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PubMed1992

Advanced prostate cancer follow-up with prostate-specific antigen, prostatic acid phosphatase, osteocalcin and bone isoenzyme of alkaline phosphatase.

We report our experience in the follow-up of 63 patients with advanced prostate adenocarcinoma. We used prostate-specific antigen and prostatic acid phosphatase in 27 patients; in 36 patients we evaluated osteocalcin and bone isoenzyme of alkaline phosphatase, two markers of bone metabolism which seem to be good markers in the follow-up of patients with bone metastases.

Acid Phosphatase↗
PubMed1991

Human prostatic acid phosphatase directly stimulates collagen synthesis and alkaline phosphatase content of isolated bone cells.

Human prostatic acid phosphatase (hPAP) directly enhances the differentiated characteristics of isolated bone cells in vitro. This enzyme, when added to cell cultures for 24 h in vitro stimulates collagen synthesis and the production of alkaline phosphatase. The effects are dose dependent, with statistically significant effects occurring from 0.1-100 nM hPAP. Concentrations higher than 100 nM do not evoke greater effects. The maximal effect of hPAP occurs between 12 and 24 h of exposure. The cells stimulated to the greatest degree are osteoprogenitor cells and osteoblasts. Fibroblasts isolated from the same tissue show a lesser sensitivity to hPAP. hPAP has no detectable effect on cell proliferation, as measured by radiolabeled thymidine incorporation or total DNA synthesis. None of the observations reported in this work can be attributed to contaminating proteins in the hPAP preparation. hPAP was radiolabeled with 125I and was used for affinity binding and cross-linking studies. Scatchard analysis of specific binding indicated the presence of 1.0 X 10(5) high affinity binding sites/cell, with a Kd of 6.5 nM. Cross-linking studies demonstrated the presence of one 320-kDa binding complex. The pH profile and kinetic determinations of Km and maximum velocity for hPAP were similar to those previously reported, except for the finding of positive cooperativity of the substrate with the enzyme under the conditions of our assay. We believe that the direct stimulation of bone-forming cells by hPAP may contribute to the sclerotic nature of skeletal bone around sites of neoplastic prostatic metastases and that the effect of the enzyme is probably mediated by a plasma membrane receptor.

Acid Phosphatase↗
PubMed2005

Cellular prostatic acid phosphatase: a protein tyrosine phosphatase involved in androgen-independent proliferation of prostate cancer.

Human prostatic acid phosphatase (PAcP) was used as a valuable surrogate marker for monitoring prostate cancer prior to the availability of prostate-specific antigen (PSA). Even though the level of PAcP is increased in the circulation of prostate cancer patients, its intracellular level and activity are greatly diminished in prostate cancer cells. Recent advances in understanding the function of the cellular form of PAcP (cPAcP) have shed some light on its role in prostate carcinogenesis, which may have potential applications for prostate cancer therapy. It is now evident that cPAcP functions as a neutral protein tyrosine phosphatase (PTP) in prostate cancer cells and dephosphorylates HER-2/ErbB-2/Neu (HER-2: human epidermal growth factor receptor-2) at the phosphotyrosine (p-Tyr) residues. Dephosphorylation of HER-2 at its p-Tyr residues results in the down-regulation of its specific activity, which leads to decreases in growth and tumorigenicity of those cancer cells. Conversely, decreased cPAcP expression correlates with hyperphosphorylation of HER-2 at tyrosine residues and activation of downstream extracellular signal-regulated kinase (ERK)/mitogen activated protein kinase (MAPK) signaling, which results in prostate cancer progression as well as androgen-independent growth of prostate cancer cells. These in vitro results on the effect of cPAcP on androgen-independent growth of prostate cancer cells corroborate the clinical findings that cPAcP level is greatly decreased in advanced prostate cancer and provide insights into one of the molecular mechanisms involved in prostate cancer progression. Results from experiments using xenograft animal models further indicate a novel role of cPAcP as a tumor suppressor. Future studies are warranted to clarify the use of cPAcP as a therapeutic agent in human prostate cancer patients.

Acid Phosphatase↗
PubMed1992

Effects of mebendazole, albendazole, and praziquantel on alkaline phosphatase, acid phosphatase, and adenosine triphosphatase of Echinococcus granulosus cysts harbored in mice.

Mice infected with protoscoleces of Echinococcus granulosus for 12-14 months were treated ig with mebendazole (Meb) 25-50 mg.kg-1 x d-1 for 7-14 d, albendazole (Alb) 200 mg.kg-1 x d-1, cr praziquantel (Pra) 500 mg.kg-1 x d-1 for 14 d. The mice were killed 24 h after the last medication, and acid phosphatase (ACP), alkaline phosphatase (AKP), and adenosine triphosphatase (ATPase) including (Na, K, Mg)-ATPase, (Na, K)-ATPase, and (Mg)-ATPase were determined and compared with those of untreated control group. The results showed that ACP activities of cyst wall in treated groups were lower than the control group. Whereas AKP activity of cyst wall in Pra group increased markedly, this is not the case in Meb and Alb groups. Three ATPase activities of cyst wall were inhibited in both Meb and Alb groups, Meb being more potent. No apparent changes in the ATPase activities were seen in Pra group.

Acid Phosphatase↗
PubMed1986

Limited proteolytic digestion and dissociation of smooth muscle phosphatase-I modifies its substrate specificity. Preparation and properties of different forms of smooth muscle phosphatase-I.

Smooth muscle phosphatase-I (SMP-I), a protein phosphatase purified from turkey gizzard smooth muscle, is composed of 2 regulatory subunits (Mr = 60,000 and 55,000) and a catalytic subunit (Mr = 38,000). Two other forms of this enzyme have been prepared and characterized. The free catalytic subunit, termed SMP-Ic, was prepared by ethanol treatment of SMP-I, and a form devoid of the 55,000-Da subunit, termed SMP-I2, was prepared by limited tryptic digestion. Exposure of SMP-I to proteases like trypsin and chymotrypsin results in a rapid degradation of the 55,000-Da polypeptide. Degradation of the catalytic subunit is observed only upon prolonged digestion. The 60,000-Da polypeptide appears to be resistant to the action of trypsin and chymotrypsin. SMP-I dephosphorylates myosin light chains but is not active toward intact myosin or heavy meromyosin. However, when the catalytic subunit is dissociated from both regulatory subunits or from the 55,000-Da polypeptide, the enzyme becomes active toward myosin suggesting that the 55,000-Da polypeptide inhibits the activity of the catalytic subunit toward myosin. In addition to alteration of the substrate specificity, the regulatory subunits also modulate the effect of divalent cations, like Mn2+, on the activity of the enzyme.

Animals↗
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↗
PubMed1994

Comparative study of three protein-tyrosine phosphatases. Chicken protein-tyrosine phosphatase lambda dephosphorylates c-Src tyrosine 527.

To examine the substrate preference of protein tyrosine phosphatases (PTPs), we compared the activity of three transmembrane PTPs on dephosphorylation and regulation of c-Src and v-Src: chicken PTP lambda (ChPTP lambda), chicken PTP alpha (ChPTP alpha), and human leukocyte common antigen-related molecule (HLAR). In vitro, all three PTPs dephosphorylated v-Src, but only ChPTP lambda dephosphorylated c-Src. Their activities were also compared in Cos cells coexpressing Src and the phosphatase domains of three PTPs. These domains were fused with peptides for myristylation, so they associated with the cellular membrane. When c-Src was coexpressed with myrPTP lambda, its kinase activity was elevated 3-4-folds. This activation was less obvious when c-Src was coexpressed with myrPTP alpha or myrLAR. Analysis by cyanogen bromide cleavage showed that ChPTP lambda and myrPTP lambda dephosphorylated Tyr-527 of c-Src. Our data demonstrated the different activities of three PTPs on phosphoproteins, suggesting that Src Tyr-527 may require more specific PTP(s) than Src Tyr-416 for dephosphorylation in vivo.

Amino Acid Sequence↗
PubMed1994

[Levels of prostate-specific antigen, acid phosphatase, alkaline phosphatase and pain in the prediction of bone metastases in patients with newly diagnosed prostatic carcinoma].

In a retrospective analytical study the authors evaluated in 86 patients, mean age 69 years (range 55-85 years), with a newly diagnosed untreated prostate carcinoma the sensitivity, specificity, positive and negative predictive value of specific prostatic antigen (PSA), acid phosphatase (AP), alkaline phosphatase (AP') and pain in relation to possible affection of bones by secondaries. The authors found a highly negative predictive value for assessment of bone metastases when PSA values were lower than 10 ng/ml (96%), at levels under 20 ng/ml (94%) and a highly positive predictive value at levels higher than 50 ng/ml (97%). When AP and AP' are negative and there is no pain the occurrence of secondaries is of low probability. These results make it possible to differentiate some patients where scintigraphy of the skeleton is not inevitable. This procedure can be applied above all in patients where radical prostatectomy is not indicated.

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↗
PubMed1996

Cloning and characterization of fetal liver phosphatase 1, a nuclear protein tyrosine phosphatase isolated from hematopoietic stem cells.

We report the isolation of cDNAs encoding protein tyrosine phosphatases (PTPs) from highly purified hematopoietic stem cell populations. One such cDNA encodes a novel PTP, designated fetal liver phosphatase 1 (FLP1), which consists of one PTP domain followed by a carboxy terminal domain of 160 amino acids. Northern blot and in situ hybridization analysis showed that expression of FLP1 mRNA is restricted to thymus in 15.5-day-old and 17.5-day-old mouse embryos and to kidney and hematopoietic tissues in adult mice. Furthermore, polymerase chain reaction-based analysis shows that FLP1 is expressed in hematopoietic stem cells as well as in more mature hematopoietic cells. Peptide antisera against FLP1 immunoprecipitated a 48-kD protein that is localized in the nuclei of Ba/F3 lymphoid cells. We have analyzed the effects of overexpressing either wild-type FLP1 or a functionally inactive mutant of FLP1 in hematopoietic cells. In the progenitor K562 cell line, cells ectopically expressing functional FLP1 differentiated normally to megakaryocytes after induction with tetradecanoyl phorbol acetate (TPA). In contrast, when K562 transfectants expressing an inactive mutant FLP1 protein were treated with TPA, the characteristic cell spreading and substrate adhesion that accompany megakaryocytic differentiation did not occur. We show that, in these cells, the induction of the differentiation marker alphaIIb beta3 is not affected. However, both constitutive and TPA-induced expression of alpha2 integrin, a late megakaryocytic marker, are inhibited. These results suggest that the expression of an inactive form of FLP1 affects late signaling events of K562 megakaryocytic differentiation.

Amino Acid Sequence↗
PubMed1991

Ultrastructural localization of tartrate-resistant acid phosphatase (purple acid phosphatase) activity in chicken cartilage and bone.

Tartrate-resistant acid adenosine triphosphatase activity at pH 6.5, using a lead-salt method, was localized at light and electron microscopic levels in cartilage and bone matrices, osteoclasts, and chondroclasts. Cartilage matrix staining occurred after vascular invasion of the growth plate. In osteoclasts, activity was present in lysosomes, extracellular ruffled border channels, and the underlying cartilage and bone matrices. Staining artifacts occurred at lower pH levels (pH 5.4, 5.0). Adenosine diphosphate, p-nitrophenylphosphate, thiamine pyrophosphate, and alpha-naphthylphosphate also acted as substrates; but no activity was observed when adenosine monophosphate, adenylate-(beta, gamma-methylene) diphosphate, and beta-glycerophosphate were used. The activity was inhibited by NaF, dithionite, and a high concentration of p-chloromercuribenzoic acid, and activated by simultaneous addition of FeCl2 and ascorbic acid, as has been shown in biochemical studies. These histochemical results support the view that the adenosine triphosphate hydrolyzing activity at pH 6.5 is due to tartrate-resistant acid phosphatase (TRAP). There were some differences in ultrastructural localization between TRAP and tartrate-sensitive acid phosphatase (TSAP) activities in osteoclasts: TSAP activity was more intense in lysosomes and Golgi complexes and TRAP was stronger in the cartilage and bone matrices. It is suggested, therefore, that most of TRAP is in an inactive form in cells and is activated when secreted.

Acid Phosphatase↗
PubMed1994

Specific activity of skeletal alkaline phosphatase in human osteoblast-line cells regulated by phosphate, phosphate esters, and phosphate analogs and release of alkaline phosphatase activity inversely regulated by calcium.

We assessed the significance of Ca and phosphate (P(i)) as determinants of (1) the amount of skeletal alkaline phosphatase (ALP) activity in SaOS-2 (human osteosarcoma) cells and normal human bone cells, and (2) the release of ALP activity from the cells into the culture medium. After 24 h in serum-free BGJb medium containing 0.25-2 mM P(i), the specific activity of ALP in SaOS-2 cells was proportional to P(i) concentration (r = 0.99, p < 0.001). The P(i)-dependent increase in ALP activity was time dependent (evident within 6 h) and could not be attributed to decreased ALP release, since P(i) also increased the amount of ALP activity released (r = 0.99, p < 0.001). Parallel studies with Ca (0.25-2.0 mM) showed that the amount of ALP activity released from SaOS-2 cells was inversely proportional to the concentration of Ca (r = -0.85, p < 0.01). This effect was rapid (i.e., observed within 1 h) and could not be attributed to a decrease in the amount of ALP activity in the cells. Phase distribution studies showed that the effect of low Ca to increase ALP release reflected increases in the release of both hydrophilic ALP (i.e., anchorless ALP, released by phosphatidylinositol-glycanase activity) and hydrophobic ALP (i.e., phosphatidylinositol-glycan-anchored ALP, released by membrane vesicle formation). The range of Ca-dependent changes in ALP-specific activity was much smaller than the range of P(i)-dependent changes. The observed correlation between skeletal ALP-specific activity and P(i) was not unique to osteosarcoma cells or to P(i). Similar effects were seen in normal human bone cells in response to P(i) (r = 0.99, p < 0.001) and in SaOS-2 cells in response to a variety of P(i) esters and analogs (e.g., beta-glycero-P(i) and molybdate). Further studies indicated that the effects of phosphoryl compounds on ALP-specific activity could not be correlated with effects on ALP reaction kinetics, cell proliferation, or acid phosphatase activity and that the beta-glycero-P(i)-dependent increase in ALP activity was blocked by cycloheximide but not actinomycin D. Together these data suggest that the function of skeletal ALP may be regulated by P(i) and that Ca may be involved in ALP release.

Alkaline Phosphatase↗
PubMed1984

Ultrastructural demonstration of alkaline phosphatase (ALP) and K+-p-nitrophenyl phosphatase (K+-p-NPPase) in the epidermal ionocytes of Blennius sanguinolentus.

Cytochemical techniques were used for the light and electron microscopical localization of alkaline phosphatase and potassium-dependent nitrophenyl phosphatase in the epidermal ionocytes of the Teleost Blennius sanguinolentus. The heavier deposition of the reaction products obtained with the different media was shown in the cytoplasmic surface of the labyrinth tubules, the apical vesicles and in intimate association with plasmic membranes. Both plasma membranes and intracellular activities are affected by the addition of specific inhibitors L-p-bromotetramisole oxalate and ouabain) to both complete and control media. The significance of the cytoplasmic localization of both the two enzymes is discussed with reference to current models of transepithelial ion transportation.

4-Nitrophenylphosphatase↗
PubMed1996

Phosphotyrosine protein phosphatases and diabetic pregnancy: an association between low molecular weight acid phosphatase and degree of glycemic control.

Low molecular weight acid phosphatase encoded by the highly polymorphic locus ACP1 is a member of the protein-tyrosin phosphatase family (PTPases) which plays an essential role in the control of receptor signalling through phosphotyrosine pathways. Recent experiments have shown that purified rat liver ACP, corresponding to human ACP1, is able to hydrolyze a phosphotyrosine-containing synthetic peptide corresponding to the 1146-1158 sequence of the human insulin receptor, and shows a high affinity for it. This prompted us to analyze the degree of glycemic control in relation to ACP1 genetic variability in a sample of 214 diabetic pregnant women including IDDM, NIDDM and gestational diabetes. The ACP1 genotype was also determined in 482 non-diabetic pregnant women. In diabetic women glycemic levels in the last trimester of pregnancy appear to be significantly associated with the ACP1 genotype, and correlate positively with ACP1 enzymatic activity. The data suggest that quantitative variations of ACP1 may influence the clinical manifestations of diabetic disorders, and call for further studies on the role of this enzyme in the modulation of insulin-receptor phosphotyrosine pathways.

Acid Phosphatase↗
PubMed1996

A one-day double-labelling technique for tissue specimens: immunogold-silver staining for in situ hybridization combined with alkaline phosphatase-anti-alkaline phosphatase (APAAP) immunohistochemistry for antigens.

An improved technique is described that addresses the problems of sensitivity, specificity, the use of hazardous radioactive equipment and time consumption in immunohistochemical labelling and double labelling of in situ hybridization of tissue specimens. It consists of a two-step protocol in which digoxigenin-uridine triphosphate (UTP) labelled riboprobes in the in situ hybridization step are visualized by the immunogold-silver staining method, and double labelling of tissue antigens is achieved by the application of an alkaline phosphatase-anti-alkaline phosphatase staining step. We tested this protocol using snap-frozen tissue sections of synovial tissue from patients with rheumatoid arthritis. The target mRNA was detected by perforin or cathepsin D riboprobes, the double labelling was performed using anti-collagen type IV and alpha-smooth muscle actin antibodies. It is concluded that, in comparison with an established three- to four-day double-labelling protocol used in many laboratories, this one-day combination is currently the most rapid assay of reliable quality for double labelling of in situ hybridization products and tissue antigens.

Alkaline Phosphatase↗
PubMed1989

Efficacy of wheat germ lectin-precipitated alkaline phosphatase in serum as an estimator of bone mineralization rate: comparison to serum total alkaline phosphatase and serum bone Gla-protein.

Serum levels of total alkaline phosphatase activity (S-T-AP), wheat germ lectin-precipitated alkaline phosphatase activity (S-L-AP), and bone Gla-protein immunoreactivity (S-BGP) were measured in 26 patients (23 females and 3 males) aged 35-73 years (mean 59 years) with primary hyperparathyroidism (n = 7), hyperthyroidism (n = 9), and hypothyroidism (n = 10) in whom the bone mineralization rate (m) was determined by 47Ca-kinetics (continuously expanding calcium pool model). A weak positive correlation (r = 0.42, P less than 0.05) was found between S-T-AP and m, which in the range from 0-18 mmol Ca/day could be estimated with a standard error of 4.6 mmol/day. A closer correlation (r = 0.65, P less than 0.001) was found between S-L-AP and m which was estimated with an error of 3.9 mmol Ca/day. The AP activity in the supernatant showed no significant correlation to m (r = 0.11, P greater than 0.50). The highest correlation coefficient (r = 0.81, P less than 0.001) was found between S-BGP and m which could be predicted with an error of 3.4 mmol Ca/day. S-BGP showed a closer correlation to S-L-AP (r = 0.71, P less than 0.001) than to S-T-AP (r = 0.58, P less than 0.01). We concluded that S-L-AP predicts bone mineralization at organ level better than S-T-AP in selected metabolic bone disorders and that the supernatant activity shows no relation to bone turnover.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMedDate not supplied

Immunocytochemical typing of fine needle aspirates by means of alkaline phosphatase anti-alkaline phosphatase method. A study of 16 selected patients.

The immunocytochemical characterization of neoplastic cells recognized by a large panel of monoclonal antibodies in fine needle aspirates obtained from 16 subjects with superficial or profound tumoral masses of unknown origin was carried out using alkaline phosphatase anti-alkaline phosphatase (APAAP) immunoenzymatic method. The patients were selected on the basis of particular clinical criteria or since a correct cytohistological diagnosis was not available. APAAP immunophenotyping allowed to establish the existence of non-Hodgkin lymphoma in 6 cases, hairy cell leukemia in 1 case and carcinoma in 5 cases, while in other 2 patients the existence of Hodgkin's disease was suspected and subsequently confirmed; only in 2 subjects diagnostic informations were lacking. Furthermore, the evaluation of growth fraction by means of Ki 67 monoclonal antibody revealed a high degree of malignancy in all cases of lymphoma. Although some cautions have to be considered in the interpretation of results, APAAP immunocytochemical typing of fine needle aspirates appears a simple and reliable noninvasive diagnostic tool in selected patients.

Adult↗