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PubMed1976

Purification and characterization of alkaline phosphatase from rat kidney.

Alkaline phosphatase [EC 3.1.3.1.] was purified about 250-fold from rat kidney, and its enzymological properties were studied. Kidney homogenate was extracted with n-butanol, passed through Sephadex G-200 and chromatographed on a DEAE-cellulose column. The peak from the DEAE-cellulose column was subjected to isoelectric focusing, and the alkaline phosphatase activity was separated into two peaks. The molecular weights of alkaline phosphatase in these peaks were 4.8.X10(4) and 1.0X10(5), as determined by SDS-polyacrylamide gel electrophoresis. Anti-serum against alkaline phosphatase from rat kidney was prepared, and was shown to neutralize the activity from kidney, liver or bone, but not that from intestine.

Alkaline Phosphatase↗
PubMed1990

Acid and alkaline phosphatase in bovine antral follicles.

Acid and alkaline phosphatases were measured in the follicular fluid of 766 individual follicles from 96 cows. Follicles were obtained by bilateral ovariectomy or at slaughter from animals at various stages of the estrous cycle and pregnancy. Mean follicle size varied with the physiological state of the cow (P less than .0001). Acid phosphatase activity (U/microliters) varied inversely with follicle size (P less than .001) but not with stage of the estrous cycle or gestation. Total acid phosphatase activity per follicle increased with follicle size (P less than .05). Neither acid phosphatase nor alkaline phosphatase concentration was associated with atresia. Alkaline phosphatase activity (U/microliters) was greater in the smallest follicles (less than 50 microliters) than in other size groups (P less than .0001). Alkaline phosphatase activity (U/microliters) was greater (P less than .05) during the preovulatory phase of the estrous cycle than during other phases. A high concentration of follicular fluid phosphatases cannot be used as a marker for atresia but is characteristic of healthy small antral follicles.

Acid Phosphatase↗
PubMed1993

Changes in cell adhesion and cell proliferation are associated with expression of tissue non-specific alkaline phosphatase.

Tissue non-specific alkaline phosphatase is a membrane-bound glycoprotein enzyme which is characterized by its phosphohydrolytic, protein phosphatase, and phosphotransferase activities. This enzyme is distributed virtually in all mammalian tissues, particularly during embryonic development. Its expression is stage-specific and can be demonstrated in the developing embryo as early as the 2-cell stage. It has been suggested that tissue non-specific alkaline phosphatase might play a role in tissue formation. In the study reported here, a gene-transfer approach was employed to investigate possible roles for this enzyme by inserting the cDNA for rat tissue non-specific alkaline phosphatase into CHO and LLC-PK1 cells. Permanently transfected cell-lines expressing varying levels of alkaline phosphatase were established. The data showed that functional enzyme was expressed in the transfected cells. Cell spreading and attachment were enhanced in transfected CHO cells expressing high levels of tissue non-specific alkaline phosphatase but not in the LLC-PK1 cells. Further, in CHO cells, proliferation was shown to be inversely proportional to the level of the tissue non-specific alkaline phosphatase expression. Homotypic cell association was demonstrated in both alkaline phosphatase-positive and alkaline phosphatase-negative cells in both CHO and LLC-PK1 cell-lines. Taken together, these findings suggest that in addition to a role in mineralization of bone, tissue non-specific alkaline phosphatase might also play a role in other cell activities, including those related to differentiation, such as cell-cell or cell-substrate interaction and proliferation.

Alkaline Phosphatase↗
PubMed1983

Solubility properties of alkaline phosphatase from matrix vesicles.

Alkaline phosphatase has been extracted from matrix vesicles of a calcifying cartilage with 0.15 M KCl, 0.4 M guanidinium chloride and 0.05 M deoxycholate/50% butanol mixture. The catalytic properties of the three extracts have been compared. Although the highest amount of enzyme activity is extracted with the latter reagent (55%), some of it is also extracted with KCl (11%) and guanidinium (7%). By submitting isolated matrix vesicles to a short time sonication the distribution pattern of the alkaline phosphatase activity in the extracts is clearly modified, as the amount extracted with KCl increases from 14 to 50% and the portion extracted with deoxycholate decreases from 55 to 27% of the total enzyme activity of matrix vesicles. The enzymatic preparations were comparable on the basis of specific activities, affinity for the substrates (p-nitrophenylphosphate, ATP), thermostability, sensitivity to inhibitors and activators. By electrofocusing a value of pI = 4.15 was found for the alkaline phosphatase of matrix vesicles independently of the extraction medium. These results contradict the concept that alkaline phosphatase is exclusively an intrinsic membrane protein.

4-Nitrophenylphosphatase↗
PubMed1993

[Analysis of abnormal alkaline phosphatase in patient with high alkaline phosphatasemia].

We describe here a 69-year-old male with high serum alkaline phosphatase (ALP) activity who was showed high alkaline phosphatasemia. High ALP level, 112.4 K.A. was found in his serum. But, except for ALP, all other laboratory data including cancer markers were within normal range in this case. An electrophoretic pattern of patient ALP isozyme without neuroaminidase digestion showed liver-type ALP, but the ALP isozyme pattern with neuraminidase digestion from Vibrio Cholerae was identified as bone-type ALP. Moreover, the patient ALP reacted with anti-bone ALP MoAb. The apparent molecular size of patient ALP was 160kDa similar to bone ALP. Furthermore, we investigated the multiformity of the sugar chain(s) of patient ALP by serious lectin affinity chromatographies. From these results, the increase of multiantennary complex type and/or bisecting GlcNAc type sugar chain(s) of ALP was shown in patient serum. These results suggested that the patient might have a distant metastasis as in a case of carcinoembryonic antigen described previously. Besides, patient urinary pyridinoline and deoxypyridinoline was high level comparing normal adult urine. From detailed bone survey, the patient was observed the bone metastasis of cancer. Thus, the measurement of ALP sugar chain subfractions may be useful for diagnosis of patient with bone metastasis of cancer.

Aged↗
PubMed2006

Beneficial effects of alkaline phosphatase in septic shock.

OBJECTIVE: Alkaline phosphatase may decrease the harmful effects of lipopolysaccharide by detoxifying lipid A. The aim of this study was to investigate whether administration of alkaline phosphatase is beneficial in a clinically relevant septic shock model. DESIGN: Interventional laboratory study. SETTING: University hospital animal research laboratory. SUBJECTS: Fourteen fasted, anesthetized, invasively monitored, mechanically ventilated, female sheep (27.6 +/- 3.9 kg). INTERVENTIONS: Each animal received 1.5 g/kg body weight of feces intraperitoneally to induce sepsis. Ringer's lactate and a 6% hydroxyethyl starch solution were infused throughout the experiment to prevent hypovolemia. Two hours after feces injection, animals were randomized to alkaline phosphatase (60 units/kg intravenous bolus followed by a continuous infusion of 20 units/kg/hr for a total of 15 hrs) or no alkaline phosphatase (control group). MEASUREMENTS AND MAIN RESULTS: All animals were studied until their spontaneous death or for a maximum of 30 hrs. Plasma alkaline phosphatase concentrations decreased in the control group but increased in the treatment group following alkaline phosphatase administration. In the treatment group, the Pao2/Fio2 ratio was higher (p < .05), blood interleukin-6 concentrations were lower (p < .05), and the survival time was longer (median time 23.8 vs. 17 .0 hrs, p < 0.05) than in the control group. There were no significant differences in systemic hemodynamics or diuresis. CONCLUSIONS: In this clinically relevant septic shock model, alkaline phosphatase administration improved gas exchange, decreased interleukin-6 concentrations, and prolonged survival time.

Alkaline 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↗
PubMed1973

Inorganic phosphate transport in Escherichia coli: involvement of two genes which play a role in alkaline phosphatase regulation.

Two classes of alkaline phosphatase constitutive mutations which comprise the original phoS locus (genes phoS and phoT) on the Escherichia coli genome have been implicated in the regulation of alkaline phosphatase synthesis. When these mutations were introduced into a strain dependent on a single system, the pst system, for inorganic phosphate (P(i)) transport, profound changes in P(i) transport were observed. The phoT mutations led to a complete P(i) (-) phenotype in this background, and no activity of the pst system could be detected. The introduction of the phoS mutations changed the specificity of the pst system so that arsenate became growth inhibitory. Changes in the phosphate source led to changes in the levels of constitutive alkaline phosphatase synthesis found in phoS and phoT mutants. When glucose-6-phosphate or l-alpha-glycerophosphate was supplied as the sole source of phosphate, phoT mutants showed a 3- to 15- fold reduction in constitutive alkaline phosphatase synthesis when compared to the maximal levels found in limiting P(i) media. However, these levels were still 100 times greater than the basal level of alkaline phosphatase synthesized in wild-type strains under these conditions. The phoS mutants showed only a two- to threefold reduction when grown with organic phosphate sources. The properties of the phoT mutants selected on the basis of constitutive alkaline phosphatase synthesis were similar in many respects to those of pst mutants selected for resistance to growth inhibition caused by arsenate. It is suggested that the phoS and phoT genes are primarily involved in P(i) transport and, as a result of this function, play a role in the regulation of alkaline phosphatase synthesis.

Alkaline Phosphatase↗
PubMed1980

Kinetics and regulation of cell-free alkaline phosphatase synthesis.

Regulation of alkaline phosphatase (EC 3.1.3.1) synthesis in a cell-free system from Escherichia coli has been observed. Synthesis from transducing phage deoxyribonucleic acid templates carrying phoA+ occurred in S30 fractions from wild-type or alkaline phosphatase-constitutive mutants. It did not occur in S30) fractions from alkaline phosphatase-negative mutants (phoB). The hybrid gene phoA-lacZ was also subject to phoB control, implying that phoA transcription is regulated. The yield of active alkaline phosphatase per phoA+ gene copy from cell-free synthesis was similar to that of beta-galactosidase. Alkaline phosphatase activity took longer to appear than beta-galactosidase activity. Synthesis of alkaline phosphatase subunits was not delayed, suggesting that a minimum number of subunits are synthesized before formation of active alkaline phosphatase occurs.

Alkaline Phosphatase↗
PubMed1994

Posttranslational heterogeneity of bone alkaline phosphatase in metabolic bone disease.

Bone alkaline phosphatase is a marker of osteoblast activity. In order to study the posttranscriptional modification (glycosylation) of bone alkaline phosphatase in bone disease, we investigated the relationship between mass and catalytic activity of bone alkaline phosphatase in patients with osteoporosis and hyperthyroidism. Serum bone alkaline phosphatase activity was measured after lectin precipitation using the Iso-ALP test kit. Mass concentration of bone alkaline phosphatase was determined with an immunoradiometric assay (Tandem-R Ostase). In general, serum bone alkaline phosphatase mass and activity concentration correlated well. The activity : mass ratio of bone alkaline phosphatase was low in hyperthyroidism. Activation energy of the reaction catalysed by bone alkaline phosphatase was high in osteoporosis and in hyperthyroidism. Experiments with neuraminidase digestion further demonstrated that the thermodynamic heterogeneity of bone alkaline phosphatase can be explained by a different glycosylation of the enzyme.

Adult↗
PubMed1987

Detection of chlamydial inclusions in cell culture or biopsy tissue by alkaline phosphatase-anti-alkaline phosphatase staining.

An immunological technique for detecting Chlamydia trachomatis and Chlamydia psittaci inclusions in infected McCoy cell cultures was developed by using a genus-specific monoclonal antibody to Chlamydia spp., rabbit anti-mouse immunoglobulin G bridging antibody, alkaline phosphatase-anti-alkaline phosphatase (APAAP) monoclonal antibody conjugate, and naphthol AS-phosphate/fast red substrate. Chlamydial inclusions stained red and were easily detected against a background of blue hematoxylin-stained nuclei. After 18 h, inclusions of C. trachomatis serovar L2 LGV434/Bu and C. psittaci strain 6BC were stained by APAAP but not by iodine or Giemsa. At 48 h inclusion counts were significantly higher in the APAAP cultures. Both the APAAP procedure and conventional staining detected 35 of 239 (15%) cultures 48 h after inoculation with urethral or endocervical specimens. However, at 24 h after inoculation 22 of 35 (63%) were positive by APAAP staining while negative by iodine. This immunostain also allowed identification of chlamydial inclusions in endometrial biopsies from patients with tubal factor infertility or pelvic inflammatory disease.

Alkaline Phosphatase↗
PubMed1976

Comparative prognostic value of serum placental and tissue oxytocinase, alkaline phosphatase and its heat-stable fraction in pregnancy at neuroendocrinological risk.

Serum enzyme determinations are now well-established diagnostic tools in so-called "placental insufficiency". A good predictability of oxytocinases (P-CAP-placental oxytocinase and T-CAP-tissue oxytocinase) and a doubtful one of those of phosphatases (AP-alkaline phosphatase, HSAP-heat stable alkaline phosphatase) has been shown in high-risk pregnancies. The purpose of this study was to determine the prognostic value of the above cited enzymes in the so-called "pregnancy at neuroendocrinological risk", i.e. pregnancy in women with a prepregnancy history of hormonal disorders. It was shown that the outcome and results of such pregnancies are poorer that those of normal pregnancies. The series studied comprised 364 pregnant patients with pregnancy at neuroendocrinological risk that were being monitored by means of serum assays of the four enzymes. An attempt was made to assess each of these enzyme activities both in single (at least one value below 2.5 percentile calculated for healthy subjects) and serial determinations (two consecutive results decreasing or remaining at the same level). Normal and abnormal enzyme results were compared with normal and abnormal conditions of the newborn. The results presented showed that P-CAP (Tab. I) and T-CAP (Tab. II) levels were useful in prenatal diagnosis of fetal impairment in heneral, in addition to perinatal mortality and low values of the APGAR score. Neither the single nor serial assays of AT (Tab. III) and HSAP (Tab. IV) were valuable in predicting birth of an impaired neonate. Sensitivity of the test, i.e. percentage of women with abnormal enzyme assays among those patients who gave birth to impaired neonates, and specificity of the test, i.e. the percentage of women delivered of impaired neonates among all women with abnormal enzyme assays, of the four enzymes were compared. Sensitvity and specificity of P-CAP and T-CAP were higher than those for AP and HSAP. Moreover, sensitivity for all four enzymes was higher in serial assays, and specificity was higher in single assays. The results of the present analysis demonstrated the prognostic value of oxytocinase assays also in the pregnancy at neuroendocrinological risk. Assays of P-CAP and T-CAP were of equal significance, notwithstanding reports of a greater usefulness of P-CAP. Assays of CAP were helpful particularly in the conditions on which neuroendocrinological gestosis exerts a direct influence, i.e. in low Apgar score and perinatal mortality. On the other hand, serum alkaline phosphatases proved useless in endocrine pathology of pregnancy and HSAP was not superior to AP. About one half of future mothers of impaired neonates had enzyme results outside the range of the assays under consideration. This could be explained by the fact that these enzymes activities reflect placental function and are not directly related to fetal metabolism. Because of that they should be supplemented by other diagnostic methods being used in a clinic of high-risk pregnancy.

Alkaline Phosphatase↗
PubMed1979

Characterization of alkaline phosphatases from human first trimester placentas.

Alkaline phosphatase from human first trimester placentas was purified, characterized, and compared with alkaline phosphatases from term placenta and liver. Three forms of first trimester placental alkaline phosphatase (I, IIa, and IIb) were isolated; their relative amounts were 35%, 39%, and 26%, respectively. Phosphatases I and IIa were found to be dimers, whereas phosphatase IIb appeared to be a tetramer consisting of two dimers of phosphatase I or IIa. Phosphatase I was indistinguishable from liver phosphatase by several criteria including apparent molecular weight (Mr = 165,000), size of the monomeric subunit (Mr = 77,000), heat liability, insensitivity to inactivation by antiserum against term placental alkaline phosphatase, and sensitivity to inactivation by antiserum against liver alkaline phosphatase. In addition, phosphatase I and liver phosphatase were equally sensitive to inhibition by amino acids, levamisole, l-p-bromotetramisole, and EDTA. Phosphatase IIa, in contrast, was indistinguishable from term placental alkaline phosphatase by the same criteria: apparent molecular weight (Mr = 115,000), size of the monomeric subunit (Mr = 63,000), heat stability, inactivation by antiserum against term placental alkaline phosphatase, and sensitivity to inhibition by various compounds. These findings clearly demonstrate the existence of two distinct placental alkaline phosphatases, one (phosphatase I) specific for the first trimester placenta and the other (phosphatase IIa) occurring in both first trimester and term placentas.

Alkaline Phosphatase↗
PubMed1985

Evidence for two isozymes of leukocyte alkaline phosphatase in leukemic leukocytes.

Leukocyte alkaline phosphatase (LAP) is a granulocyte enzyme whose level of expression is markedly altered in various disease states. We have characterized LAP from normal cells and leukemic cells with a high level of LAP activity in order to determine whether increased enzyme levels are caused by increased levels of the same enzyme or induction of a different alkaline phosphatase. Leukocyte alkaline phosphatase was purified from normal granulocytes and from leukemic cells of a patient with chronic granulocytic leukemia (CGL) in blast phase with an elevated LAP level. LAP was partially purified utilizing diethylaminoethyl (DEAE)-cellulose ion exchange chromatography, gel filtration, and preparative electrophoresis. The sample prepared from normal granulocytes contained a single protein with LAP activity having a molecular weight of 61,000 as determined by SDS gel electrophoresis. The sample from the CGL blast-phase cells, however, demonstrated two proteins with alkaline phosphatase activity, one with a molecular weight of 61,000 (LAPs) and one with a molecular weight of 45,000 (LAPf). Differential heat inactivation and distinct isoelectric points of the two isozymes suggest that they are different proteins. We interpret our data to suggest two closely related LAP alleles whose expression is controlled independently. This may represent either genetic heterogeneity or induction of "tumor marker" gene expression.

Alkaline Phosphatase↗