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PubMed1982

[Quantitative-cytochemical evaluation of acid phosphatase activity in skin window macrophages (author's transl)].

The acid phosphatase activity (acP) of developing skin window macrophages topically treated with 6-methyl-prednisolone (6-MP) has been evaluated by a quantitative-cytochemical technique (SMP 05/PDP 12-20). The following conclusions can be drawn: 1. The degranulation of migrated monocytes can be inhibited by local application of 0.1 to 10.0 micrograms of 6-MP per skin window lesion. 2. The increase of acP-activity associated with the physiologic transformation of monocytes into macrophages and the concomitant activation of the lysosomal system was clearly inhibited by 0.05 to 10.0 micrograms per skin window lesion. 3. 6-MP alters the morphology of the developing macrophages and alters the intracellular distribution of acP. 4. It can be concluded that 6-MP inhibits the development of monocytogenic macrophages. This effect is observed with amounts of 6-MP which correspond to those obtained by systemic application of 6-MP in usual dosages. The antiphlogistic effect of 6-MP probably is due to a considerable proportion by the direct influence on the inflammatory cells.

Acid Phosphatase↗
PubMed1980

Comparative performance of three radioimmunoassays for prostatic acid phosphatase.

Three commercial radioimmunoassays and one enzymatic assay for prostatic acid phosphatase (PAP) have been tested on 122 patients to determine their relative specificity, sensitivity, and diagnostic value. Each of the three radioimmunoassays was found to have special merits. For distinguishing Stage IV prostatic cancer from normal patients without prostatic disease, the Smith Kline (SKF) and New England Nuclear (NEN) assays provide more significant differences. The SKF test also best distinguishes all stages of prostatic cancer from benign prostatic hyperplasia (BPH), but is inferior to the Malinckrodt (MAL) assay for contrasting Stage IV prostatic cancer from BPH. Values obtained with the NEN assay best distinguish the stages of prostatic cancer. Only with the MAL assay are significantly higher PAP values obtained in patients with metastases to bone than those without positive bone scans. Viewed from the point of sensitivity, the SKF assay proves best at all levels of specificity examined in detecting all stages (I-IV), and Stage IV prostatic cancer. By none of the assays can estrogenized Stage III and IV cancer patients be distinguished from those not on estrogen.

Acid Phosphatase↗
PubMed1990

Comparative study of the sensitivity and specificity of the zinc and acid phosphatase spot tests for the detection of seminal stains.

The sensitivity and specificity of a zinc spot test for the detection of semen were compared with those of an acid phosphatase detection method. As screening techniques both tests were found to be very sensitive, but the zinc test was more specific and was more reliable in older and especially in deteriorated specimens. It is concluded that the zinc spot test deserves at least the same place as the acid phosphatase test in the primary investigation of suspected semen stains and might well be the test of choice in older and poorly preserved stains.

Acid Phosphatase↗
PubMed1986

Alteration of acid phosphatase isoenzyme in a human prostatic cancer cell line.

The acid phosphatase (AcP) isoenzyme in a human prostatic cancer cell line was compared to that of prostatic tissue extract by electrophoresis. The major isoenzyme by prostatic tissue extract is the AcP isoenzyme 2, while only AcP isoenzyme 4 (AcP-4) was observed in the human prostatic cancer cell line. A monoclonal antibody specific to AcP-4 was used to investigate the ultrastructural distribution of AcP-4 in a prostatic cancer cell line. The peroxidase staining pattern indicates that AcP-4 is synthesized on bound ribosomes, discharged into the cisternae of rough endoplasmic reticulum, transported to the cisternae of Golgi apparatus for concentration and packaging, and transferred to the secretory vesicles for exocytosis. It is well known that synthesis and secretion of AcP-2 are the major characteristics of the highly differentiated prostatic epithelial cells. The present data demonstrate the loss of this specific function in the prostatic cancer cell line. Instead of AcP-2, the dedifferentiated cancer cell line synthesizes and secretes AcP-4, which is a common AcP isoenzyme of many nonprostatic tissues.

Acid Phosphatase↗
PubMed1989

Lysosomal acid phosphatase is transported to lysosomes via the cell surface.

Lysosomal acid phosphatase (LAP) is transported as a transmembrane protein to dense lysosomes. The pathway of LAP to lysosomes includes the passage through the plasma membrane. LAP is transported from the trans-Golgi to the cell surface with a half-time of less than 10 min. Cell surface LAP is rapidly internalized. Most of the internalized LAP is transported back to the cell surface. On average, each LAP molecule cycles greater than 15 times between the cell surface and the endosomes before it is transferred to dense lysosomes. At equilibrium approximately 4 times more LAP precursor is present in endosomes than at the cell surface. Exposing cells to reduced temperature or weak bases such as NH4Cl, chloroquine and primaquine decreases the steady-state concentration of LAP at the cell surface. The recycling pathway is operative at greater than or equal to 20 degrees C and does not include passage of the Golgi/trans-Golgi network. LAP is transferred with a half-time of 5-6 h from the plasma membrane/endosome pool to dense lysosomes, from where it does not recycle to the endosome/plasma membrane pool at a measurable rate.

Acid Phosphatase↗
PubMed1982

Monoclonal antibodies to human prostatic acid phosphatase: probes for antigenic study.

Hybrid cell lines producing monoclonal antibodies against human prostatic acid phosphatase [PAPase; orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) were prepared by the fusion of mouse myeloma cells with the spleen cells of PAPase-immunized BALB/c mice. Approximately 23% of the hybrid cells initially plated after cell fusion produced specific antibodies: 34 microcultures were cloned, and 8 eventually yielded stable cell lines. The monoclonal antibodies produced by these eight hybridomas were characterized for their isotypes, isoelectric points, concentrations, and affinities. All of the eight monoclonal antibodies exhibited strict specificity for PAPase as determined by radioimmunoassay and immunohistochemical methods. These antibodies were used as probes for the antigenic mapping of this enzyme, and three nonoverlapping determinants were recognized. Further binding studies with PAPase fragments, generated by cleavage with a submaxillaris protease, showed that those three determinants are clustered on one fragment of PAPase. These monoclonal antibodies may be useful in refinement of clinical immunoassays of PAPase or immunohistological study of PAPase-synthesizing cells.

Acid Phosphatase↗
PubMed1987

[Evaluation of a monoclonal antibody-based enzyme immunoassay (IQ(Bio) PAP-AELIA kit) for prostatic acid phosphatase].

The clinical application of enzyme immunoassay (EIA) for prostatic acid phosphatase (PAP) is reported. PAP concentration was measured by an IQ(Bio)PAP-AELIA kit. Serum samples were collected from 20 healthy individuals, 31 patients with benign prostatic hypertrophy, 14 patients with prostatis, 23 patients (47 samples) with prostatic cancer and 29 patients with various other malignancies. The coefficients of variation (%CV) in intraassay and interassay ranged from 2.3 to 4.4%, and from 3.0 to 3.6%, respectively. The recovery rate in the dilution test and recovery test were 106.2 +/- 8.9% and 101.3 +/- 6.9% respectively. A significant correlation (r = 0.994, p less than 0.01) was observed between EIA and RIA methods in the prostatic cancer patients. PAP concentration was elevated above 2.0 ng/ml in 0/2 (0%) of the treated patients with stage B prostatic cancer, 1/5 (20%) of those with stage C, 6/16 (38%) of those with stage D, and in 4/5 (80%) of the untreated patients with stage D prostatic cancer. False positive results were seen in 2/31 (6%) of the patients with benign prostatic hypertrophy, 3/14 (21%) with prostatis and 3/29 (10%) of the patients with various other malignancies. In the majority of the false positive cases, elevated levels were only just above the normal value. In conclusion, the PAP level measured by this EIA kit was correlated with the clinical response to hormone therapy for prostatic cancer.

Acid Phosphatase↗
PubMed1998

Extralysosomal localisation of acid phosphatase in the rat kidney.

There is strong evidence that acid phosphatase (AcPase) plays an important role in the catabolism of the glomerular basement membrane (GBM) and the removal of macromolecular debris resulting from ultrafiltration. Recent enzyme histochemical investigations provide new evidence of the antithrombotic and anti-inflammatory function of ADPase and on the distribution of AcPase in mouse kidney tubule cells. By means of 3 mM cerium as the trapping agent and 1 mM p-nitrophenyl phosphate as the substrate, extralysosomal AcPase could be demonstrated at the ultrastructural level. Following a mild perfusion fixation (2% formaldehyde + 0.07% glutaraldehyde), an effective postfixation and short enzyme incubations (20 min) with microwave irradiation, highly specific enzyme histochemical reaction product and reasonable structural preservation were obtained. Extralysosomal, membrane-bound AcPase was observed along the endoplasmic reticulum, the trans-Golgi cisternae, the nuclear envelope, basal infoldings of the proximal and distal tubular cells and on glomerular profiles, e.g. cell membranes of podocytes, endothelium and basement membrane. Large amounts of extralysosomal AcPase were observed in the basement membrane of glomeruli, in contrast to no AcPase activity in the tubular and mesangial basement membrane. The observed difference in AcPase activity in the tubular epithelial basement membrane and the GBM supports the idea that AcPase in GBM specifically serves in the clearance of macromolecular debris to facilitate ultrafiltration. In the GBM a laminar distribution is observed, suggesting that both epithelial and endothelial cells are involved in the production of AcPase.

Acid Phosphatase↗
PubMed2002

Association of the acid phosphatase (ACP1) gene with triglyceride levels in obese women.

The acid phosphatase (ACP1) locus codes for a low molecular weight protein tyrosine phosphatase (LMPTP) that is found ubiquitously in human tissues. The *A allele of the ACP1 gene is associated with lower total enzymatic activity than the *B and *C alleles. An association between the *A allele and extreme values of body-mass-index (BMI) and dyslipidemia has previously been described in several samples of obese subjects from the Italian population. In the present study, we investigated the relationship between ACP1 *A allele genotypes (*A/*A, *A/*B, and *A/*C) and non-*A allele genotypes (*B/*B, *B/*C, and *C/*C) and metabolic variables in 277 Caucasian post-menopausal subjects consisting of 82 non-obese subjects (BMI</=29), 60 moderately obese (BMI 30-34) and 135 very obese (BMI>/=35) subjects. ACP1 genotypes were found to be significantly associated with total cholesterol (p</=0.002) and triglyceride (p</=0.001) levels in the obese and very obese women only. The significantly lower levels of triglycerides in *A carriers in this group suggest a protective effect of the *A allele against hypertriglyceridemia. It has been unclear why some individuals who gain weight develop dyslipidemia and other aspects of the metabolic syndrome while others do not. The present study suggests that those who gain weight and carry the ACP1 *A allele may be partially protected against developing the metabolic syndrome. The confirmation of ACP1 as a modifier gene of the metabolic complications could open the door to the prevention of the lethal complications of obesity.

Acid Phosphatase↗
PubMed1995

The distribution of cathepsin D in two types of lysosomal or endosomal profiles of rat hepatocytes as revealed by combined immunocytochemistry and acid phosphatase enzyme cytochemistry.

In the electron micrographs of rat hepatocytes, acid phosphatase (ACPase)-positive profiles were classified as either round or elongate types by image analysis, according to a shape index. The former is typical of spherical lysosomes, and the latter are presumed to be the same structures that we have previously termed nematolysosomes. The localization of cathepsin D in these two types of ACPase-positive profiles was electron microscopically examined by a combination of enzyme cytochemistry for ACPase and postembedding immunocytochemistry for cathepsin D. Gold particles showing antigenic sites for cathepsin D were largely present in ACPase-positive structures, although the labeling intensity of gold particles varied with individual sectional profiles of these structures. Quantitative analysis of the labeling density in the two types of ACPase-positive profiles revealed that the amount of cathepsin D in the elongate-type population was smaller than that in the round-type one. This result suggests that the contents of most elongate ACPase-positive structures are different from those of spherical lysosomes and may be similar to those of endosomes. It was also frequently observed that some of the elongate ACPase-positive profiles labeled with few or no gold particles were fused with round profiles which were heavily labeled with gold particles for cathepsin D. It is possible that such fused profiles may be sites for junctions of the two different transport pathways for ACPase and cathepsin D being delivered to lysosomes. Finally, these elongate ACPase-positive structures seem to be equivalent to late endosomes or a different kind of lysosomes containing lower concentrations of hydrolases.

Acid Phosphatase↗
PubMed1987

Zymograms of Kurloff cell acid phosphatases. Thin layer isoelectric focusing and native polyacrylamide 4-15% gradient gel electrophoresis.

Following previous light and ultrastructural cytochemical reports, this paper presents the first zymograms of Kurloff cell acid phosphatases extracted from highly purified cell suspensions. Using isoelectric focusing, up to 20 isoenzymes were observed both with hexazotised pararosanilin or fast garnet GBC as coupler and naphthol ASB1 phosphate as substrate. Most were tartrate-labile. After Clostridium-derived neuraminidase digestion, the highly stained bands observed at pH 4-5 disappeared and, simultaneously, a few alkaline bands were enhanced. Two main bands of Mr 190,000 and 500,000 were characterized by their acid phosphatase activity after electrophoresis on a 4-15% gradient native polyacrylamide gel.

Acid Phosphatase↗
PubMed1996

Cloning and characterization of the human tartrate-resistant acid phosphatase (TRAP) gene.

The expression and protein structure of the tartrate-resistant acid phosphatase (TRAP), an iron-containing lysosomal glycoprotein in cells of the mononuclear phagocyte system, have been analyzed extensively in the past. In some diseases, like hairy cell leukemia and Gaucher's disease, cytochemically detected TRAP expression is used as a disease-associated marker. In this paper we describe the isolation of a genomic cosmid clone of the human TRAP gene. Restriction mapping revealed a 22-kb insert and the complete genomic structure of the TRAP gene. A 6-kb HindIII-fragment harboring the entire TRAP gene was subcloned and the 5'-flanking region of 3026 bp was sequenced. Analysis of the sequence data showed the presence of potential transcription factor binding sites. Two transcriptional start sites were identified in the untranslated exon 1 at positions -349 and -347 bp relative to the translational start codon. Linked to a luciferase-encoding reporter gene the 5'-flanking region was sufficient to direct transcription in the heterologous cell line BHK-21. Treatment of the transfected cells with different modulators of the intracellular iron content showed that regulation of TRAP expression is dependent on iron. In summary, these data imply a possible functional role of the TRAP gene product either in the storage or the transport of iron.

Acid Phosphatase↗
PubMed1993

Overexpression of uteroferrin, a lysosomal acid phosphatase found in porcine uterine secretions, results in its high rate of secretion from transfected fibroblasts.

Lysosomal enzymes can, under certain circumstances, be secreted in large amounts. One example is uteroferrin (Uf), an iron-containing, purple-colored acid phosphatase secreted by the uterus of the pig during pregnancy. Uf is identical to the intracellular tartrate-resistant acid phosphatase of pig spleen, yet is the major protein component of uterine secretions. To investigate possible regulatory mechanisms that might direct Uf along a secretory pathway, we expressed Uf in Chinese hamster ovary (CHO) cells under the control of the SV40 early promoter using an expression construct, pX/Uf. The proportion of Uf secreted into the medium relative to the amount retained intracellularly increased as total Uf expression was increased. At transfection doses of 15 micrograms pX/Uf per 10(6) cells, over 80% of the Uf produced in 48 h was secreted. A parallel situation was observed when human cathepsin D was overexpressed in CHO cells. Thus, high production of Uf, as occurs in the uterus in response to progesterone, may overwhelm the intracellular enzymatic and receptor systems that are normally employed to target acid hydrolases to lysosomes, resulting in secretion. Both Uf and cathepsin D secreted by CHO cells possess N-linked, phosphorylated high-mannose oligosaccharide chains. However, the phosphate groups on the oligosaccharide chains of Uf, unlike those on cathepsin D, cannot be readily removed by alkaline phosphatase treatment. These results suggest that the phosphate groups on Uf are masked at least partially by covering N-acetylglucosamine residues and that two mechanisms may contribute to hypersecretion of Uf in the uterus: 1) very high rates of synthesis and 2) partial masking of the mannose 6-phosphate recognition signal.

Acid Phosphatase↗
PubMed2000

Molecular characterization of a novel yeast cell-wall acid phosphatase cloned from Kluyveromyces marxianus.

A novel Kluyveromyces marxianus gene that encodes an acid phosphatase, Pho610, was cloned in Saccharomyces cerevisiae. The deduced amino acid sequence was distinct from S. cerevisiae phosphatases but similar to some fungal enzymes. A peculiar feature of the sequence is that it has hydrophobic stretches both at the N- and C-termini, which is a characteristic of the precursors of glycosylphosphatidylinositol(GPI)-anchored proteins. When the gene was expressed in S. cerevisiae, the active enzyme was recovered in the periplasmic fraction by glucanase digestion. The Pho610 polypeptide was highly glycosylated and a significant portion was covalently linked to the cell-wall glucan. The enzyme was secreted when the C-terminal region was truncated to remove the GPI signal. Therefore, Pho610 is a novel cell-wall protein having an enzyme activity.

Acid Phosphatase↗
PubMed1990

[Ultrastructural localization of myelin bodies and acid phosphatase activities in the liver and kidney induced by quinacrine in rats].

Electron microscopic studies were conducted to reveal the ultrastructural aspects of the myelin body and acid phosphatase activity in rats induced by quinacrine, an antimalarial drug. Each of 22 rats in three groups were examined. The first group of control rats was initially given a single i.p. dose (200 mg/kg) of diethylnitrosamine (DEN) only and then fed a CRF-1 basal diet for 8 weeks. The second and third group were treated with DEN or saline, and starting 2 weeks later, were fed a CRF-1 basal diet supplemented with 500 ppm quinacrine for 6 weeks. All animals were subjected to a partial hepatectomy at week 3, and then sacrificed at week 8. Liver and kidney tissues specimens from 2 rats per group were collected for routine electron microscopic study. Furthermore, the activity of acid phosphatase, a key enzyme for lysosomal activity, was also investigated. In this study, tissues were fixed with a solution of 2.5% glutaraldehyde in 0.1 M sodium cacodylate buffer. After fixation, tissues were frozen and their 8 microns sections were treated with Gomori's lead nitrate buffer solution, and post-fixed with a 1% osmium solution. After being embedded in Epon 812, ultrathin sections were made. Intracellular myelin bodies were observed in the hepatocytes, interlobular bile duct cells, renal glomerular podocytes and renal tubular cells in the quinacrine treated groups, but not were observed in rats treated with DEN alone.(ABSTRACT TRUNCATED AT 250 WORDS)

Acid Phosphatase↗
PubMed1984

Comparison of p30 and acid phosphatase levels in post-coital vaginal swabs from donor and casework studies.

The application of p30 detection to casework analysis of seminal traces on vaginal swabs is reported and compared with the levels of acid phosphatase determined. A simple crossed-over immunoelectrophoresis system was used for batch identification of swab extracts using a commercially obtained anti-p30 serum. Positive p30 results were obtained in less than 20% of the casework swab extracts, but they provide conclusive proof of the presence of semen which is a substantial advantage over the quantitative determination of acid phosphatase.

Acid Phosphatase↗
PubMedDate not supplied

[Formation of secreted acid phosphatase during the growth of Saccharomyces cerevisiae yeasts on different sources of carbon and nitrogen nutrition].

The effect of certain components in the growth medium on the secretion of acid phosphatase was studied with Saccharomyces cerevisiae. The presence of phosphate at a concentration of 10 mM in the medium inhibited the formation of repressible forms of this enzyme. The synthesis of the secreted enzyme depended on the sources of carbon and nitrogen nutrition. The enzyme yield was highest in a medium with sucrose as a carbon source and ammonium chloride as a nitrogen source. The secretion of acid phosphatase is stimulated by an increase in the sugar content and a deficiency of the nitrogen source in the medium.

Acid Phosphatase↗