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PubMed1978

Tumour production of alkaline phosphatase in a patient with giant-cell carcinoma of bronchus.

A patient with a giant-cell carcinoma of the bronchus was found to have a raised serum alkaline phosphatase without any evidence of bone or liver involvement. After necropsy the excised tumour was found to be producing alkaline phosphatase. The alkaline phosphatase found in the serum during life was heat-labile but that in the tumour was heat-stable. The significance of this is unknown.

Alkaline Phosphatase↗
PubMed1975

Possible identity between the hepatoma alkaline phosphatase and an isozyme of human amniotic membrane (FL cells).

The electrophoretically faster migrating alkaline phosphatase isozyme in FL cells derived from the human amniotic membrane was similar in some of the enzymatic and immunochemical properties to the variant alkaline phosphatase which occurs in serum and cancerous tissue of some patients with hepatocellular carcinoma. These facts suggest that the hepatoma-associated alkaline phosphatase may be the resurgence of the isozyme originally present in the amniotic membrane.

Alkaline Phosphatase↗
PubMed1967

Origins of serum alkaline phosphatase.

A very rapid method of agar gel electrophoresis on glass slides, together with a superior visualization technique employing simultaneous coupling of a hydrolysed naphthol substrate, have been developed for the identification of the tissues of origin of serum alkaline phosphatase. Combined with L-phenylalanine inhibition, specific for the intestinal enzyme, and heat inactivation, specific for the placental enzyme, the heterogeneity of serum alkaline phosphatase has been demonstrated. Normal adult serum contains predominantly liver-type alkaline phosphatase with a small but variable quantity of intestinal enzyme, and little or no bone enzyme. In childhood and in infancy there is in addition a bone isoenzyme present, the amount gradually falling to adult levels with age. In pregnancy, the rise in serum alkaline phosphatase is due to the placental enzyme.A study of nearly 2,000 sera has been undertaken and it is found that the bone enzyme is increased in osteoblastic bone diseases while in hepato-biliary disorders there is an increase in liver type enzyme. The main theories explaining the rise in serum alkaline phosphatase are examined.

Adult↗
PubMed1985

Evidence for homology of normal and neoplastic human placental alkaline phosphatases as determined by monoclonal antibodies to the cancer-associated enzyme.

The HeLa TCRC-1 human adenocarcinoma cell line expresses a form of alkaline phosphatase that is similar to the common S-variant of placental alkaline phosphatase (PLAP) on the basis of electrophoretic mobility, catalytic properties, and reactivity with polyclonal antibodies. More sensitive probes of changes in protein structure than polyclonal antibodies are monoclonal antibodies (MAbs) which recognize individual antigenic sites on molecules. Therefore, we produced MAbs to HeLa TCRC-1 cells and selected those which bound to the alkaline phosphatase expressed by the cancer cells. Seven MAbs were obtained and characterized by (a) fine specificity analysis using allelic variants of PLAP and other human alkaline phosphatase isozymes, (b) immunoglobulin isotype, and (c) relative binding affinities to PLAP from two sources, placental tissue and HeLa TCRC-1 cells. The seven MAbs bind the enzymes from both sources with equal affinity indicating a high degree of structural homology if not identity between the normal S-variant of PLAP and its cancer-associated counterpart. We note that most of the MAbs to cancer cell surface-bound PLAP express either Ig (immunoglobulin) G2a or IgG2b heavy-chain isotypes, a higher incidence of these classes of IgG than has been observed with the purified and soluble PLAP immunogen which yields MAbs predominantly of the IgG1 isotype. Finally, some of these antibodies, like the ones prepared from purified PLAP, recognize differences between allelic variants.

Adenocarcinoma↗
PubMed1988

[Effect of the protonophore carbonylcyanide-m-chlorophenylhydrazone on the localization of secreted alkaline phosphatase in E. coli].

It was shown that the total amount of synthesized alkaline phosphatase as well as the value of enzymatic activity in E. coli cells decrease in the presence of the protonophore, carbonylcyanide-m-chlorophenylhydrazone. The enzyme content in the periplasm also decreases, while the amount of the enzyme bound to the spheroplasts increases. This effect is enhanced with a rise in the protonophore concentration. An electron cytochemical analysis showed that in the presence of the protonophore, alkaline phosphatase is partly localized in the cytoplasm and on the inner surface of the cytoplasmic membrane, which is unobserved in control cells. It was assumed that carbonylcyanide-m-chlorophenylhydrazone suppresses the translocation of alkaline phosphatase across the cytoplasmic membrane and enzyme biosynthesis, on the whole.

Alkaline Phosphatase↗
PubMedDate not supplied

[Inhibition of alkaline phosphatase I of Pichia guilliermondii yeast in vitro and in vivo].

The rate of p-nitrophenyl phosphate and flavin mononucleotide (FMN) hydrolysis by the partially purified preparation of alkaline phosphatase I of Pichia guilliermondii flavinogenic yeast was studied as affected by different substrates and inorganic ions. Their Km was established to be 2.0 X 10(-4) m and 2.5 X 10(-4) M, respectively. Dephosphorylation of p-nitrophenylphosphate and FMN was inhibited competitively by beta-glycerophosphate (Ki = 3.1 X 10(-3) M, respectively). The presence of inorganic phosphate ions in the reaction mixture decreases or removes inhibition of these compounds hydrolysis by other substrates of alkaline phosphatase I. The activity of alkaline phosphatase I increases in the presence of Mg2+ and was strongly inhibited in the presence of Be2+, Cu2+, Zn2+, Cd2+ and inorganic phosphate, the mixture of Be2+ and F- being the most effective. This mixture inhibited the phosphatase activity of the partially purified preparation of alkaline phosphatase I of the cell-free extract as well as of intact cells in both the alkaline and acid zones of pH (8.6 and 5.5, respectively). Incubation of the washed iron-deficient P. guilliermondii cells in the presence of Be2+ and F- did not result in accumulation of FMN in the yeast culture. A possible role of nonspecific phosphomonoesterases in hydrolysis of FMN in vivo is discussed.

4-Nitrophenylphosphatase↗
PubMed1989

Biochemical data and diagnoses--a novel use for alkaline phosphatase.

In biochemical profiles of bone and liver diseases, alkaline phosphatase values range in a continuum from within the normal range to grossly elevated as disease states evolve. The way that raised values of alkaline phosphatase, from 438 consecutive adult cases followed prospectively, were treated by the requesting clinicians during the course of a hospital admission, and for a two-month follow-up period, was used as a guide to data wastage to determine an analyser policy appropriate for the introduction of computerised interpretative reporting. There was sufficient clinical and biochemical data in 67 per cent of cases to suggest a diagnosis. A basic chemistry profile appears necessary for interpretative reporting, and 'random access' is best employed in the 'stat' mode and also in follow-up monitoring.

Alkaline Phosphatase↗
PubMed1992

Initial effects of partially purified bone morphogenetic protein on the expression of glycosaminoglycan, collagen, and alkaline phosphatase in nonunion cell cultures.

Bone morphogenetic protein (BMP) stimulates mesenchymal cells to differentiate, resulting in de novo endochondral ossification in vivo. The response of fibrocartilage and periosteal cells from human and canine nonunion tissues to partially purified BMP was examined in culture. Cells derived from neonatal rat muscle explants were used for comparison. Alkaline phosphatase activity and expression of alkaline phosphatase and Types I and II collagen mRNAs were compared to that of rat chondrocytes. Synthesis of Type II collagen by the muscle cells was verified by enzyme-linked immunosorbent assay (ELISA). Addition of BMP to the muscle cell and nonunion cell cultures resulted in a dose-dependent decrease in cell number. There was a decrease in matrix vesicle and plasma membrane alkaline phosphatase activity concomitant with an increase in mRNA levels for alkaline phosphatase and collagen genes. Synthesis of immunoreactive Type II collagen increased. These data indicate that neonatal rat muscle cells and nonunion cells may respond in a similar fashion to BMP. Bone morphogenetic protein stimulated hyaluronic acid synthesis at three days, but chondroitin sulfate synthesis did not increase until ten days exposure to BMP. These data, together with those summarized above, suggest that more than three days may be required for complete expression of the chondrocyte phenotype typical of endochondral ossification.

Alkaline Phosphatase↗
PubMed1978

Factors affecting measurement of total alkaline phosphatase activity in human serum, especially wavelength accuracy.

Serum alkaline phosphatase estimations by the Selected Method [Clin. Chem. 21, 1988 (1975)] are very sensitive to small errors in the wavelength setting of the spectrophotometer. With a setting error as small as 3 nm, results can be too low by as much as 23%. The product of the reaction, 4-nitrophenol, can be prepared in very pure form and can be used to check both the wavelength and absorbance accuracy of a spectrophotometer. The molar absorptivity for 4-nitrophenol obtained in the instrument being used should be used in calculating alkaline phosphatase activities.

Alkaline Phosphatase↗
PubMed1977

Source and significance of serum alkaline phosphatases in diseases of the locomotor system.

A group of 292 patients with diseases of the locomotor system was examined. Elevated activity of the liver isoenzyme of serum alkaline phosphatase was found in rheumatoid arthritis. Evaluation of the alkaline phosphatase isoenzyme in these states is especially important for studying nonspecific irritation of the liver tissue as a result of long-term therapy. Significantly elevated bone isoenzyme activity was found in Paget's disease, ankylosing spondylitis and osteoporomalacia, gout, the hyperuricaemic syndrome and some osteoarthroses. In these states, study of the alkaline phosphatase isoenzymes is of particular significance in evaluation of the development of metabolic bone changes. An association between elevated bone and intestinal isoenzyme activity was found. The diagnostic value of the determination of serum alkaline phosphatase is multiplied if the isoenzymes are also evaluated.

Adult↗
PubMed1978

Characteristics of the inhibition of serum alkaline phosphatase by theophylline.

1. The effect of various parameters on the inhibition of alkaline phosphatase activity by theophylline was studied. The influence of pH is great, being optimum for a value of 9.4. The temperature and the magnesium ion concentration have no to low effect. 2. The nature of the substrate and the nature of the buffer in which the enzymatic activity is measured have an effect:by measuring the activity of alkaline phosphatase in serum by a method with phenolphthaleinphosphate in Tris buffer, a negligible interference by therapeutic or toxic levels of theophylline is observed. 3. The inhibition by theophylline varies greatly with the origin of alkaline phosphatase: the liver isoenzyme is strongly inhibited, the intestinal one to a lesser degree and the placental isoenzyme almost not inhibited. 4. The inhibition of the liver and intestinal isoenzymes are uncompetitive and the inhibition constants were measured.

Alkaline Phosphatase↗
PubMed1976

[Adrenaline-induced release from thrombocytes of beta-lipoprotein, alkaline phosphatase and 5'-nucleotidase].

Platelet aggregation induced by adrenaline is accompanied by release of beta-lipoprotein, alkaline phosphatase, 5'-nucleotidase and factor 3. Electrophoretic mobility of platelet alkaline phosphatase was the same as that of beta-lipoprotein. This suggest that beta-lipoprotein, alkaline phosphatase and 5'-nucleotidase are structural components of platelet compounds which possess factor 3 activity.

Alkaline Phosphatase↗
PubMedDate not supplied

Modifications induced by ascorbic acid on alkaline phosphatase fluorescence.

Ascorbic acid, isoascorbic acid and dehydroascorbic acid quench the tryptophyl fluorescence of alkaline phosphatase. The quenching is protein aspecific, although its extent reflects the different inhibitory efficiency of the compounds. The kinetic inactivation and emission deactivation of alkaline phosphatase isoenzymes present also striking similarities. The fluorescence modifications, moreover, show a particular pattern, indicative of a transition phenomenon. The quenching effects displayed by the ascorbic system on alkaline phosphatase can then supply an interesting insight into other aspects of the inhibitor-enzyme interaction.

Alkaline Phosphatase↗
PubMed1986

Properties of Na+/K+ ATPase and alkaline phosphatase alter during spontaneous and radiation-induced leukemogenesis in mice.

We characterized properties of Na+/K+ ATPase and alkaline phosphatase in thymocytes or thymoblasts from mice of two strains: AKR, in which thymoma developed spontaneously and C57Bl, in which the development was induced by X-irradiation (total dose: 5.4 Gy in 3 fractions). We found that before thymoma could be discerned morphologically--properties of the two enzymes altered. There was a decrease in 86Rb uptake and in the rate of ATP hydrolysis per cell (both strains) as well as an increase in alkaline phosphatase activity per cell (C57Bl mice). In both spontaneous and radiation-induced thymomas 86Rb uptake, ATP hydrolysis and 3H-ouabain binding per cell were higher than in normal thymuses. Likewise, alkaline phosphatase activity per cell was higher in thymomas than in thymuses; this increase was accompanied by the appearance of additional isoenzyme(s) (1 in AKR, 2 in C57Bl). These changes were compared with cAMP content and 3H-thymidine incorporation, taken as indicators of the proliferative activity, and their high correlation in both AKR and C57Bl mice allowed to distinguish a pre-leukemic period. In that period thymoblasts clearly differed from the normal ones in Na+/K+ ATPase and alkaline phosphatase properties, as well as proliferation, although the morphology of the thymus was still unchanged.

Age Factors↗
PubMed1979

Comparison of human alkaline phosphatase isoenzymes. Structural evidence for three protein classes.

The structural relationships among human alkaline phosphatase isoenzymes from placenta, bone, kidney, liver and intestine were investigated by using three criteria. 1. Immunochemical characterization by using monospecific antisera prepared against either the placental isoenzyme or the liver isoenzyme distinguishes two antigenic groups: bone, kidney and liver isoenzymes cross-react with anti-(liver isoenzyme) serum, and the intestinal and placental isoenzymes cross-react with the anti-(placental isoenzyme) antiserum. 2. High-resolution two-dimensional electrophoresis of the 32P-labelled denatured subunits of each enzyme distinguishes three groups of alkaline phosphatase: (a) the liver, bone and kidney isoenzymes, each with a unique isoelectric point in the native form, can be converted into a single form by treatment with neuraminidase; (b) the placental isoenzyme, whose position also shifts after removal of sialic acid; and (c) the intestinal isoenzyme, which is distinct from all other phosphatases and is unaffected by neuraminidase digestion. 3. Finally, we compare the primary structure of each enzyme by partial proteolytic-peptide 'mapping' in dodecyl sulphate/polyacrylamide gels. These results confirm the primary structural identity of liver and kidney isoenzymes and the non-identity of the placental and intestinal forms. These data provide direct experimental support for the existence of at least three alkaline phosphatase genes.

Adolescent↗
PubMed1988

Circulating levels of 1,25 dihydroxyvitamin D, alkaline phosphatase, hydroxyproline, and osteocalcin associated with antler growth in white-tailed deer.

Alkaline phosphatase, hydroxyproline, osteocalcin, and 1,25(OH)2D were measured in biweekly serum samples obtained from 6 adult (greater than 4 years), 4 juvenile (1-4 years) and 4 fawn (less than 1 year) male white-tailed deer from Oct. 1983 to Oct. 1984. Antler length, from the pedicle to the tip, was measured at the time of serum sampling. Serum alkaline phosphatase activity and levels of hydroxyproline and osteocalcin were higher (P less than 0.05) in fawns compared with juveniles and adults reflecting increased bone metabolism in the younger deer. In adult deer serum alkaline phosphatase activity and hydroxyproline levels were elevated (P less than 0.05) during the period of antler growth, whereas serum osteocalcin and 1,25(OH)2D increased (P less than 0.05) during antler mineralization. Similar but less pronounced trends occurred in juvenile deer, possibly a reflection of skeletal growth in the younger animals. The data lend support for utilization of the deer antler cycle as a model for studies of bone disorders. Further work is needed to help clarify the role of hydroxyproline, osteocalcin, and 1,25(OH)2D in the antler cycle.

Age Factors↗