. Administration of 17 beta-estradiol to OVX (E-OVX) reduced gene expression of these osteoclastic bone-resorbing enzymes 18 hours after injection. It appeared that the suppression of the osteoclastic bone-resorbing enzymes by 17 beta-estradiol was most effective during the first 1-2 weeks but the degree of suppression was reduced at 8 weeks after ovariectomy. In conclusion, our results suggest that estrogen prevents bone loss by reducing the mRNA levels of osteoclastic bone-resorbing enzymes in bone tissue.

Acid Phosphatase↗
PubMed1992

Expression of human prostatic acid phosphatase activity and the growth of prostate carcinoma cells.

Human prostatic acid phosphatase (PAcP) is a tissue-specific differentiation antigen and is the major phosphotyrosyl (p-tyr) protein phosphatase in normal differentiated prostate epithelial cells. In prostate carcinomas, cellular PAcP has a low expression. We examined the expression of cellular PAcP activity and its correlation with cell growth that may lead us to understand the role of tyrosine phosphorylation in human prostate cells. LNCaP cells, which expressed the highest cellular PAcP activity, had the slowest growth rate and the lowest p-tyr level among three human prostate carcinoma cell lines: LNCaP, DU145, and PC-3. This inverse correlation was further examined in LNCaP cells, since these cells remain hormone-sensitive. Androgen, a classical stimulator of prostate cells, stimulated the growth of LNCaP cells while cellular PAcP activity decreased and p-tyr levels increased. This phenomenon was also observed when cells were treated with epidermal growth factor and fetal bovine serum. Both epidermal growth factor and fetal bovine serum stimulated the growth of LNCaP cells whereas cellular PAcP activity decreased. Furthermore, when cell growth was arrested at low temperatures (23 degrees C), cellular PAcP activity was elevated. To establish the relationship of cellular PAcP activity with cell growth rate, we transfected a complementary DNA encoding the full length PAcP protein into another human prostate carcinoma line, PC-3, that lacks endogenous PAcP. Two stable transfectants, designated PC-18 and PC-416 cells, were obtained and shown to express PAcP mRNA transcribed from the transfected complementary DNA. The expression of PAcP activity in PC-416 cells, but not PC-18 cells, was associated with a lower p-tyr level and a slower growth rate than control cells transfected with the expression vector alone. In conclusion, in LNCaP cells, the stimulated cell growth is associated with an increased p-tyr level and a decreased cellular PAcP activity. In PAcP complementary DNA-transfected PC-416 cells, the low level of p-tyr corresponds to a slow growth rate.

Acid Phosphatase↗
PubMed1998

A second two-component regulatory system of Bordetella bronchiseptica required for bacterial resistance to oxidative stress, production of acid phosphatase, and in vivo persistence.

Random minitransposon mutagenesis was used to identify genes involved in the survival of Bordetella bronchiseptica within eukaryotic cells. One of the mutants which exhibited a reduced ability to survive intracellularly harbored a minitransposon insertion in a locus (ris) which displays a high degree of homology to two-component regulatory systems. This system exhibited less than 25% amino acid sequence homology to the only other two-component regulatory system described in Bordetella spp., the bvg locus. A risA'-'lacZ translational fusion was constructed and integrated into the chromosome of B. bronchiseptica. Determination of beta-galactosidase activity under different environmental conditions suggested that ris is regulated independently of bvg and is optimally expressed at 37 degrees C, in the absence of Mg2+, and when bacteria are in the intracellular niche. This novel regulatory locus, present in all Bordetella spp., is required for the expression of acid phosphatase by B. bronchiseptica. Although catalase and superoxide dismutase production were unaffected, the ris mutant was more sensitive to oxidative stress than the wild-type strain. Complementation of bvg-positive and bvg-negative ris mutants with the intact ris operon incorporated as a single copy into the chromosome resulted in the reestablishment of the ability of the bacterium to produce acid phosphatase and to resist oxidative stress. Mouse colonization studies demonstrated that the ris mutant is cleared by the host much earlier than the wild-type strain, suggesting that ris-regulated products play a significant role in natural infections. The identification of a second two-component system in B. bronchiseptica highlights the complexity of the regulatory network needed for organisms with a life cycle requiring adaptation to both the external environment and a mammalian host.

Acid Phosphatase↗
PubMed2000

Osteoclastic tartrate-resistant acid phosphatase (Acp 5): its localization to dendritic cells and diverse murine tissues.

Tartrate-resistant acid phosphatase (TRAP) is a histochemical marker of the osteoclast. It is also characteristic of monohistiocytes, particularly alveolar macrophages, and is associated with diverse pathological conditions, including hairy cell leukemia and AIDS encephalopathy. To study the biology of this enzyme, we investigated its expression and activity in mouse tissues. Confocal fluorescence studies showed that TRAP is localized to the lysosomal compartment of macrophages. In adult mice, high activities of the enzyme were demonstrated in bone, spleen, liver, thymus, and colon, with lower amounts in lung, stomach, skin, brain, and kidney. Trace amounts were detected in testis, muscle, and heart. Expression of TRAP mRNA was investigated in tissue sections by in situ hybridization and protein expression was monitored by histochemical staining or immunohistochemically. TRAP is widely expressed in many tissues, where it is associated with cells principally originating from the bone marrow, including those of osteoclast/macrophage lineage. The cellular distribution of TRAP mRNA and enzyme antigen in the tissues corresponds closely to that of cells staining with an antibody directed to the CD80 (B7) antigen. Therefore, to confirm its putative localization in dendritic cells, isolated bone marrow dendritic cells were matured in culture. These co-stained strongly for TRAP protein and the CD80 antigen. These studies demonstrate that TRAP is a lysosomal enzyme that is found in diverse murine tissues, where it is expressed in dendritic cells as well as osteoclasts and macrophages, as previously shown. (J Histochem Cytochem 48:219-227, 2000)

Acid Phosphatase↗