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PubMed1992

[Analysis of the quaternary structure of secreted repressible acid phosphatase from the yeast Saccharomyces cerevisiae].

The structural organization of extracellular repressible acid phosphatase from S. cerevisiae has been studied. The existence of multiple acid phosphatase forms with isoelectric points at pH 4.1-4.8 has been confirmed by isoelectrofocusing. The molecular masses of three acid phosphatase isoforms (56, 57-59, and 60 kDa) obtained after enzymatic deglycosylation correlate with the data obtained previously during the analysis of translation products in cell-free systems. Electron microscopic studies revealed that the acid phosphatase molecule has a square shape and is made up of four identical subunits with molecular masses of about 125 kDa.

Acid Phosphatase↗
PubMed1982

Prostatic cancer, acid phosphatase, creatine kinase-BB and race: a prospective study.

To examine the effectiveness of prostatic acid phosphatase and creatine kinase-BB determinations in detecting prostatic cancer serum from 594 men more than 40 years was assayed for prostatic acid phosphatase with the thymolphthalein monophosphate substrate and a radioimmunoassay kit. Creatine kinase-BB levels also were measured with a radioimmunoassay kit. Patients with benign prostatic hyperplasia had higher prostatic acid phosphatase levels than normal controls. Accordingly, to avoid a high incidence of false positives in patients with benign prostatic hyperplasia the 92.5 percentile level of the patients with benign prostatic hyperplasia (3.9 ng./ml.) was chosen as the upper limit of normal. With this critical value elevated prostatic acid phosphatase levels were observed in 6 per cent of the patients with clinical stage A disease, 8 per cent with stage B, 35 pr cent with stage C and 68 per cent with stage D. The radioimmunoassay was no more effective than the enzymatic assay in detecting prostatic cancer. A correlation between prostatic acid phosphatase levels and patient race was observed, with 80 per cent of the black patients with extracapsular prostatic cancer having elevated prostatic acid phosphatase levels compared to 34 per cent of the white patients with similar stage disease. Creatine kinase-BB was elevated only in patients with advanced disease and was of little value in the diagnosis of prostatic cancer.

Acid Phosphatase↗
PubMed1980

Testicular acid phosphatases in cattle, sheep, guinea pig, and rabbit.

Acid phosphatase activities were measured with five different substrates in the total homogenates as well as after gel filtration on Sepharose 6B and cellulose chromatography of bull, guinea pig, rabbit, and ram testes. The response of the hydrolysis rate to NaF (5 mmol/l), Co2+ (5 mmol/l) and Zn2+ (5 mmol/l) was also tested. In the total homogenate the hydrolysis of p-nitrophenyl phosphate was markedly activated by Co2+, while in the presence of Zn2+ an activation was recorded in guinea pig and some inhibition in the bull, rabbit, and ram testes. NaF caused a decline in the total acid phosphatase activity, particularly in guinea pig and ram. The gel filtration resulted in three separate activity peaks with p-NPP and beta-NP as substrates. N-ASBI-P, alpha-NP, and Tym-P gave only two peaks. After subsequent cellulose chromatography of the activities only peak II gave rise to two further activities. Peak I of gel filtration (enzyme I) was able to hydrolyze all substrates tested and was highly sensitive to NaF. Peak I of cellulose chromatography (enzyme II) also hydrolyzed p-NPP and beta-NP. It was rather resistant to NaF but sensitive to Zn2+. It was slightly activated by Co2+. Peak II of cellulose chromatography (enzyme IV) hydrolyzed only p-NPP and was markedly activated by Co2+ and Zn2+. The adult testes of bull, guinea pig, rabbit, and ram have a closely similar testicular acid phosphatase pattern. Due to relative differences in the concentrations of the four enzymes in the tissue, varying activity levels are recorded in the presence of different substrate and modifier combinations.

Acid Phosphatase↗
PubMed1988

Secretion of an active nonglycosylated form of the repressible acid phosphatase of Saccharomyces cerevisiae in the presence of tunicamycin at low temperatures.

The role of mannan chains in the formation and secretion of active acid phosphatase of yeast (Saccharomyces cerevisiae), a repressible cell surface mannoprotein, was studied in yeast protoplast systems by using tunicamycin at various temperatures. At 30 degrees C, tunicamycin-treated protoplasts did not produce active acid phosphatase; however, at 25 or 20 degrees C they formed and secreted active enzyme. This form of acid phosphatase gave 59-, 57-, and 55-kDa bands on SDS-PAGE which neither bound to concanavalin A Sepharose, nor changed in molecular weight upon treatment with endoglycosidase H, indicating that the peptides are nonglycosylated. The nonglycosylated form, like its glycosylated counterpart, is a dimer on the basis of gel permeation chromatography. The Km for para-nitrophenyl-phosphate and Ki for inorganic phosphate of both glycosylated and nonglycosylated acid phosphatases were almost the same. These results suggested that 1) the conformation of the nonglycosylated acid phosphatase secreted at low temperatures is probably identical with that of the glycosylated one, and 2) the conformation of acid phosphatase is very important for its secretion. The rate of intracellular transport of nonglycosylated acid phosphatase is about one-fourth that of the glycosylated enzyme, indicating that glycosylation facilitates the transport of acid phosphatase proteins.

Acid Phosphatase↗
PubMed1989

Processing, transport, and secretion of the lysosomal enzyme acid phosphatase in Dictyostelium discoideum.

To explain the different secretion kinetics of lysosomal enzymes in Dictyostelium discoideum, previous investigators have hypothesized the existence of a heterogeneous population of lysosomes containing either the enzyme acid phosphatase or other hydrolase enzymes. This proposal predicts that at least two targeting mechanisms exist for lysosomal enzymes in this organism. To begin to investigate this possibility, the transport, processing, and targeting of acid phosphatase was studied by using a combination of radiolabel pulse-chase procedures, subcellular fractionations, and indirect immunofluorescence microscopy. Acid phosphatase was initially synthesized in axenically growing cells as a 56-kDa precursor polypeptide that was proteolytically processed after 20 min to a 55-kDa mature protein. This enzyme was rapidly transported from the endoplasmic reticulum to Golgi complex (halftime of 3 min) as measured by the acquisition of resistance to the enzyme endoglycosidase H. Furthermore, Percoll gradient fractionations indicated that radiolabeled forms of acid phosphatase reached dense lysosomal vesicles at about the same time as final processing was occurring. Proper sorting of acid phosphatase in D. discoideum apparently was not critically dependent on low intravacuolar pH since the addition of ammonium chloride did not stimulate the missorting and secretion of acid phosphatase. These results are very similar to previous observations concerning other Dictyostelium lysosomal enzymes. Consistent with the existence of a heterogeneus population of lysosomes, the percentage of radiolabeled acid phosphatase secreted 4 h into a chase period was 15-fold lower as compared with another lysosomal enzyme, beta-glucosidase. However, acid phosphatase, alpha-mannosidase, and beta-glucosidase were all predominantly colocalized as determined by indirect immunofluorescence, which for the first time demonstrates the homogeneous nature of the lysosomal system in D. discoideum. Taken together these results suggest that the processing and transport of acid phosphatase may be similar in nature to the glycosidases. However, the different kinetics of secretion of acid phosphatase versus the colocalized glycosidase enzymes suggests that an undefined mechanism operates to distinguish these classes of enzymes at a step after localization to lysosomes but prior to secretion.

Acid Phosphatase↗
PubMed1996

Value of acid phosphatase in screening for carcinoma in patients with prostatism in Nigeria.

Analyses of total and prostatic acid phosphatase levels in patients undergoing prostatectomy at Iyi-Enu Hospital, Ogidi, Nigeria between June, 1989 and May, 1992 showed the following: total acid phosphatase sensitivity 72%; specificity 27%; predictive value 28% and while prostatic acid phosphatase sensitivity 72%; specificity 41%; predictive value 50%. While the prostatic acid phosphatase is better than total acid phosphatase both suffer from unacceptably low specificity and high rate of false positives. The clinical value is therefore poor and decision on surgery should be made on other parameter, especially rectal examination.

Acid Phosphatase↗
PubMed1981

Effectiveness of radioimmunoassay of human prostate-specific acid phosphatase in the diagnosis and follow-up of therapy in prostatic carcinoma.

The radioimmunoassay of human prostate-specific acid phosphatase and the measurement of the catalytic activity of acid phosphatase using p-nitrophenyl phosphate as substrate were compared in the diagnosis and follow-up of therapy of prostatic cancer patients. We monitored 17 patients without metastases and eight patients with metastases for 12 months. We detected elevation of the catalytic activity of acid phosphatase [the upper limit for the reference range was mean + 2 (S.D.)] in 24% of the sera of all these patients (n = 25), and the concentration of prostate-specific acid phosphatase measured by radioimmunoassay [the upper limit for the reference range was mean + 3 (S.D.)] was elevated in 80% of these samples before therapy. The radioimmunological measurement of prostate-specific acid phosphatase was therefore more efficient in detecting prostatic cancer than was measurement of the catalytic activity. Favorable effects of the various forms of endocrine treatment were detected more clearly by the measurement of immunoassayable prostatic acid phosphatase than by the measurement of catalytic activity. Activation of the disease during various forms of endocrine treatment of prostatic carcinoma is possibly more efficiently signaled by radioimmunoassay than by measurement of catalytic activity.

Acid Phosphatase↗
PubMed1999

Clinical significance of immunoassays for type-5 tartrate-resistant acid phosphatase.

BACKGROUND: Tartrate-resistant acid phosphatase (TRAP; EC 3.1.3.2) is a product of osteoclasts and a biochemical marker of bone resorption rate. However, erythrocytes and platelets contribute to total TRAP activity in serum, reducing the specificity of direct biochemical assays in serum. Osteoclast TRAP is also known as type-5 TRAP and is antigenically unique. Immunoassays are sought to improve the specificity and sensitivity of TRAP as a bone marker. METHODS: We developed two colorimetric microplate assays for type-5 TRAP: an enzyme capture immunoassay to measure antibody-bound enzymatic activity, and a two-site immunoassay to measure bound enzyme protein. Both use the same monoclonal antibody (14G6) to capture type-5 TRAP, which permits determination of specific activity of serum TRAP in health and disease. RESULTS: Both TRAP assays were linear from one-tenth to fivefold the mean value in 18 healthy subjects. In these subjects, the mean (SD) TRAP activity was 3.2 (0.54) U/L for the enzyme capture assay and 37 (13) microg/L for the two-site assay. Mean TRAP activity was not significantly increased in 64 patients with endstage renal disease requiring hemodialysis (HD) or 99 unselected patients with rheumatic diseases. By contrast, TRAP protein was increased in both the HD and rheumatic disease groups. The specific activity of TRAP in the 17 of 64 HD sera that had increased TRAP activity (0.088 U/microg) was similar to that in healthy subjects (0.091 U/microg). By contrast, the specific activity of TRAP in the 31 of 99 rheumatic sera with increased TRAP protein (0.035 U/microg) was significantly decreased. CONCLUSIONS: Wide sample distributions for TRAP activity in HD patients and TRAP protein in rheumatic disease patients suggest the presence of subpopulations of HD patients with increased TRAP activity and of rheumatic patients with increased TRAP protein. Each assay for TRAP activity and protein may have its own biological significance and clinical applications in specific groups of patients.

Acid Phosphatase↗
PubMed1987

Biosynthesis and secretion of acid phosphatase by Leishmania donovani promastigotes.

Metabolic labeling and immunoprecipitation experiments demonstrated that soluble acid phosphatase (EC 3.1.3.2) was rapidly synthesized and released into culture medium by Leishmania donovani promastigotes. The kinetics of release indicated a constitutive secretory process (t 1/2 = 45 min). Moreover, acid phosphatase was the major secretory protein. The extracellular enzyme is composed of two heterodisperse bands of approximately 110 and 130 kDa in sodium dodecyl sulphate-polyacrylamide gels. It is synthesized as two intracellular precursors of 92.5 and 107 kDa which acquire the heterodisperse form characteristic of the mature extracellular enzyme during biosynthesis. Labeling in the presence of tunicamycin altered the electrophoretic mobility of the acid phosphatase, indicating the presence of several N-linked oligosaccharides on the mature enzyme. However, tunicamycin did not block secretion of the enzyme or its processing to the heterodisperse form. The biosynthetic effect of tunicamycin was mimicked by N-glycosidase F treatment of acid phosphatase immunoprecipitates. In contrast to tunicamycin, labeling in the presence of monensin inhibited processing of the phosphatase to its heterodisperse form. This indicates that Golgi processing, probably glycosylation, is responsible for the heterodispersity of the mature enzyme in sodium dodecyl sulphate-polyacrylamide gels. As with tunicamycin, monensin treatment did not prevent secretion of the acid phosphatase. These cumulative results demonstrate that release of this enzyme by L. donovani promastigotes occurs via a secretory pathway.

Acid Phosphatase↗
PubMed1981

Histochemical tracing of lysosomal enzymes. Improved preparation technique for acid phosphatase, beta-glucuronidase, acid-beta-galactosidase, and arylesterase in rat liver.

The efficiency of the membrane methods of Meijer (1972) and Lojda (1973) in histochemical lysosome tracing was studied and compared with the results of a preparation technique developed by us, employing fresh-frozen celloidin-coated sections; in addition, these methods were compared with results obtained with conventional formalin-sucrose-fixed livers. The lysosomes were traced by reactions for ACPase, beta-glucuronidase, arylesterase and acid-beta-galactosidase activity in rat livers systematically harvested at different time points of occurence of their maximal and minimal activities during the 24-h period, thus indicating a heterogeneity of lysosomes. 3. Optimal results with respect to the morphological appearance of lysosomes were obtained in fresh-frozen celloidin coated sections. This preparation method also caused no enzyme inhibition or loss, thus delivering comparatively the strongest reactions in livers and in enzyme models. 4. Day-time-dependent extralysosomal enzyme activities regularly occur in hepatocytes. Extralysosomal localizations however, are not a consequence of technically induced enzyme diffusion; they are best visualized in celloidin-coated sections; the membrane method produces less satisfactory results, and formalin-sucrose-fixed livers were least satisfactory.

Acid Phosphatase↗
PubMed1984

Regulation of repressible acid phosphatase by cyclic AMP in Saccharomyces cerevisiae.

One of the cyr 1 mutants (cyr 1-2) in yeast produced low levels of adenylate cyclase and cyclic AMP at 25 degrees and was unable to derepress acid phosphatase. Addition of cyclic AMP to the cyr1-2 cultures elevated the level of repressible acid phosphatase activity. The bcy1 mutation, which suppresses the cyr1-2 mutation by allowing activity of a cyclic AMP-independent protein kinase, also allows acid phosphatase synthesis without restoring adenylate cyclase activity. The CYR3 mutant had structurally altered cyclic AMP-dependent protein kinase and was unable to derepress acid phosphatase. The cyr1 locus was different from pho2, pho4 and pho81, which were known to regulate acid phosphatase synthesis. Mutants carrying cyr1-2 and pho80, PHO81c, PHO82 or pho85 mutations, which confer constitutive synthesis of repressible acid phosphatase, produced acid phosphatase. The cyr1-2 mutant produced significantly low levels of invertase and alpha-D-glucosidase. These results indicated that cyclic AMP-dependent protein kinase exerts its function in the synthesis of repressible acid phosphatase and other enzymes.

Acid Phosphatase↗
PubMed1989

Decrease of acid phosphatase activity in murine peritoneal macrophages infected with Leishmania donovani.

The effect of infection with Leishmania donovani on the activity and isoenzyme composition of acid phosphatase within individual murine peritoneal macrophages maintained in vitro was studied. Concentrations of acid phosphatase activity and number of intracellular parasites were quantitated using a computer-assisted cytospectrophotometry system. Changes in the isoenzyme composition of macrophages during infection with L. donovani were detected by comparing the patterns of acid phosphatase levels between macrophages treated in the absence and presence of an enzyme inhibitor. It was observed that the concentration levels of acid phosphatase activity in macrophages were decreased significantly by infection with L. donovani. An inverse relation existed between concentration of acid phosphatase activity and the number of intracellular L. donovani. Reduced concentrations of acid phosphatase activity were also observed in macrophages uninfected but exposed to L. donovani. The isoenzyme composition in macrophages did not change during the course of infection with L. donovani. These results demonstrate that L. donovani reduces the acid phosphatase activity of macrophages.

Acid Phosphatase↗
PubMed1987

Native blot and immunotransfer of human prostatic acid phosphatase isozymes.

Agarose gel isoelectrofocusing is used to separate the isozymes of human prostatic acid phosphatase with retention of enzyme activity. The native blotting of the isozymes onto a nitrocellulose membrane increases the sensitivity of the enzyme stain and is suitable for analysis of isozymes in prostate tissue, which contains little nonprostatic acid phosphatase. The specificity of the transfer is increased by treating the membrane with antibody to human prostatic acid phosphatase prior to the transfer. The specificity of the antibody is conferred to the membrane resulting in a transfer specific for prostatic acid phosphatase. The immunotransfer procedure is applicable to serum which contains appreciable amounts of nonprostatic acid phosphatase.

Acid Phosphatase↗
PubMedDate not supplied

Abnormal serum alkaline and acid phosphatase isoenzymes in female breast cancer patients.

Serum total, different isoforms of both alkaline and acid phosphatases, liver function enzymes, calcium, inorganic phosphate, heamatocrit, white blood cells and platelet counts were determined in 50 female patients suffering from breast cancer. The serum total alkaline and total acid phosphatases within the breast cancer group were variable with significant elevation of both enzymes compared with the corresponding control values. The activities of alanine and aspartate transferases were higher than the control values, while the decreases in serum albumin and heamatocrit were statistically significant. In the breast cancer patients, the increases in the activities of both heat and urea labile alkaline phosphatases were significant. Similarly, in the patients, the tartrate-labile acid phosphatases activity was significantly elevated while the difference in tartrate resistant activity was not significant. In 9 patients (18%), both total alkaline and acid phosphatases were excessively raised when compared with the control. The increased activities of urea-labile and heat-labile alkaline phosphatases as well as tartrate-resistant acid phosphatases are suggestive of increased activities of osteoclast and osteoblasts associated with bone metastasis. A possible diagnostic importance of this observation deserves further investigation, using monoclonal antibody techniques.

Acid Phosphatase↗
PubMed2003

Multiple tissue-specific promoters control expression of the murine tartrate-resistant acid phosphatase gene.

Tartrate-resistant acid phosphatase (TRAP) is highly expressed in osteoclasts and in a subset of tissue macrophages and dendritic cells. It is expressed at lower levels in the parenchymal cells of the liver, glomerular mesangial cells of the kidney and pancreatic acinar cells. We have identified novel TRAP mRNAs that differ in their 5'-untranslated region (5'-UTR) sequence, but align with the known murine TRAP mRNA from the first base of Exon 2. The novel 5'-UTRs represent alternative first exons located upstream of the known 5'-UTR. A similar genomic structure exists for the human TRAP gene with partial conservation of the exon and promoter sequences. Expression of the most distal 5'-UTR (Exon 1A) is restricted to adult bone and spleen tissue. Exon 1B is expressed primarily in tissues containing TRAP-positive non-haematopoietic cells. The known TRAP 5'-UTR (Exon 1C) is expressed in tissues characteristic of myeloid cell expression. In addition the Exon 1C promoter sequence is shown to comprise distinct transcription start regions, with an osteoclast-specific transcription initiation site identified downstream of a TATA-like element. Macrophages are shown to initiate transcription of the Exon 1C transcript from a purine-rich region located upstream of the osteoclast-specific transcription start point. The distinct expression patterns for each of the TRAP 5'-UTRs suggest that TRAP mRNA expression is regulated by the use of four alternative tissue- and cell-restricted promoters.

5' Untranslated Regions↗
PubMed2006

[Comparison and evaluation of two methods for measuring acid phosphatase activity in seminal plasma].

OBJECTIVE: To compare the routine method and the kit method for the measurement of acid phosphatase activity in seminal plasma, and to explore the possibility of the kit method for routine measurement. METHODS: Seventy-nine seminal plasma samples were assayed by routine method and kit method respectively for acid phosphatase. One sample was detected 10 times for within-run analysis, and an other two were measured by both the methods once a day for 10 days for between-run analysis. Acid phosphatase activities in another 10 seminal plasma samples collected at random were measured immediately or 30 min after dilution by two technicians, respectively. RESULTS: There were significant positive correlations between the acid phosphatase activities measured by routine and kit methods (r = 0.745, P = 0.000). In the within-run assay, the coefficient of variation for the kit method (13.72%) was similar with that for the routine method (10.66%). But in the between-run assay, the coefficients of variation for the kit method (13.8% and 15.49%) were obviously lower than those for the routine method (24.43% and 21.04%). Compared with the acid phosphatase activities in seminal plasma measured immediately after dilution, those measured after 30-min standing were notably lower for either of the methods (P < 0.05). However, there wasnt significant difference in the acid phosphatase activities detected by the routine method between the two technicians (P = 0.165). CONCLUSION: The kit method is superior and preferable to the routine method for the measurement of acid phosphatase in seminal plasma.

Acid Phosphatase↗