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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↗
PubMed1986

Protein phosphorylation and oocyte maturation. II. Inhibition of starfish oocyte maturation by intracellular microinjection of protein phosphatases 1 and 2A and alkaline phosphatase.

Oocyte maturation (meiosis re-initiation) in starfish is induced by the natural hormone 1-methyladenine (1-MeAde). Following hormonal stimulation of the oocyte, an intracellular Maturation Promoting Factor (MPF) appears in the cytoplasm which triggers nuclear envelope breakdown and maturation divisions. Microinjection of pure preparations of the catalytic subunits of protein phosphatases 1 and 2A inhibits 1-MeAde-induced maturation in a dose-dependent manner. Calmodulin-dependent protein phosphatase 2B is inefficient. Maturation induced by mimetics of 1-MeAde, such as dithiothreitol (DTT), methylglyoxal-bis(guanylhydrazone) (MGBG), 8-hydroxyeicosatetraenoic acid (8 HETE) and arachidonic acid (AA) is also inhibited by these protein phosphatases. In all cases inhibition can be reversed by increasing the concentration of 1-Me-Ade or of mimetic. Alkaline phosphatase also inhibits maturation in a dose-dependent way and in a reversible manner. Microinjection of protein phosphatase is still effective when preformed long after the end of the hormone-dependent period, and can even be effective a few minutes before the breakdown of the nuclear envelope. No detectable MPF activity is found in 1-MeAde-treated phosphatase-injected oocytes. However, microinjection of phosphatase 2A simultaneously with MPF (obtained from 1-MeAde-treated donors) does not result in inhibition. These results constitute direct evidence for the necessity of an elevated level of phosphorylated proteins for MPF activity and maturation. The mode of action of 1-MeAde in inducing starfish oocyte maturation is discussed in relation to protein phosphorylation.

Adenine↗
PubMed1998

Isolation and properties of extracellular alkaline phosphatase from Bacillus intermedius.

Alkaline phosphatase (APase) was isolated from the culture liquid of the streptomycin-resistant strain of Bacillus intermedius S3-19 and purified as a homogeneous preparation by ion-exchange chromatography and FPLC. Electrophoresis and gel-filtration revealed that the active enzyme is a monomer with molecular weight of 46-47 kD. The enzyme possessed phosphomonoesterase and phosphodiesterase activities with maximal levels at pH 9.5 and 55 degreesC and was stable until 60 degreesC at pH 8.0-10.0. The isolated APase exhibits a broad specificity towards a wide variety of substrates. The effect of divalent metal ions and other reagents on its catalytic activities was studied. It was concluded that alkaline phosphatase of B. intermedius is similar to the secreted alkaline phosphatases from other Bacillus species in its physicochemical and catalytic properties.

Alkaline Phosphatase↗
PubMed2001

[Alkaline phosphatase].

High levels of alkaline phosphatase activity are characteristic of bone disease with increased osteoblastic activity, hepatobiliary disease with partial or complete biliary obstruction and transient hyperphosphatasemia in children. A gamma-glutamyl transpeptidase is often useful to differentiate whether an elevated alkaline phosphatase originates in the bones or the liver. A normal gamma-glutamyl transpeptidase suggests bone origin. A serum alkaline phosphatase isozyme pattern by electrophoresis is also necessary to differentiate various pathological states.

Alkaline Phosphatase↗
PubMed1978

Anomalous behaviour of control sera in automated versions of the Kind and King alkaline phosphatase method.

Differences in alkaline phosphatase activity of some commerical control sera were observed when comparing manual with AutoAnalyzer versions of the Kind and King procedure. This phenomenon was found to be associated with sera boosted with exogenous alkaline phosphatase and to be owing mainly to inadequate provision of buffer in some automated methods. It is suggested that a modification to the SMA procedure may lessen the problem, but the constraints of the system necessitate a compromise. There was better precision after the modification had been introduced. Awareness of this phenomenon is of paramount importance if commerical sera are to be used in any way in the calibration of automated systems for alkaline phosphatase assay.

Alkaline Phosphatase↗
PubMed1976

Cyclic changes of cervical mucus enzymes related to the time of ovulation. I. Alkaline phosphatase.

The concentration of alkaline phosphatase in cervical mucus was serially determined during a menstrual cycle in five normal ovulatory women and correlated with the time of ovulation as monitored by the basal body temperature and radioimmunoassay of serum lutenizing hormone (LH), progesterone, and estradiol. The activity of alkaline phosphatase decreased significantly at midcycle just prior to the LH surge and began to rise after ovulation. Self-detection of cervical mucus alkaline phosphatase may provide a practical method of ovulation prediction.

Adult↗
PubMed1975

Significance of elevated liver alkaline phosphatase in serum.

The serum alkaline phosphatase was fractionated by polyacrylamide gel electrophoresis in 317 patients with elevated serum alkaline phosphatase activity. In 253 patients the source of the elevation was the isoenzyme of presumed liver origin, band L. In 87 of these patients, there was either no obvious liver disease or the alkaline phosphatase elevation was inappropriately high. In 19 of the 87, liver disease was further excluded by liver biopsy or by laparotomy. Because of this, biochemical studies were done to verify the hepatic origin of band L. Band L and alkaline phosphatase extracted from human liver migrated together on polyacrylamide gel electrophoresis before and after digestion with Vibrio cholerae neuraminidase. They had identical pH optima, sedimentation coefficients, Michaelis constants, and rates of inactivation at 55.5 degrees C. They had different rates of inactivation in 3 M urea. Over-all, the data indicate that band L is of liver origin, and that elevation of the hepatic alkaline phosphatase isoenzyme may be a nonspecific finding in certain patients.

Alkaline Phosphatase↗
PubMed2002

Serum activities of tartrate-resistant acid phosphatase and bone specific alkaline phosphatase as indices of bone metabolism in the cow.

The correlation between the serum hydroxyproline concentration and serum activity levels of TRAP and BALP was examined in 41 cows. The correlated coefficient (r) was 0.6391 for TRAP and 0.3147 for BALP, respectively. Judging from the significant correlation to the serum hydroxyproline concentration, serum TRAP activity is an index for bone metabolism in cows. Serum TRAP activity was therefore measured in 205 healthy cows (2-9 years old) in order to observe the changes in bone resorption with aging and milk production. TRAP levels differed slightly between group A (< or =4 yrs) and B (5 yrs< or =) at the same stage of lactation. The activity levels rose slightly at the height of lactation stage and during the dry stage.

Acid Phosphatase↗
PubMed1996

Bone alkaline phosphatase isoenzyme in renal osteodystrophy.

Serum total alkaline phosphatase is the most commonly used biochemical marker of bone disease in renal patients, but alkaline phosphatase originates from different organs and sometimes lacks specificity. Bone isoenzyme measurement is considered superior to total alkaline phosphatase for the assessment of bone metabolism. We have studied the value of bone isoenzyme, determined by a new. IRMA (Tandem-R-Ostase), in haemodialysis patients with secondary hyperparathyroidism and renal osteodystrophy. Fifty-six haemodialysis patients were studied. Intact parathyroid hormone (PTH), osteocalcin, total alkaline phosphatase and bone alkaline phosphatase were determined. A transiliac bone biopsy was performed in 20 of the 56 patients after double tetracycline labelling. There was a significant correlation between bone alkaline phosphatase and PTH (r = 0.79, P < 0.001) and between bone and total alkaline phosphatase (r = 0.84, P < 0.001) in all patients. The patients who underwent a bone biopsy showed osteitis fibrosa in 17, mixed lesion in one, adynamic bone disease in one and normal bone in one. Bone alkaline phosphatase showed a significant correlation with static and dynamic histomorphometric indices similar to that obtained with PTH and better than those of total alkaline phosphatase and osteocalcin. It is concluded that bone alkaline phosphatase (ostase) seems to be a useful non-invasive marker of bone metabolism in patients on haemodialysis with high turnover bone disease. More studies are necessary to know its value in low turnover bone disease.

Adult↗
PubMed1982

Chick embryo intestine in culture: influence of insulin and other hormones on sucrase, maltase, and alkaline phosphatase.

The development of alkaline phosphatase, maltase, and sucrase activities in the duodenum of the chick embryo was followed in organ culture in chemically defined medium; 14-day duodenum was used in most experiments, with comparisons being made with 18-day tissue. As has been previously shown for the other enzymes, sucrase activity also rises at an accelerated rate in vitro. Since chick sucrase has maltase activity, its increase appears to account for the spontaneous rise of maltase activity; the form of maltase devoid of sucrase activity seems not to be accelerated. Sucrase, sucrase-free maltase, and alkaline phosphatase are all elevated by the addition of insulin to the medium. Intestinal sucrase is well known to be responsive to hydrocortisone, but it has now been found to be unresponsive to thyroxine, except that its dissociation from the brush border is increased at hormone concentrations above 1 nM. Insulin and thyroxine act synergistically on alkaline phosphatase, but the addition of hydrocortisone diminishes the effect of the other two. With sucrase, insulin and hydrocortisone have a synergistic effect which is intensified by addition of thyroxine. The previously demonstrated influence of hydrocortisone on maltase is accounted for by the maltase activity of sucrase. In combination, however, hydrocortisone and thyroxine elevated maltase much more strongly than sucrase, and the highest maltase levels were attained when all three hormones were present.

Alkaline Phosphatase↗