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PubMed1989

Correlation between alkaline and acid phosphatase activities and age-related osteopenia in murine vertebrae.

Lumbar vertebrae (L4) from CW-1 female mice were examined for age-related changes in alkaline and acid phosphatase activities from young to old age. Histochemically, both enzymes were encountered along the bony surfaces of both trabecular and cortical bones with no significant age-related changes in their distribution. Biochemical determinations of bone alkaline phosphatase (Alk'ase) activity revealed that for a given unit level of bone or the bone as a whole no significant changes took place, whereas acid phosphatase (Acid'ase) activity was found to have increased significantly with age. A high positive correlative relationship was noted between the calcium content and the trabecular bone volume of the same vertebrae. It may, therefore, be proposed that age-related bone loss in mice could be attributed to an enhanced resorption rather than to a substantial reduction in the formative potential of bone cells.

Acid Phosphatase↗
PubMed1976

A comparative study of histochemical mapping on the distribution of acid phosphatase and 5-nucleotidase in the forebrain of frog (Rana tigrina).

The four well defined dorsal, lateral, medial and intermediate olfactory tracts of the frog have been studied. During their courses they become intermingled with fibers related to the primordial septum, the primordial hippocampus, the primordial dorsal pallium and the primordial piriform areas. In acid phosphatase preparations all these tracts are completely negative, and, therefore, are not identifiable. However, these tracts have intense staining reaction to 5-nucleotidase throughout their courses. Differences in the distribution of acid phosphatase and 5-nucleotidase are apparent in the hippocampal and anterior commissures. These are negative for acid phosphatase. In 5-nucleotidase preparations the anterior commissure has an intensely positive whereas the hippocampal commissure has a completely negative reaction. The medial septal nucleus is intensely positive for 5-nucleotidase at the anterior hemisphere level. There is a gradual decrease in intensity of staining in this nucleus towards the posterior hemisphere levels so that in the last few sections of the forebrain of the frog the medial septal nucleus is completely unstained or negative. In the acid phosphatase preparations at all levels the medial septal nucleus presents a moderately positive reaction. In 5-nucleotidase preparations, the dorsomedial part of primordial hippocampus is intensely positive whereas the dorsal part of the hippocampus is completely negative. In acid phosphatase preparations, both dorsal and dorsomedial parts of hippocampus are intensely positive. The striatal complex and the lateral septal nucleus are positive for acid phosphatase and negative for 5-nucleotidase. The possible significance of some of these similarities and differences in tracts and nuclei has been considered with reference to the functioning of the various parts. The present histoenzymological preparations have revealed distinct nerve pathways. In some instances clear-cut connections, which had hitherto been unrevealed by neuroanotomical methods, have been demonstrated.

Acid Phosphatase↗
PubMed1993

Cationic liposome-mediated incorporation of prostatic acid phosphatase protein into human prostate carcinoma cells.

Lipofectin, the commercially available cationic liposome, was used to introduce the purified prostatic acid phosphatase protein into the established human prostate carcinoma cells. The incorporated phosphatase protein which retained its enzymatic activity as demonstrated by the tartrate-sensitive acid phosphatase assay was localized in the cytoplasm by immunofluorescence staining. Further, cells that were treated with phosphatase/Lipofectin complexes expressed a decreased phosphotyrosine level, presumably due to the endogenous protein tyrosine phosphatase activity of the acid phosphatase protein. A cationic liposome such as lipofectin may thus be employed to mediate transport of other acidic proteins into cells, providing a way to examine their biological functions in vivo.

Acid Phosphatase↗
PubMed1979

Ultracytochemical characterization of non-specific acid phosphatase activities in Saccharomyces cerevisiae.

Glutaraldehyde prefixation causes a considerable inactivation of the acid phosphatase of yeast protoplasts in dependence on the duration of aldehyde influence. Lead ions necessary for ultracytochemical demonstration effect a still stronger inhibition of enzymatic activity. Prefixation, however, protects the enzyme from further inhibition by lead. At pH 4.4 in intact cells acid phosphatase activities are mainly localized in the periplasmic space and in vesicles fused with the plasma membrane. The cell wall and cytoplasm usually remain free of reaction products. On the cell surface activities are found in form of globular lead deposits. At pH 5.2 and 6.3 the periplasmic activity appears decreased compared to that at lower pH values and the intracellular activity is increased. The plasma membrane of protoplasts is completely free of precipitates. The intracellular activity sites of protoplasts (cisternae of endoplasmic reticulum and/or Golgi-like system, small vesicles, central vacuole, nuclear envelope) are the same as for intact cells. The occurrence of at least two forms of acid phosphatase in S. cerevisiae id deduced.

Acid Phosphatase↗
PubMed1986

The association of distinct acid phosphatases with the flagella pocket and surface membrane fractions obtained from bloodstream forms of Trypanosoma rhodesiense.

Cell fractionation of bloodstream Trypanosoma rhodesiense, using isopycnic sucrose gradient centrifugation, reveals acid phosphatase activities against a range of substrates to be associated, to varying degrees, with subcellular particle populations identified as derived from flagella pocket membrane and surface membrane. Using these same substrates (alpha and beta glycerophosphate, p-nitrophenyl phosphate and glucose-6-phosphate) at least two distinct acid phosphatase activities can be distinguished. One is thermolabile (approximately 80% inactivated after 30 min. at 60 degrees C), sensitive to tartrate (50% inhibited at 1.8 mM Na tartrate) with a pH optimum approximately 4.5 and appears to exhibit little substrate preference. The other acid phosphatase is relatively heat stable (approximately 30% inactivated), insensitive to tartrate (greater than 5.0% inhibited using 1.8 mM Na tartrate) exhibits a somewhat higher pH optimum (approximately 6.0) and is more substrate specific (6X more active toward glucose-6-PO4 than beta-glycerophosphate). Further cell fractionation experiments reveal 85% of the tartrate sensitive acid phosphatase to be associated with flagella pocket membrane and to account for 80% of the organisms hydrolytic activity toward beta-glycerophosphate. The tartrate resistant acid phosphatase however, has a much less exclusive localization being almost equally distributed between surface membrane (40%) and flagella pocket membrane (60%).

Acid Phosphatase↗
PubMed1985

Lens epithelium and radiation cataract. V. Observations on acid phosphatase and meridional row nuclear fragmentation.

The influence of X-radiation on acid phosphatase activity in differentiating meridional row cells of rat lens epithelia was examined by ultrastructural cytochemistry. X-ray doses of 10-12 Gy (1000-1200 rads) produced clearly observable nuclear and cytoplasmic damage at 13-19 hr postirradiation. In those cells, acid phosphatase reaction product was associated with much of the electron dense material of fragmented nuclei and various parts of the cytoplasm. In addition, many irradiated cells without observable damage were positive for reaction product. The presence of acid phosphatase activity in these otherwise normal-appearing cells is suggestive of more subtle radiation damage than that observed in the more severely damaged cells.

Acid Phosphatase↗
PubMed1984

Tartrate-inhibitable acid phosphatase. Purification from placenta, characterization and subcellular distribution in fibroblasts.

Tartrate-inhibitable acid phosphatase was purified to apparent homogeneity from human placenta. The enzyme is composed of two subunits with an apparent molecular mass of 48 kDa. Each subunit carries one oligosaccharide of the high-mannose/hybride type. The purified enzyme has an isoelectric point of pH 6.2. It cleaves phosphomonoester bonds at acid pH, is competitively inhibited by L-tartrate, Ki = 0.51 microM, and phosphate, Ki = 0.8mM. A monospecific antiserum raised against the purified placental enzyme precipitated 62% and 85% of the tartrate-inhibitable acid phosphatase present in extracts of placenta and fibroblasts, respectively. By means of subcellular fractionation and immunoprecipitation it was shown that the majority of tartrate-inhibitable acid phosphatase is located in lysosomes in normal and mucolipidosis II fibroblasts. In the human Hep G-2 hepatoma cells a significant fraction of the enzyme appears to be associated with non-lysosomal organelles.

Acid Phosphatase↗
PubMed1975

Localization of acid phosphatase in protoplasts from Saccharomyces cerevisiae.

The localization of acid phosphatase (EC 3.1.3.2) in secreting protoplasts prepared from Saccharomyces cerevisiae is reported for the first time. Using a Gomori technique we were able to show acid phosphatase at those organelles in the protoplasts which are generally involved in the processes of biosynthesis and secretion of glycoproteins in eukaryotic cells.

Acid Phosphatase↗
PubMed1987

An isoelectric focusing study of acid phosphatase heterogeneity in rat liver.

The different forms of acid phosphatase (EC 3.1.3.2) in rat liver homogenates, lysosomal, mitochondrial, microsomal fractions and cytosol were studied with isoelectric focusing. Evidence is presented that isoelectric focusing of acid phosphatase in subcellular fractions shows individual changes and time related patterns. Mild autolysis shifted all enzyme activity peaks of isoelectric focusing patterns to the one at pH 7.04.

Acid Phosphatase↗
PubMed1992

Evaluation of the modified zinc test and the acid phosphatase test as preliminary screening methods in sexual assault case material.

The modified zinc test and a commercially available acid phosphatase test were compared as to their screening parameters according to the microscopical finding of spermatozoa in cases of alleged sexual assault. The study involved 65 pieces of evidence material. It was found that the modified zinc test has a higher sensitivity and higher predictive values than the acid phosphatase test. However, when both tests are combined in parallel, the sensitivity and the negative predictive value could be raised to 99%. This finding suggests that a negative result obtained from the parallel combination of the modified zinc test and the acid phosphatase test predicts very well that no spermatozoa will be found at microscopical examination. Since the latter technique is the only one to give absolute proof of the seminal origin of stains or traces, the parallel combination of the zinc test and the acid phosphatase test might be useful in sorting out these cases or materials that deserve further investigation by more elaborate techniques.

Acid Phosphatase↗
PubMed1992

Pre-analytical and biological variability of prostatic acid phosphatase and prostate-specific antigen in serum from patients with prostatic pathology.

We determined the pre-analytical and biological variation of prostatic acid phosphatase and prostate-specific antigen in the same patient samples. Prostatic acid phosphatase and prostate-specific antigen were both stable when stored for at least 3 weeks with acidification (acetate buffer) or without acidification, except for prostate-specific antigen in samples stored unacidified at 4 degrees C. A significant elevation of prostate-specific antigen was noted in four patients with benign prostatic hyperplasia between 1/2 and 6 hours after prostatic massage. No significant effect was shown of changes in the glomerular filtration rate on prostate-specific antigen concentration, in spite of its low molecular mass. The estimate of within-subject biological variation showed a coefficient of variation of 33.8% for prostatic acid phosphatase and 14% for prostate-specific antigen. Desirable analytical imprecisions based on these findings were about 17% for prostatic acid phosphatase and 7% for prostate-specific antigen, these goals being achieved in practice for marker values higher than or equal to the upper reference limit.

Acid Phosphatase↗
PubMed1983

Serum acid phosphatase elevation associated with transurethral resection syndromes.

In 6 patients undergoing transurethral resection of the prostate for benign prostatic hyperplasia symptoms of post-transurethral prostate resection syndrome developed. Serum acid phosphatase determinations in the recovery room showed that all patients had high acid phosphatase levels although each had normal levels preoperatively. All patients showed a normal acid phosphatase level on the first postoperative day. The acid phosphatase elevations indicate significant intraoperative absorption of prostate tissue substances. The association of clinical symptoms with enzyme elevation suggests that the etiology of the confusing clinical syndromes following transurethral prostate surgery may be due to the intravenous absorption of not only irrigant solution but also tissue substances from the prostate gland.

Acid Phosphatase↗
PubMed1974

Human acid phosphatase in somatic cell hybrids.

The human enzyme, lysosomal acid phosphatase ACP2, is expressed in nan-rodent somatic cell hybrids as a dimeric molecule. The human-rodent heteropolymer, as well as the human and rodent homopolymer, is associated with lysosomes in these cells. The genes specifying lysosomal acid phosphatase ACP(2) and LDH A are syntenic.

Acid Phosphatase↗
PubMed1984

Radioimmunoassay (RIA) for prostatic acid phosphatase in patients with prostatic carcinoma.

In recent years radioimmunological measurements of prostatic acid phosphatase have been proposed for the diagnosis, follow-up and prognosis of prostatic carcinoma. The possibility of screening male populations at risk has even been suggested. The present paper deals with the current position of this method. We studied the specificity and sensitivity of the radioimmunoassay (RIA) for prostatic acid phosphatase in three groups of patients: a normal population, patients with benign prostatic hyperplasia, and patients with untreated prostatic carcinoma. The conclusions of this study are that the RIA is a specific method but the sensitivity is much too low to use the RIA for diagnosis and screening of patients. Comparison with the enzymatic method indicates that under good laboratory conditions the latter is preferable except for patients with metastatic disease and normal enzymatic acid phosphatases.

Acid Phosphatase↗
PubMed1993

Acid phosphatase activity in the larval salivary glands of developing Drosophila melanogaster.

Both the biochemical profile and the optical and fine structural localization of acid phosphatase activity in the larval salivary glands of developing Drosophila melanogaster is described. Biochemically, acid phosphatase shows peak activity in the glands of feeding larvae, followed by a marked decline. Directly preceding the onset of cell histolysis however, enzyme activity increases 1.5 fold and is maintained at this level. Histochemically, acid phosphatase activity initially appears as discrete point or lysosomal sources. As development proceeds, an intense and diffuse form of enzyme is seen, accompanying an extremely vacuolated cytoplasm. Ultrastructurally, the enzyme is located in lysosomes, Golgi elements, multivesicular bodies and both within, and on the extracisternal surface of the rough endoplasmic reticulum. This extracisternal or cytosolic form appears directly preceding cell lysis and eventually shows a comprehensive cellular distribution. Large numbers of acid phosphatase positive haemocytes are attached to the basal glandular surface at all developmental stages. In morphologically intact gland cells, discrete extracisternal enzyme activity appears associated with local areas of degradation.

Acid Phosphatase↗
PubMed1993

Histochemical demonstration of acid phosphatase activity in terminal Schwann cells associated with Ruffini endings in the periodontal ligament of rat incisors.

Histochemical staining for acid phosphatase, a marker for lysosomal elements, distinguished rounded, intensely reactive cells from less reactive fibroblasts and osteoblasts in the lingual periodontal ligament. The highly reactive cells were located exclusively in the alveolar half of the ligament. Double staining for acid phosphatase and S-100 protein confirmed that these reactive cells were identical with the terminal Schwann cells associated with periodontal Ruffini endings. Electron microscopically, reaction products for acid phosphatase were observed in the lysosomes and Golgi apparatus in the paranuclear cytoplasm of the terminal Schwann cells. As the terminal Schwann cells associated with the Ruffini endings are assumed to be capable of synthesizing exportable proteins, acid phosphatase in this type of cell may be involved in the processing of macromolecules in synthetic and/or secretory pathways.

Acid Phosphatase↗
PubMed1978

A solid phase radioimmunoassay for prostatic acid phosphatase.

The sensitivity of a recently developed solid phase radioimmunoassay for human prostatic acid phosphatase was compared to that of an enzymatic method using p-nitrophenylphosphate as substrate. In 109 histologically verified untreated stages I to IV prostatic cancers and 200 men without such cancer the solid phase radioimmunoassay method demonstrated substantially greater sensitivity and specificity than the enzymatic technique. In the 109 prostatic malignancies the immunochemical method correctly classified 80 (73 per cent) versus 34 (31 per cent) for the p-nitrophenylphosphate enzymatic technique (p less than 10(-6). In 44 stages I and II cancers confined to the prostate the radioimmunoassay was abnormally elevated in 19 (43 per cent) with only 4 (9.1 per cent) enzymatic elevations (p less than 10(-3). In 65 stages III and IV extraprostatic cancers correct classifications were noted in 61 (94 per cent) of the radioimmunoassays and 30 (46 per cent) enzymatic tests (p less than 10(-6). The radioimmunoassay in 200 male controls yielded 11 (5.6 per cent) and the p-nitrophenylphosphate enzymatic test yielded 7 (3.5 per cent) falsely positive results. In 90 non-prostatic human cancer sera 85 (94.5 per cent) were correctly classified as negative by the radioimmunoassay for prostatic acid phosphatase versus 66 (73 per cent) as negative by the enzymatic method. These data are discussed in terms of the merits of a radioimmunochemical approach for the measurement of human serum prostatic acid phosphatase.

Acid Phosphatase↗