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PubMedDate not supplied

Isoenzymes of alkaline and acid phosphatases as bones metastasis marker in breast cancer patients.

Bone alkaline phosphatase (B-ALP) and tartrate resistant acid phosphatase (TR-ACP) are markers of osteoblastic and osteoclastic activities respectively. During a period of up to two years, these isoenzymes have been assayed in the sera of 191 breast cancer patients; 80 had bone metastases (BM). In BM bearing patients, B-ALP activity was 261 IU/l and 63 IU/l for patients without BM; TR-ACP was respectively 6.6 and 3.3 IU/l. Specificity and sensitivity were calculated according to several criteria. These isoenzyme serum levels were well correlated with those of two breast cancer markers (CEA and CA15.3) and radiograph.

Acid Phosphatase↗
PubMed1986

A deletion that includes the segment coding for the signal peptidase cleavage site delays release of Saccharomyces cerevisiae acid phosphatase from the endoplasmic reticulum.

We studied ultrastructural localization of acid phosphatase in derepressed Saccharomyces cerevisiae cells transformed with a multicopy plasmid carrying either the wild-type PHO5 gene or a PHO5 gene deleted in the region overlapping the signal peptidase cleavage site. Wild-type enzyme was located in the cell wall, as was 50% of the modified protein, which carried high-mannose-sugar chains. The remaining 50% of the protein was active and core glycosylated, and it accumulated in the endoplasmic reticulum cisternae. The signal peptide remained uncleaved in both forms. Cells expressing the modified protein exhibited an exaggerated endoplasmic reticulum with dilated lumen.

Acid Phosphatase↗
PubMed1980

Purification and some properties of the main polymorphic form of acid phosphatase from Poa pratensis seeds.

The main polymorphic form of acid phosphatase was isolated from Poa pratensis seeds by chromatography on DEAE- and CM-cellulose and gel filtration on Bio-Gel P-100. The enzyme migrated as a single band in disc electrophoresis at pH 4.5 and 8.4. The purified enzyme is a glycoprotein of molecular weight about 33 000. Carbohydrate content accounts for 40% of the total weight. The optimum pH is at 5.2 and the apparent Km for p-nitrophenylphosphate, 0.55 mM. Fluoride ions are non-competitive and zinc ions-uncompetitive inhibitors, with the apparent Km values of 0.55 and 0.28 mM, respectively.

Acid Phosphatase↗
PubMed2002

Osteoclasts from mice deficient in tartrate-resistant acid phosphatase have altered ruffled borders and disturbed intracellular vesicular transport.

Tartrate-resistant acid phosphatase (TRAP) is an enzyme highly expressed in osteoclasts (OC) and chondroclasts. As an approach to pinpoint the function of TRAP in bone-resorbing osteoclasts, the morphological phenotypic alterations of bone and osteoclasts in mice with targeted disruption of the TRAP gene were assessed by quantitative histomorphometry and immunocytochemistry at the light microscopic and ultrastructural levels. TRAP-deficient mice display alterations in the epiphyseal growth plates as evidenced by increased height with disorganized columns of chondrocytes, in particular affecting the zone of hypertrophic chondrocytes, consistent with a disturbance of chondrocyte maturation and chondroclastic resorption at the epiphyseal/metaphyseal junction. TRAP -/- mice express an early onset osteopetrotic bone phenotype, apparent already at 4 weeks of age. The differentiation of OCs was apparently normal; however, the osteoclasts in TRAP-deficient mice were less active in terms of degradation or release of the resorption marker C-terminal type I collagen cross-linked peptide, indicative of an intrinsic defect. Ultrastructural morphometry disclosed that OCs from TRAP-deficient young mice exhibited an increased relative area of ruffled borders. Moreover, mutant OC accumulated cytoplasmic vesicles 200-500 nm in size in both ruffled border and basolateral parts of the cytoplasm, reflecting disturbed intracellular transport. The accumulated vesicles were not likely derived from the secretory pathway, since cathepsin K was detected at normal levels in the ruffled border area and matrix in TRAP -/- mice. In summary, the resorptive defect in TRAP-deficient OCs is reflected by a disturbance at the level of ruffled borders and intracellular transport vesicles. Consequently, accumulation of vesicles in the cytoplasm of mutant OCs indicates a novel function for TRAP in modulating intracellular vesicular transport in osteoclasts.

Acid Phosphatase↗
PubMed1994

Histochemical and biochemical studies of the kinetics of non-specific acid phosphatase in rat kidney.

Kinetic characteristics of non-specific acid phosphatase (orthophosphoric monoester phosphohydrolase, E.C.3.1.3.2.) from rat kidney were determined fluorometrically using 4-methylumbelliferyl phosphate as the substrate. Kinetic characteristics measured by similar methods both histochemically in cryostat sections and biochemically in tissue extracts were compared. Histochemical and biochemical methods gave essentially similar results in respect of Michaelis-Menten constants (Km), pH optima, effect of fluoride inhibition and the effect of changes in incubation temperatures in the range 10 degrees C to 37 degrees C. This confirms the validity of both methods, and also gives greater confidence that the enzyme in vitro closely approximates the properties of the enzyme as it functions in vivo.

Acid Phosphatase↗
PubMed1989

Acid phosphatase in lymphoid tissues of developing chick embryos.

Activity of acid phosphatase (ACPase) in bursa and thymus has been determined in developing chick embryos of either normal or treated with bovine serum albumin (BSA). From the study of light microscopical histochemistry, ACPase activity could be detected in cytoplasm. These ACPase activities were detected in both the follicular medulla and cortex in bursa. In thymus, moderate ACPase activities were also obtained in both the cortex and medulla. ACPase activity in the tissue homogenate was increased in the bursa but the thymic ones showed constant level during the incubation days examined in normal embryos. ACPase distribution observed at the distinct developing stage indicates that ACPase is a useful parameter for growth and development of chicken lymphoid tissues.

Acid Phosphatase↗
PubMed1976

Acid phosphatases: androgen dependent markers of rat prostate.

Our investigations on acid phosphatase (AP) were aimed at finding a biochemical assay marker for androgen actions in the rat prostrate. We quantitatively examined the effects of l-tartrate or formaldehyde on AP activity in tissue filtrates from nine adult male rat tissues, plasma and hemolysed red blood cells (HRBC). There was significant inhibition of AP activity in all instances with the exception of HRBC with tartrate. The prostate inhibition results were not different from those for seminal vesicles and adrenals but were different from the other tissues studied. Ten days following castration the inhibition by tartrate was less in all tissues studied except plasma and HRBC; the formaldehyde inhibition percentages were not altered.

Acid Phosphatase↗
PubMed1975

[Properties and isoenzymes of acid phosphatase in erythrocytes and various tissues (kidney, liver, spleen, small intestine mucosa, testis, myocardial and skeletal musculature) of cattle].

The substrate that was split most rapidly by acid phosphatase was p-nitrophenylphosphate. Two peaks of activity were obtained at pH 4.6-4.8 and 5.1-5.4. The enzyme remained stable for a long time when refrigerated. It was inhibited strongly by urea and tartrate, and slightly by fluoride and L-phenylalanine. Mercaptoethanol elicited pronounced activation of the enzyme. Four different forms of isoenzyme, giving rise to 11 phenotypes, were identified. A suitable analytical technique was electrophoresis on polyacrylamide gel with phosphate-citrate buffer. Mean activity was 3.15 +/- 0.41 units per gramme of haemoglobin haemolysate. Some of the isoenzyme preparations showed considerable variation in activity. There was no change in enzyme activity after temporary hypomagnesaemia. Acid phosphatase activity was high in testis, kidney and intestinal mucosa; myocardium, liver and spleen showed moderate activity. Five isoenzymes were demonstrable in a starch column and six in PAA gel.

Acid Phosphatase↗
PubMed1991

Studies on the oligosaccharide heterogeneity of the isoelectric forms of the lower molecular weight acid phosphatase of frog liver.

1. The lower molecular weight, heterogeneous acid phosphatase (AcPase) from the frog liver (Rana esculenta) containing AcPase I, II, III and IV was separated into enzymatically active components by isoelectric focusing in an immobilized pH gradient. 2. The blotted enzyme bands were characterized by their different binding patterns obtained with the lectins concanavalin A, wheat germ agglutinin (WGA), Lens culinaris hemagglutinin (LcH) and peanut agglutinin (PNA). 3. In situ neuraminidase treatment reduced the staining intensity of some WGA-bands and increased that of PNA-bands. 4. The finding that AcPases I, II, III and IV differ in their carbohydrate chain composition, together with previous results showing different bioactivities of AcPases III and IV, indicates a correlation between the glycosylation state of enzyme forms and their physiological action.

Acid Phosphatase↗
PubMed1982

An interaction between human seminal acid phosphatase and Canavalia gladiata DC lectin.

Interactions between human seminal acid phosphatase (AcP) and five kinds of lectins were studied. Seminal plasma was mixed with the lectins at various ratios. The mixtures were centrifuged and the supernatants were assayed for AcP activity. The activity was effectively reduced only with Canavalia gladiata DC (CG) lectin. CG lectin purified by Sephadex G-200 gel filtration was added to two fractions of AcP separated by Sephadex G-200 gel filtration. There was no difference in the rate of reduction of the two fractions. To isolate seminal AcP by affinity chromatography, CG lectin was coupled to agarose gel. AcP bound with the agarose gel could be eluted with alpha-methyl-D-mannoside. Specific activity of the purified AcP was elevated to as much as 54-fold.

Acid Phosphatase↗
PubMed1986

Acid phosphatase activity and intracellular collagen degradation by fibroblasts in vitro.

Human gingival fibroblasts were cultured with collagen fibrils. The precise process of collagen phagocytosis and the relationship between acid phosphatase activity and intracellular degradation of collagen were investigated by cytochemical methods at the ultrastructural level. The collagen fibrils were first engulfed at one end by cellular processes, or the cell membrane wrapped itself around the middle of the fibrils. Collagen phagocytosis induced acid phosphatase activity in the fibroblast Golgi-endoplasmic reticulum-lysosome system. By application of the tracer lanthanum, deposits were observed in the intercellular spaces and along the fibrils being phagocytosed. At this stage, primary lysosomes were seen in close proximity to the collagen being engulfed, but no signs of fusion were observed. When the fibrils had been interiorized in whole or in part, they ultimately became enclosed within phagosomes, and no tracer was observed along the interiorized portion of the fibrils. Primary lysosomes then fused with these collagen-containing phagosomes to form phagolysosomes. Collagen degradation occurred within these bodies even though the end of a fibril might have protruded outside of the cell. These results suggest that selective and controlled phagocytosis of collagen and intracellular digestion of it may play a central role in the physiological remodeling and metabolic breakdown of the collagen of connective tissues.

Acid Phosphatase↗
PubMed1989

Behavior of animal blood in blood typing systems. Isoelectric focusing of erythrocyte acid phosphatase and phosphoglucomutase.

Isoenzyme band patterns of animal blood erythrocyte acid phosphatase (EAP) and phosphoglucomutase-1 (PGM) were studied by isoelectric focusing on ultrathin polyacrylamide gels. For blood from all animals tested (dog, cat, cow, sheep, and goat), the overall band patterns for both isoenzymes were different from those of the most common human types of these enzymes, although some animal EAP and PGM bands appeared in the human band areas. When mixtures of human and animal red blood cells were studied, it was found that misinterpretation of human types was possible only if the overall band pattern of the mixtures was ignored. For the animal blood tested, the strong PGM bands appearing outside the human band areas could be used as "markers" for the possible presence of animal blood in the samples tested.

Acid Phosphatase↗
PubMed1975

Qualitative and quantitative determinations of acid phosphatase activity in vaginal washings.

In the absence of spermatozoa, acid phosphatase activity (ACP) is an indicator of seminal fluid in cases of sexual assault. Both qualitative and quantitative ACP methods are employed by medical examiners. A large series of cases in which a qualitative test was employed is reported. A method for obtaining and handling specimens by vaginal washing was developed. This method provides suitable specimens for the examination for spermatozoa and the determination of ACP. Specimens obtained from 41 women provided examples of endogenous vaginal ACP and intravaginal seminal ACP. These specimens were used to evaluate qualitative and quantitative ACP methods for the detection of seminal ACP. Tartrate inhibition was not useful for separating endogenous vaginal and seminal ACP activities. The advantages of the method developed for specimen acquisition and of quantitative assays for ACP are discussed.

Acid Phosphatase↗
PubMed1986

[Prostatic acid phosphatase and prostatic specific antigen measured by immunoenzyme assay].

Prostatic acid phosphatase (PAP) and prostatic specific antigen (PA) were determined with a Cetus test kit (California, USA) for prostatic cancer and others. Abnormal values of PAP in untreated prostatic cancer were found in 0, 0, 50, 50, 0, 73% of stage A1, A2, CpN0, CNX, D1 and D2 cases, respectively, and those of PA were found in 25, 0, 50, 100, 100, 100% of the same stages, respectively. Grade was not related to the level of PAP or PA. Prostatic hypertrophy showed increased values of PAP and PA in 11.1% and 7.4%, respectively. The levels of PAP were not correlated to those of PA. Endocrine treatment decreased the elevated values of PAP and PA in 60% of the cases. Most of the PAP and PA levels in the cases controlled under endocrine therapy were within normal values, but after relapse most showed elevated levels.

Acid Phosphatase↗
PubMed1991

Quantification of tartrate resistant acid phosphatase activity using a computerized image analysis system.

Tartrate resistant acid phosphatase (TRAP) has been accepted as a marker for identification of osteoclasts. A method is reported here for quantitating TRAP using an image analysis system. The amount of the enzyme specific to osteoclasts can be used to differentiate osteoclasts from other cells capable of TRAP expression. TRAP expression characteristic of the osteoclast was compared with that of multi-nucleated giant cells (MNGC)s recruited to the site of subcutaneously implanted mineralized bone matrix. Two weeks post-implantation, the pellets were removed and processed for the demonstration of TRAP along with rat proximal tibiae. A large amount of TRAP was consistently expressed by the in situ osteoclasts. The MNGCs associated with the mineralized bone implants expressed little if any TRAP reaction product. Using this system, the amount of TRAP reaction product or any other enzyme reaction product expressed can be objectively and reproducibly quantitated.

Acid Phosphatase↗
PubMed1985

Cloning and characterization of two genes restoring acid phosphatase activity in pho1- mutants of Schizosaccharomyces pombe.

Schizosaccharomyces pombe acid phosphatase (APh) is a secreted cell surface glycoprotein which is deficient in pho1 mutants. By screening an S. pombe gene bank for sequences which can functionally rescue the pho1-44 mutation, we have isolated two genomic clones carried in plasmids pSp4B and pSp4C/2. These two sequences map of different genetic loci and show no cross hybridization by Southern blotting. pSp4C/2 was found to contain the PHO1 gene, and cells transformed with this plasmid produce a protein which cross-reacts with antibodies raised against the protein moiety of APh. Data from Northern blotting experiments show that pSp4C/2 encodes a 1.6-kb transcript, and that mRNA levels are increased when cells are grown in low concentrations of inorganic phosphate. The results indicate that pSp4C/2 contains the structural gene for APh, PHO1, whereas pSp4B appears to carry a gene coding for a minor species of APh, PHO4 which is not regulated by extracellular phosphate.

Acid Phosphatase↗
PubMed1983

Acid phosphatase among Brahmin and Kamma caste populations of coastal Andhra Pradesh, India.

Haemolysate samples from two caste populations, namely Brahmin and Kamma from coastal Andhra Pradesh, India, were typed for acid phosphatase by using starch gel electrophoresis with the discontinuous buffer system. The sample includes 225 Brahmins and 221 Kammas. Only A, B and AB phenotypes were observed and a statistically significant difference was found between the two caste groups in their acid phosphatase distribution. An association of higher B gene frequency with non-vegetarian diet is also suggested.

Acid Phosphatase↗
PubMed1994

The cellular level of prostatic acid phosphatase and the growth of human prostate carcinoma cells.

Prostatic acid phosphatase (PAcP) is a prostate epithelium-specific differentiation antigen. It has been demonstrated that human PAcP exhibits endogenous protein tyrosine phosphatase (PYP) activity, and that it represents the major PYP activity in normal prostate cells. Thus, it has been postulated that cellular PAcP may play a role in the tyrosine phosphorylation-mediated signal transduction. In this paper, we used LNCaP human prostate carcinoma cells, which express the endogenous PAcP, to study changes in cellular PAcP activity during cell growth. Our results demonstrated that PAcP activity increased when the cells reached confluence. Stimulation of cell growth by fresh culture medium or 5 alpha-dihydrotestosterone (DHT), a classical stimulator of prostate epithelial growth, resulted in a decline in PAcP activity. Moreover, transfection of PC-3 cells, which do not express PAcP, with a PAcP-expressing vector led to diminished cellular growth rate. These data established an inverse relationship between the cellular level of PAcP and the cell growth rate, suggesting that PAcP may be involved in regulating the growth of human prostate carcinoma cells.

Acid Phosphatase↗