Acid phosphatase mouse

The changes in calvarial phosphatase activities observed in animals treated with 25-(OH)D3 are totally different from those obtained with either 1.25-(OH)2D3 or 24.25—(OH)2D3. This fact indicates that physiological doses of 25-(OH)D3 may have an effect on cellular activity, independent of the conversion of this metabolite into these dihydroxyderivatives. The various effects of these vitamin D3 metabolites cannot be correlated with changes in serum calcium and/or phosphate concentrations. Among those factors other than serum calcium and phosphate concentrations that may be involved in the mechanism of action of vitamin D3 metabolites on bone phosphatase activities, the parathyroid hormone is of importance. This hormone is known to be a potent activator of bone phosphatases223,224,228. Parathormone increases the content of alkaline, neutral and acid phosphatases in mouse calvaria in vitro. Calcitonin does not prevent the increase of those enzymes while dichloromethylene diphosphonate causes a decrease in acid phosphatase and pyrophosphatase226. ... 

Mouse liver acid phosphatase is localized in the Kupffer cells in contrast to the alkaline phosphatase activity which is largely confined to the endothelial linings of the sinusoids. Under the conditions in which the activity of the reticuloendothelial system is enhanced, both enzymic activities are increased (97, 98). 

MacDonald (99) showed that mouse liver acid phosphatase required active sulfhydryl groups for activity and that malonate buffer, pH 5.9, was useful for the assay of this enzyme because it stabilized the enzyme during the period of the assay. 

The centrifugal method of separation employed by Van Lancker and Holtzer (V2) was among the earlier ones in the field, and there was probably considerable cross contamination of the fractions. Nonetheless, the distribution seems more disperse than that obtained by de Duve et al. (DIO) for rat liver with a comparable method. For example, in the case of the mouse pancreas the small mitochondrial fractions, c, d, and e, obtained by centrifugation between 17 X 10 and 263 X 10 gr-min contained 27% of the acid phosphatase and the succeeding microsomal fractions, f and g, obtained by centrifugations between 263 X 10 g-min and 3170 X 10 g-min, contained 24% of the acid phosphatase (V2). For rat liver, comparable fractions, obtained by centrifugation between 33 X 10 to 250 X 10 g-min and 250 X 10 to 3000 X 10 g-min contained 41 and 20%, respectively (DIO). 

R9. Russo, J., Subcellular distribution of acid phosphatase in the mouse testis. Ada Physiol. Lat. Amer. 20, 78-80 (1970). 

Kai M, Wada I, Imai S, Sakane F, Kanoh H (1996) Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase. J Biol Chem 271 18931-18938... 

Mouse Fid Phosphatidic acid phosphatase 1 (lipin-1) Impaired adipose development, insulin resistance, increased P-oxidation... 

Acid phosphatase activity in 10 B5C3F1 mouse peritoneal macrophages was depressed by 22.8 and 44.7 % when ammonium metavanadate (2.5 mg and 10 mg V/kg) was given i.p. every 3 d for 6 weeks, while the activities of 3-glucuronidase, N-acetyl-P-D-glucosaminidase, and lysozyme were not significantly influenced (Vaddi and Wei 1991). 

Particularly relevant in this discussion is acid phosphatase which is widely considered to be exclusively a lysosomal enzyme. Evidence from this laboratory will be presented which indicates that acid phosphatase is a component of membranes in epithelial cells of mouse kidney and that lysosomal and microsomal acid phosphatases are two different isoenzymes. With this demonstration, all of the phosphohydrolases discussed in this chapter do exist in a membrane-associated form among others. 

Fig. 9. Dense body-type lysosome of epitheUal cell in mouse renal cortex showing reaction product for acid phosphatase obtained with the Smith-Fishman technique (Smith and Fishman, 1969 Sasaki and Fishman, 1972). Most of the organelle is composed of concentric whorls of membranes with reaction product. X 20,000.

Lin and Fishman (1972) prepared subcellular fractions of homogenates of mouse kidney and assayed them for the activities of acid phosphatase (phenylphosphatase, )3-glycerophosphatase), )3-glucuronidase, glu-cose-6-phosphatase, and succinic dehydrogenase. As shown in Fig. 10,... 

Comparison of Substrate SpECiFicrnES of Microsomal and Lysosomal Acid Phosphatases of Mouse Kidney... 

Not only are phosphohydrolases membrane components, but a variety of other enzymes such as glycosidases have been shown to share the same location. For example, the microvillar membranes of the absorbing epithelial cells of the intestine contain sucrase, maltase, and leucine amino-peptidase the basal infolding membranes of mouse renal epithelial cells exhibit both acid phosphatase and yS-glucuronidase. 

The embryonic morphogenesis of alkaline and acid phosphatases in fish (Tatarskaya et al., 1958), in the rat kidney (Pinkstaff et al., 1962), the rat lung (Zawistowska et al., 1963), the mouse brain (Lierse, 1963), the chick brain (Lee et al., 1961), in insects (Chaudhary and Lemonde, 1964), etc and of several other enzymes of phosphorus and nucleotide metabolism (Donath, 1962 Baker and... 

In the granules of mouse juxtaglomerular cells, acid phosphatase and 9-glucuronidase activities were found while sulfatase and nonspecific esterase could not bo demonstrated, -Glucuronidase activity was more intense than that of acid phosphatase (Gomba and Soltesz, 1969). 

Geier, C., von Figura, K., and Pohlmann, R., 1991, Molecular cloning of the mouse lysosomal acid phosphatase. Biol. Chem. Hoppe-Seyler 372 301-304. 

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