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PubMed1977

Comparative studies on immobilization of human prostatic acid phosphatase.

Acid phosphatase (othophosphoric monoester phosphohydrolase (acid optimum), EC 3.1.3.2) from the human prostate was immobilized by its protein moiety on cyanogen bromide-activated Sepharose, by carbohydrate moiety on Concanavalin-A-Sepharose, and by Schiff base formation with partially oxidized carbohydrate groups on ethylenediamine-Sepharose. The highest retention of enzyme activity, 80%, was found for the noncovalent immobilization on Concanavalin-A-Sepharose. It was demonstrated that the optimal pH changes for the Concanavalin-A-Sepharose and CNBr-Sepharose-enzyme complexes are electrostratic in character. In all cases of immobilization the enzyme has higher thermostability than that for the native enzyme under the same conditions. The effects of the enzyme stabilization were interpreted in terms of the multipoint interaction between the enzyme molecule and the carrier.

Acid Phosphatase↗
PubMed1975

Radiation effects on rat testes. V. Studies on lysosomal enzymes (acid phosphatase and acid DNAse) and their physiological significance following partial body gamma-irradiation.

Acid phosphatase is present in the nucleus and cytoplasm of cells in the seminiferous tubules and the interstitium of rat testes. The effect of irradiation on acid phosphatase is dependent on the environmental temperature and the dose of irradiation. It appears that initial rise in the enzyme at a low radiation dose and a high environmental temperature or at a high dose and low temperature is associated with a lysosomal breakdown of the germinal cells of the testes. A decrease in acid phosphatase in the advanced stages of radiation injury is a secondary radiation effect which may lead to decreased metabolic synthesis of phosphate esters owing to the unavailability of orthophosphate in the testicular tubules. The reduced acid phosphatase activity can be detected in the seminiferous tubules, suggesting that the enzyme activity is related to the state of the germ cell population. An initial increase in acid phosphatase is matched by an initial rise in acid DNAse within hours of irradiation, further suggesting that there is radiation interaction with the cells of the germinal epithelium. The enhanced activity of DNAse following a 2nd week of irradiation at 2000 R confirms the phagocytic activity of the non-germinal cells.

Acid Phosphatase↗
PubMed1976

[Cathepsin, phosphoprotein-phosphatase and acid phosphatase in the soluble fraction of the cattle brain cortex: purification and properties (author's transl)].

Cattle brain cortex was homogenised in 0, 29 mol/1 sucrose and centrifuged at 101 000 X g. The supernatant contains the majority of 3 enzymes participating in protein turnover: cathepsin (EC 3.4.4.23), phosphoprotein phosphatase (EC 3.1.3.16) and acid phosphatase (EC 3.1.3.2). They were separated by chromatography on Sephadex G 200 in neutral buffer. The cathepsin was purified up to 380 fold by gel filtration on Sephadex and column electrophoresis. The pH optimum of cathepsin was 5.7. At 37 degrees C no decrease of activity was measurable during 30 min. The Km was found to be 2.75 mg/ml Casein Hammarsten. The molecular weight by gel filtration and exclusion-gel electrophoresis was about 45 000, corresponding to the cathepsin from human liver (Barrett, A.J. (1970) Biochem. J. 117, 601-607). The sedimentation constant 3.0 S20,W is comparable with the values of proteinase of different origin, and the composition is similar with respect to the high proportion of acidic amino acids. The phosphoprotein phosphatase can be further purified by chromatography on hydroxyapatite and by column electrophoresis. The pH optimum of phosphoprotein phosphatase was about pH 5.5. At 45 degrees C no decrease of activity was measurable during 20 min; the Km was 1.43 mg/ml casein isoelectric. The pH optimum of acid phosphatase was about 5.6. At 54 degrees C NO DECREASE OF ACTIVITY WAs measurable during 30 min; the Km was 2 mumol/1 for Sodium phenolphthalein diphosphate. All three enzymes slowly lost their activity during several weeks at - 4 degrees C, apparently by self digestion in the cold.

Acid Phosphatase↗
PubMed1990

Experimental model of acute appendicitis in the rabbit with determination of leucine amino peptidase (LAP) and acid phosphatase (acid-P) activities in portal blood samples.

The activities of leucine amino peptidase (LAP) and acid phosphatase (Acid-P), conceivable markers of acute appendicitis, were determined in the portal blood of rabbits with acute appendicitis. An experimental model of acute appendicitis was established using No.-O silk ties to block the base of the appendix. The clinical and histopathological picture of acute appendicitis was seen after 12 hr in all the rabbits in the model group (9/9) and in none of the control group. Catheterization of the superior mesenteric vein was performed in rabbits with acute appendicitis, and portal blood samples were taken at 0, 6, and 12 hr for assay of LAP and Acid-P activities. No statistically significant difference between the experimental group and the control group, in the activities of LAP and Acid-P, was found at any time interval. The experimental model of acute appendicitis in the rabbit which is described here is simple and carries a high rate of success. This is probably the first report of using continuous catheterization and repeated sampling of portal blood, for the measurement of enzyme activities, in an experimental model of acute appendicitis. It was concluded that serum LAP and Acid-P activities cannot be used as markers for acute appendicitis.

Acid Phosphatase↗
PubMed1980

Isoelectric focusing pattern of acid phosphatase and acid esterase in human blood cells, including thymocytes, T lymphocytes, and B lymphocytes.

Lysosomal acid phosphatase and acid esterase from highly purified, viable human thymocytes, T lymphocytes, B lymphocytes, granulocytes, monocytes, platelets, and erythrocytes were subjected to direct measurement of activity and to isoelectric focusing in polyacrylamide thin-layer slabs. The typical patterns for each cell line were found to be distinctly different from the results recently presented in this journal. The study described here opens a new possibility for the biochemical identification of cells and their functional derivatives and neoplastic variants.

Acid Phosphatase↗
PubMed1985

Acid phosphatase and phosphoamino acid phosphatases in murine erythroleukaemic cells.

The activities of acid and alkaline phosphatases and phosphotyrosine, phosphoserine and phosphothreonine phosphatases were measured in Friend murine erythroleukaemic (MEL) cells. The effects of treating the cells with dimethyl sulphoxide (DMSO), an inducer of differentiation, were examined. In untreated cells alkaline phosphatase activity was undetectable, though there were significant amounts of acid phosphatase (76 +/- 15 mU/mg protein) and phosphotyrosine phosphatase (16 +/- 0.9mU/mg protein); phosphoserine and phosphothreonine phosphatase activities (9 +/- 0.4 and 7 +/- 0.6mU/mg protein, respectively) were lower than for phosphotyrosine phosphatase. Addition of 1 or 2% DMSO to the culture medium resulted in the expected cell death within 2 weeks. With 0.5% DMSO, cells remained viable for at least 8 weeks, but while some appeared to have smaller nuclei and retained their rounded appearance, others became fibroblastic within several days and adhered to the culture vessel. The treated cells which had kept their morphology showed no difference in acid phosphatase activities as compared with untreated controls; phosphotyrosine phosphatase was lower (9 +/- 0.8mU/mg protein) and phosphoserine and phosphothreonine phophatases higher (11 +/- 0.5 and 10 +/- 0.4mU/mg protein, respectively) than in the controls. The Km values for p-nitrophenyl phosphate were similar in untreated and treated cells (0.069 and 0.068mM, respectively); for phosphotyrosine the Km value was lower in the treated cells (0.97mM) than in the controls (1.9mM).

Acid Phosphatase↗
PubMed1987

Cytochemistry and biochemistry of acid phosphatases VII: Immunohistochemistry of canine prostatic acid phosphatase.

Acid phosphatase (E.C. 3.1.3.2.) has been isolated from canine prostatic gland homogenates by gel permeation chromatography (AcA34 or G150), by affinity chromatography (con A-Sepharose), or by using fluid phase liquid chromatography (FPLC) using Superose 12 and Mono P columns. Acid phosphatase-enriched fractions were submitted to analytical SDS-PAGE or to analytical isoelectric focusing. A protein with a molecular weight of 30 kD (on SDS gels) was used for immunization of rabbits. The antiserum produced was cross-reactive with prostatic acid phosphatase (canine and human) as shown by immunoblotting. When applied to paraffin or plastic sections of normal canine prostate, a positive immunoreaction was found exclusively in the secretory cells. In experimentally altered glands (castration and/or hormone treatment), a varying pattern of immunoreactive cells was found. In canine prostatic carcinomas, intensively reacting cell clusters were found along with nonreactive cells. The antiserum was also slightly cross-reactive with the respective human antigen, but the cross-reactivity of an antiserum prepared against human prostatic secretory acid phosphatase with canine prostatic acid phosphatase was far more pronounced.

Acid Phosphatase↗
PubMed1984

Histochemical activity of alkaline phosphatase and acid phosphatase in the epididymis of mature intact and androgen-deprived bulls.

The histochemical localization of alkaline phosphatase (ALP) and acid phosphatase (ACP) was determined in regions I to VI of the epididymis in mature intact, orchidectomized, and orchidectomized testosterone-treated bulls. The intensity of ALP activity was essentially the same in all regions; however, its localization varied depending upon the region. Although the stereocilia and luminal border of epithelial cells were strongly-positive in regions I to III, these were negative in regions IV to VI. The basement membrane and circumtubular smooth muscle cells were strongly ALP reactive in all regions. Epithelial ALP activity was abolished completely by orchidectomy; however, it was restored to normal concentration by testosterone treatment implying its dependence on circulating testosterone. The ACP activity was present in the epithelial cells of all regions with the strongest activity in the supranuclear region. Similar to ALP, ACP activity was markedly reduced in the epithelial cells by orchidectomy. However, in contrast to ALP activity, lost ACP activity was only minimally increased by testosterone treatment in all regions, except in region VI where it was restored to a normal concentration. These observations imply that although the epithelial ACP activity of region VI was mainly under the influence of circulatory testosterone, there may be other factors such as luminal androgens, testicular fluid, and sperm that may be important in regulating the ACP activity of regions I to V of the epididymis. The importance of ALP and ACP in the epididymal epithelium was discussed.

Acid Phosphatase↗
PubMed1984

Acid phosphatase and acid esterase activity in neoplastic and non-neoplastic lymphoid cells. A semiquantitative evaluation related to immunological markers in 112 cases.

Acid phosphatase (AcP) and acid alpha-naphthylacetate esterase (ANAE) were examined in lymphoid cells from 104 patients suffering from various lymphoproliferative disorders and from 8 healthy controls. Enzyme activities were evaluated by means of a scoring system. Scores of AcP and ANAE were higher in normal T cells than non-T cells. In comparison, the activated T cells in infectious mononucleosis showed increased AcP and decreased ANAE reaction. Malignant T lymphoblasts had a distinct granular AcP positivity in contrast to the faint reactivity observed in cALL blasts, whereas ANAE showed negative or weak reaction in both subsets. High scores and distinct staining patterns for both enzymes were found in T CLL and T prolymphocytic leukaemia, clearly different from the weak activities seen in B CLL, B PLL and some B cell lymphomas. The latter, too, could be distinguished by mutual differences in enzyme reactions. High AcP and ANAE scores were also found in hairy cell leukaemia, and the staining patterns together with the tartrate resistance firmly established the diagnosis. Thus, simultaneous determinations of AcP and ANAE can be of great value in the diagnosis of lymphoid malignancies.

Acid Phosphatase↗
PubMed1976

Effects of prednisolone metasulfabenzoate on the induction of DNase II in comparison to alkaline phosphatase and acid phosphatase activities in cultures of HeLa S3 cells.

Cultures of HeLa S3 cells were treated with prednisolone metasulfobenzoate (Na), a derivative of prednisolone which is readily soluble in water. The steroid induced an increase in DNase II, a lysosomal enzyme which was not used previously in enzyme induction by steroids. Alkaline phosphatase, a known inducible enzyme by other steroids and acid phosphatase, a known uninducible enzyme by other steroids, were included for comparative reasons.

Acid Phosphatase↗
PubMed2003

Suppression of LNCaP prostate cancer xenograft tumors by a prostate-specific protein tyrosine phosphatase, prostatic acid phosphatase.

BACKGROUND: Although the molecular mechanism of androgen-independent prostate cancer growth and progression has been gradually elucidated, there is limited effective treatment for this prevalent disease. Human prostatic acid phosphatase (PAcP), a major protein tyrosine phosphatase in prostate epithelium, plays a critical role in regulating the growth of prostate cancer cells. In prostate carcinomas, the expression of cellular PAcP decreases. To explore directly the possible therapeutic potential of cellular PAcP, we investigated the suppression effect of PAcP by utilizing cDNA direct intratumoral administration in androgen-independent LNCaP xenograft tumors. METHODS: An androgen-independent LNCaP cell model (C-33 and C-81 cells) and stable subclones of PAcP cDNA-transfected C-81 cells (LNCaP-23 and LNCaP-34 cells) were used for the experiments. We examined the growth property and expression of PAcP and c-ErbB-2 of these different LNCaP cells in vitro and in vivo. We subsequently investigated the growth suppression effect of PAcP cDNA intratumoral injection in pre-established C-81 xenograft tumors, and analyzed the expression of PAcP, prostate-specific antigen (PSA), proliferating cell nuclear antigen (PCNA), and c-ErbB-2 in the tumors by immunohistochemistry and Western blotting. RESULTS: The different LNCaP cells exhibited different growth property and tumorigenicity, both in cell culture and xenograft. Biochemical characterizations revealed that the level of cellular PAcP correlated negatively with the growth property of different LNCaP cells, while the level of tyrophosphorylated c-ErbB-2 had an inverse correlation with cellular PAcP. The single intratumoral administration of the wild type PAcP cDNA showed a significant suppression effect on C-81 xenograft tumor growth, compared to vector alone-injected control (P<0.05). In the tumors injected with this PAcP cDNA, the PAcP expression was detected 1 week (wk) after injection, but was undetectable at 6 wk, which inversely correlated with the level of tyrophosphorylated c-ErbB-2 and the degree of cell proliferation indicated by PCNA staining. CONCLUSIONS: Our results clearly demonstrated that cellular PAcP has a suppression effect on the growth of androgen-independent LNCaP xenograft tumors. This effect occurs at least partly through the dephosphorylation of c-ErbB-2 by PAcP, the prostate-specific protein tyrosine phosphatase. The data indicates that human PAcP could be utilized in the corrective gene therapy for a subgroup of androgen-independent human prostate cancer cells that lack cellular PAcP expression.

Acid Phosphatase↗
PubMed1994

[Effect of artemether on glycogen, protein, alkaline phosphatase and acid phosphatase of Schistosoma japonicum].

When mice infected with Schistosoma japonicum for 32-35 d were treated ig with artemether (Art) at a single dose of 300 mg.kg-1 for 24 h, the glycogen content of female and male schistosomes decreased significantly with reduction rates of about 50%. 72 h after medication, the glycogen reduction rates were 64.1-77.9%. Meantime, the protein content of female and male worms was also decreased, the reduction rates being 68.1% and 49.3%, respectively. In infected mice treated ig with Art at the same dosage for 24 h, the inhibition rates of alkaline phosphatase (AKP) activity in female and male worms were 30% and 25%, respectively. 72 h later, the AKP activity of female worm was further inhibited to 62.3% as compared with the control. Besides, the inhibitory effect of Art on acid phosphatase (ACP) activity of female worm was also more apparent than that of male worm. 72 h after medication, the respective inhibition rates of ACP activity in female and male worms were 75.7% and 47.6%. The results indicated that Art might exert its effect on both carbohydrate and protein metabolism of schistosomes.

Acid Phosphatase↗
PubMed1982

Bone acid phosphatase: tartrate-resistant acid phosphatase as a marker of osteoclast function.

Organ cultures of newborn mouse calvaria were used to test the hypothesis that tartrate-resistant acid phosphatase might serve as a biochemical marker for osteoclast function. When bone resorption was stimulated in vitro with either parathyroid hormone or 1,25(OH)2D3, there was a significant increase in both tartrate-resistant and tartrate-sensitivity acid phosphatase activity in the medium relative to cultured controls. Tartrate-resistant activity was localized histochemically primarily over the osteoclast and appeared as three distinct activity bands when electrophoresed on polyacrylamide gels. The tartrate-sensitive activity was found primarily associated with bone cells other than the osteoclast using histochemical techniques, and was resolved into five bands on polyacrylamide gels. The results obtained from biochemical assays, histochemical observations, and polyacrylamide gel electrophoresis suggest that bone resorption in vitro results in the release of tartrate-resistant acid phosphatase from osteoclasts and tartrate-sensitive acid phosphatase from other bone cells as well as osteoclasts. Tartrate-resistant acid phosphatases of bone may be suitable biochemical probes for osteoclasts function, but it will be necessary to achieve further purification in order to develop analytical methods with sufficient sensitivity and specificity (e.g., immunochemical) to ensure precise localization and quantitation.

Acid Phosphatase↗
PubMed1977

"Prostatic acid phosphatase?" A comparison of acid phosphatase activities in epithelial cells, granulocytes, monocytes, lymphocytes, and platelets purified by velocity sedimentation in isokinetic gradients of Ficoll in tissue culture medium.

Numerous investigators have found several substrates and inhibitors to be particularly suited for the demonstration of acid phosphatase of prostatic origin. There has been much controversy over the specificity or lack of specificity of several substrates and inhibitors. We have investigated acid phosphatase activities obtained from several kinds of purified cells. None of the substrates or inhibitors which we studied permitted us to discriminate "prostatic" acid phosphatase from acid phosphatase activities obtained from other kinds of cells.

Acid Phosphatase↗
PubMed1989

High degree of homology between primary structure of human lysosomal acid phosphatase and human prostatic acid phosphatase.

Alignment of the amino-acid sequences of the human lysosomal acid phosphatase (LAP) and human prostatic acid phosphatase (PAP) yielded an extensive homology between the two mature polypeptide chains. In the overlapping part, which extends over the entire PAP sequence and the N-terminal 90% of the LAP sequence, the identity is 49.1%. The LAP has an additional C-terminal sequence, which is encoded by the last exon of the LAP gene. This sequence contains the transmembrane domain of LAP, which is lacking in the secretory PAP. All six cysteine residues as well as 20 out of 27 (LAP) and 26 (PAP) proline residues present in the overlapping part of the proteins are conserved, suggesting that they are involved in stabilization of the tertiary structure of both proteins. Only two out of 8 N-glycosylation sites in LAP and 3 in PAP are conserved, suggesting that the dense N-glycosylation of LAP is related to its function in lysosomes.

Acid Phosphatase↗