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PubMed1977

The histochemical demonstration of human prostatic acid phosphatase with phosphorylcholine.

Tissues from patients with benign prostatic hyperplasia were used for the cytochemical demonstration in light and electron microscopy of a secreted, nonlysosomal prostatic acid phosphatase (PAP) with phosphorycholine, substrate specific for PAP. The specificity of phosphorylcholine for PAP is attributable to the pentavalent nitrogen in phosphorylcholine, a feature that renders it resistant to hydrolysis by all other acid phosphatases. PAP activity was found in the Golgi cisternae and its associated vacuoles and in secretory vacuoles localized in the nuclear, Golgi, and apical areas of the prostatic epithelial cell. These results confirm the existence of two types of acid phosphatase in prostatic tissue. One is lysosomal and is prevalent in many tissues and the other, PAP, is the major enzymatic product secreted by the prostate. The specificity of PAP for phosphorylcholine, one of the natural substrates for this enzyme, validates the use of this method for the histochemical characterization of PAP and indicates the prostatic origin of cells showing PAP activity.

Acid Phosphatase↗
PubMed2001

Cooperative kinetics of human prostatic acid phosphatase.

The steady-state kinetics of hydrolysis reaction catalysed by human prostatic acid phosphatase (PAP) by using 1-naphthyl phosphate, phenyl phosphate and phosphotyrosine as substrates has been studied at pH 5.5. The substrate binding curves were sigmoidal and Hill cooperation coefficient h was higher than 1 for each of the examined compounds. Thus, human prostatic acid phosphatase kinetics exhibits positive cooperativity towards the studied substrates. The extent of cooperativity was found to depend on the substrate used and on enzyme concentration. The highest cooperativity of PAP was observed for 1-naphthyl phosphate and the lowest for phosphotyrosine. When prostatic phosphatase concentration increased, Hill cooperation coefficient (h) and half saturation constant (K(0.5)) both grew, but the catalytic constant (k(cat)) remained constant, for each of the substrates studied. Ligand-induced association-dissociation equilibrium of the active oligomeric species (monomer-dimer-tetramer-oligomers) is suggested.

Acid Phosphatase↗
PubMed1981

Serum acid phosphatase activities in patients with lung cancer: a biochemical and immunohistochemical analysis of 25 cases.

A series of 25 cases of lung cancer are presented in which total (TAcP) and nonprostatic serum acid phosphatase (NPAcP) activities were measured. Of these cases, 36% had raised TAcP and NPAcP activities in their serum. However, the serum activities of TAcP and NPAcP did not correlate with either the presence of lung cancer nor with the morphological tumour type. This fact indicates that, despite isolated reports of raised serum acid phosphatase activities in cases of lung cancer, acid phosphatase is of no value as a marker for lung cancer. We sought alternative explanations for the raised TAcP and NPAcP activities observed in our series in the hope that this enzyme might prove useful as a marker for early metastatic disease in lung cancer patients. This possibility is not substantiated, and the findings are analyzed and discussed. It is tentatively suggested that raised NPAcP activities in patients with lung cancer may relate to haemostasis.

Acid Phosphatase↗
PubMed1982

Immunoperoxidase localization of prostatic acid phosphatase in prostatic carcinoma with sarcomatoid changes.

Immunoperoxidase staining of tissue for prostatic acid phosphatase has been useful in confirming the prostatic origin of metastatic deposits. This technique was used on the prostate tumors of 2 patients to differentiate between a true carcinosarcoma and a pure epithelial carcinoma with sarcomatoid changes. Positive staining for prostatic acid phosphatase in both the sarcomatoid element, as well as the area of well-differentiated carcinoma, confirmed the common epithelial cell origin of these components. Electron microscopy further confirmed these findings by demonstrating desmosomes in the sarcomatoid areas. Although each type of tumor is rare, differentiation between true carcinosarcomas and true carcinomas with sarcomatoid changes is important to elucidate further their different clinical behaviors and responses to therapy.

Acid Phosphatase↗
PubMed2000

Purification and partial characterisation of tentatively classified acid phosphatase from the earthworm Eisenia veneta.

In order to use leakage of lysosomal acid phosphatase (AP) as a biomarker of stress to earthworms, more information about AP's in earthworms are needed. This paper describes the details about tentatively classified APs in the earthworm Eisenia veneta. Two isoenzymes (enzyme I and II) of acid phosphatase (AP) and one alkaline phosphatase (enzyme III) from the earthworm E. veneta were separated by gel filtration. All three enzymes were further purified and concentrated on a Con A Sepharose 4B column. Enzyme I was inhibited by tartrate, showed an optimal pH range between 4.0 and 5.0 and was assumed to be of lysosomal origin. Enzyme II was the major enzyme showing the highest activity of the three enzymes. It was expected to be a lysosomal AP under physiological conditions. Enzyme II had a molecular mass 113 kDa and was composed of apparently identical polypeptide chains of 36 kDa each. This enzyme was inhibited by tartrate, showed an optimal pH in the range 6.0-7.5 and was slowly degraded at temperatures above 40 degrees C. Enzyme III is not inhibited by tartrate and has a pH-optimum > 9. The subcellular location under physiological conditions was assumed to be the cytosol.

Acid Phosphatase↗
PubMed1975

[Immunological cell markers on lymphoblasts of patients with acid phosphatase positive acute leukemia (author's transl)].

Blast cells of 4 patients with acid phosphatase positive acute leukemia were investigated for T and B lymphocyte markers. Nearly all blast cells showed a typical T cell marker, namely spontaneous rosette formation with sheep red blood cells. No surface immunoglobulin was demonstrable on these cells. 3 of these 4 patients showed an enlargement of the upper mediastinum most probably due to the thymus. The conclusion is drawn that the acid phosphatase positive acute leukemia is a T cell leukemia. Some clinical data about these 4 patients are given.

Acid Phosphatase↗
PubMedDate not supplied

Activity and electrophoretic forms of alkaline and acid phosphatases in the reproductive system of laying hen.

The activity of both enzymes was measured in the extracts of all parts of the reproductive system of the hen. Very high activity of alkaline phosphatase was found in the follicle membranes and very low values in the oviduct. The values of the activity of acid phosphatase are similar in various parts of the oviduct and ovary. Only in the contents of the follicle and in the yolk the activity was near zero. The electrophorograms of alkaline and acid phosphatases in the ovary and the oviduct show similar phenotypes as in the blood. It seems that acid phosphatase does not play any topical role in the functions of the reproductive system. Very high activity of alkaline phosphatase, particularly in the membrane of the ovarian follicles, confirms the suggestion that this enzyme has an active role in the transport of yolk material from the blood into the follicle during its growth.

Acid Phosphatase↗
PubMedDate not supplied

[Ecdysterone induces the activity of multiple forms of acid phosphatase and malate dehydrogenase in fat bodies of Anterahea pernyi pupae].

The method of electrophoresis in PAAG has been used to study activity of multiple forms of acid phosphatase and malate dehydrogenase of the fat body of Anterahea pernyi pupae in norm and affected by ecdysterone. It is shown that an increase of total activity of acid phosphatase and malate dehydrogenase with administration of a steroid hormone is promoted by growth of activity of certain inducible multiple forms of the studied enzymes. Ecdysterone injection considerably elevates activity of the most electrophoretically mobile form of acid phosphatase and provokes new formation of malate dehydrogenase form. Ecdysterone-induced increase of activity of the studied enzyme forms in the fat body of Anterahea pernyi pupae is blocked by actinomycin D, an inhibitor of transcriptional processes, and by puromycin, a translation inhibitor. These data permit concluding that an increase in activity of the mentioned forms of enzymes observed with hormonal induction is a result of their synthesis de novo and is mediated by the DNA-dependent RNA-synthesis.

Acid Phosphatase↗
PubMed1992

Acid phosphatase activity in the supramedullary neurons of Coris julis (L.).

This work describes the acid phosphatase activity in supramedullary neurons of Coris julis, analyzed by a cytochemical method. The presence of both acid phosphatase-positive and -negative membrane bound granules indicates that only a part of the numerous electrodense granules in the supramedullary neurons can be interpreted as lysosomes. The great number of lysosomes in these large neurons of young animals is indicative of the rapid turnover of cell structures, which may be correlated with the high rate of synthesis. The electrodense granules showing no acid phosphatase activity are postulated to be vesicles containing gastrin/CCK-like peptide or precursors of this neuromediator.

Acid Phosphatase↗
PubMed1979

Demonstration of multiple forms of acid phosphatase in hemolymph of the African snail, Archachatina marginata.

1. Hemolymph from the giant African snail Archachatina marginata has been analyzed for its content of certain lysosomal hydrolases and shown to contain substantial quantities of acid phosphatase (285 units/ml) hexosaminidase (512 units per ml) and beta-glucuronidase (28 units/ml). 2. Hemolymph acid phosphatase can be fractionated into 6 active components by DEAE-Sephadex chromatography. 3. Some of the acid phosphatase species can be distinguished on the basis of heat stability, pH dependency and sensitivity to inhibitors including phosphate, L(+) tartrate, fluoride, formaldehyde and 1.10 phenanthroline.

Acid Phosphatase↗
PubMed2000

Inhibition of acid phosphatase isoforms purified from mature soybean (Glycine max) seeds.

The four soybean seed acid phosphatase isoforms AP1, AP2, AP3A and AP3B were competitively inhibited by phosphate, vanadate, fluoride and molybdate, using p-nitrophenylphosphate as substrate. The four isoforms were not significantly affected by compounds that can interact with SH residues or by pyridoxal phosphate. These results indicated that cysteine and lysine residues are not present in the active site of the four soybean seed acid phosphatase isoforms. The inhibition constant values for phosphate, vanadate, fluoride and molybdate at pH 5.0 were respectively: API (250, 12.8, 1.7, 0.05 microM). AP2 (800, 10, 500, 0.025 microM), AP3A (250, 24.2,250, 0.032 microM ), AP3B (2400 36.9, 750, 0.05 microM).

Acid Phosphatase↗
PubMed1989

The extracellular acid phosphatase of the mosquito-parasitizing fungus Lagenidium giganteum.

The mosquito-parasitizing fungus Lagenidium giganteum secreted a soluble acid phosphatase and beta-D-glucosidase into the growth medium. The acid phosphatase was isolated and purified to single component, and some of its physicochemical properties were determined. The enzyme exhibited a pH optimum of 5.6 in phthalate buffer with p-nitrophenyl phosphate and was temperature-inactivated at 55 degrees C. Enzyme activity seems to be limited to phenyl-phosphate substrates. A molecular weight of 42,800 was found and the amino acid content was also determined. A Km for p-nitrophenyl phosphate of 1.6 x 10(-7) M was found. The possible involvement of the enzyme in the infective process was discussed.

Acid Phosphatase↗
PubMed1995

Clinical and biological aspects of acid phosphatase.

The identity and genetic origins of the nonspecific orthophosphate monoesterases with an acid pH optimum--the acid phosphatases--are now becoming clear. They form a family of genetically distinct isoenzymes, many of which show significant posttranslational modification. Four true isoenzymes exist. The erythrocytic and lysosomal forms show widespread distribution and are expressed in most cells; in contrast, the prostatic and macrophagic forms have a more limited expression. The erythrocytic and macrophagic forms are distinguished from the others in resisting inhibition by dextrorotatory tartrate. The prostatic form has long been used as a marker for prostatic cancer and the macrophagic forms have been linked with miscellaneous disorders, notably increased osteolysis, Gaucher's disease of spleen, and hairy cell leukemia, whereas the normal levels of intravesical lysosomal acid phosphatase in I cell disease pointed the way toward the mechanisms underlying its intracellular processing.

Acid Phosphatase↗
PubMed1983

Separation of acid phosphatases in the rat ventral prostate by gel filtration, isoelectric focusing, and chromatofocusing.

Acid phosphatases of the rat ventral prostate were fractionated by gel filtration (GF) on Sepharose 6B, isoelectric focusing (IEF), and chromatofocusing (CF). In GF three activity peaks (GF-1, GF-2, GF-3) were disclosed. They showed some differences in substrate preference when six substrates (p-nitrophenyl phosphate; p-NPP; phenolphthalein phosphate, Phe-P; thymolphthalein phosphate, Tym-P; alpha-naphthyl phosphate, alpha-NP; beta-naphthyl phosphate, beta-NP; naphthol ASBI phosphate, N-ASBI-P) were tested. Differences were also encountered in their sensitivity to tartrate and fluoride. IEF gave seven bands at different pI values (8.3, 8.1, 7.9, 7.1, 6.4, 5.5, and 5.0) with alpha-NP and beta-NP but only four with N-ASBI-P. Four of the bands (8.3, 8.1, 7.9, 5.5) were sensitive to tartrate. In CF eight activity peaks (CF-1 to CF-8) were resolved with the six substrates. They differed from each other in pI values, pH optima, substrate preference, and modifier characteristics. Peaks CF-1 (pI 8.3, pH 5.5), CF-2 (pI 8.1, pH 4.2) and CF-3 (pI 7.9, pH 4.2) had a large substrate spectrum and high sensitivity to tartrate and fluoride. CF-4 (pI 7.1, pH 6.0) and CF-7 (pI 5.5, pH 4.2) were low in activity, preferred alpha-NP as substrate, and were moderately sensitive to tartrate. CF-5 (pI 6.4, pH 5.5) and CF-8 (pI 5.0, pH 5.0) were able to hydrolyse all substrates tested with moderate inhibition by tartrate. CF-6 (pI 6.0, pH 5.0) showed a relative preference for p-NPP and Phe-P with no hydrolysis of N-ASBI-P and Tym-P. Of these activities CF-6 and CF-7 were also clearly activated by Co2+. Peaks CF-6 and CF-7 appeared the most sensitive to p-chloromercuribenzoate. It is concluded that activities CF-1, CF-2, and CF-3 are lysosomal isoenzymes with minor structural differences. The others are possibly all nonlysosomal with greater biochemical differences. Some of them apparently represent the secretory form(s) of acid phosphatase in the rat ventral prostate.

Acid Phosphatase↗
PubMed1978

Acid phosphatase activity in normal and denervated chick skeletal muscle.

Histochemical and biochemical changes in acid phosphatase activity were studied in the normal and denervated gastrocnemii of chick for a maximum period of 8 weeks. In the normal muscle, fibre heterogeneity with respect muscles exhibit greater susceptibility to degenerative changes on account of denervation. Quantitatively higher enzyme levels in the denervated muscles confirm the lytic role of acid phosphatase.

Acid Phosphatase↗
PubMed1983

Changes of the activity of acid phosphatase and beta-glucuronidase in isolated platelets of whole-body irradiated rats.

In the work presented here we paid our attention to studying changes of the activity of two lysosomal enzymes-acid phosphatase and beta-glucuronidase in platelets after whole-body irradiation and application of certain clinically applied antifibrinolytics (Antilysin Spofa and epsilon-aminocaproic acid) on the activity of these enzymes in isolated platelets. From the results it is obvious that the activity of acid phosphatase and beta-glucuronidase increases in platelets of irradiated rats with a maximum on the 11th day after irradiation. In the same time interval after irradiation the most remarkable thrombocytopenia was observed. The application of Antilysin or EACA to intact, non-irradiated rats affects remarkably neither the activity of the followed enzymes nor the count of platelets. A statistically significant thrombocytopenia, in a comparison with controls was found in whole-body irradiated rats who received EACA or Antilysin. The postirradiation increase of the level of acid phosphatase in platelets exerts a similar character in rats who received EACA or Antilysin as in those who were only irradiated with a difference that the increase of the level of this enzyme was essentially lower in all the time intervals of interest. The beta-glucuronidase level in platelets of rats, who received EACA, was essentially unchanged as compared to controls. The application of Antilysin altered remarkably the level of beta-glucuronidase in platelets of whole-body irradiated rats in a comparison with a level of this enzyme in platelets of rats who received no Antilysin. Most remarkable changes were observed in latter time intervals (11th and 15th day) when the beta-glucuronidase level in platelets of rats after the application of Antilysin was remarkably higher than that in solely irradiated rats.

Acid Phosphatase↗
PubMed1987

Tyrosinase and acid phosphatase activities in melanocytes from avian albinos.

Two forms of cutaneous albinism in the chicken were investigated for the presence and distribution of tyrosinase and acid phosphatase in melanocytes in situ and in culture. In sex-linked recessive tyrosinase-positive albinism, sal, melanocytes in regenerating feathers and neural tube-derived cultures contained morphologically normal and abnormal premelanosomes. Tyrosinase was localized primarily to the abnormal premelanosomes and probably not to the normal ones. The cells possessed, in addition, vacuoles with membranous inclusions, located in the dendrites, and capped by dopa-positive vesicles (capping vesicles). Acid phosphatase colocalized with tyrosinase in the abnormal premelanosomes and capping vesicles. Tyrosinase activity in extracts of cultured sal melanocytes equalled that of e+ control melanocytes. A tyrosinase antiserum, raised against hamster tyrosinase (Pomerantz), precipitated 2 proteins, 68 kD and 82 kD, which had a precursor-product relationship. The amount of immunoprecipitate was the same in sal and control extracts, but in sal extracts the lower-molecular-weight protein was twice as abundant as the higher-molecular-weight protein. Melanocytes in regenerating feathers from an autosomal recessive, tyrosinase-negative albino, ca, also contained morphologically normal and abnormal premelanosomes. In culture, ca melanocytes had no formal premelanosomes but only dopa-negative multivesicular bodies with wispy filamentous material. Tyrosinase activity and immunoprecipitable tyrosinase were absent. These results suggest that: the tyrosinase-positive albino, sal, has an aberration in both its tyrosinase and acid phosphatase profiles and the tyrosinase-negative albino, ca, lacks functionally and antigenically normal tyrosinase.

Acid Phosphatase↗
PubMed1976

Separation of cells with histochemically demonstrable acid phosphatase activity from suspensions of cells from human prostatic carcinomas in an isokinetic gradient of Ficoll in tissue culture medium.

This report describes the separation of cells exhibiting histochemically demonstrable acid phosphatase from suspensions of cells obtained from human prostatic carcinomas by velocity sedimentation. In the unseparated suspensions of cells, 40.5 +/- 7.7% of nucleated cells contained histochemically evident acid phosphatase. After cells were separated by velocity sedimentation, 86.4 +/- 9.4% of the nucleated cells in the purest fractions exhibited histochemically demonstrable acid phosphatase activity. More than 95% of these cells excluded trypan blue. To our knowledge, this is the first report of a method for the separation of viable epithelial cells from human prostatic carcinomas.

Acid Phosphatase↗