Acid phosphatase induction

Enhancement of POD-capacity and appearance of new isoforms is generally considered as an important criterion for senescence (Hazell and Murray, 1982). Lee et al. (1976a) suggested that the cadmium-induced capacity increase of POD and several hydrolytic enzymes (ribonuclease, deoxyribonuclease, acid phosphatase) in Glycine max should constitute an accelerated senescence response. In Zea mays, an induction of leaf acid phosphatase was also reported for toxic concentrations of lead (Maier, 1978 b). 

Hatoff DE, Hardison WG (1981) BUe acids modify alkaline phosphatase induction and... 

Yun, S.j. and Kaeppler, S.M. (2001) Induction of maize acid phosphatase activities under phosphorus starvation. Plant and Soil 237, 109-1 15. 

Lee, T.-M. (2000) Phosphate starvation induction of acid phosphatase in Ulva lactuca L. (Ulvales, Chlorophyta). Botanical Bulletin Academia Sinica4l, 19-23. 

Some physiological or pathological stimuli induce the liver cell to synthesize or break down some protein selectively. Even during starvation the content of all liver protein does not drop simultaneously. For example, while the activities of catalase, xanthine oxidase, alkaline phosphatase, and acid phosphatase drop at various rates as starvation progresses, that of glucose-6-phosphatase increases. Hydrocortisone and tryptophan administration induces a massive increase in tryptophan peroxidase activity. In either case, at least part of the increase in enzyme activity results from de novo enzyme synthesis. If tryptophan administration is interrupted, the activity of the peroxidase returns to normal. During the induction, turnover rates of other proteins do not change. 

Cyclosporine A (CsA) is a water-insoluble cyclic peptide from a fungus composed of 11 amino acids. CsA binds to its cytosolic receptor cyclophilin. The CsA/cyclophilin complex reduces the activity of the protein phosphatase calcineurin. Inhibition of this enzyme activity interrupts antigen receptor-induced activation and translocation of the transcription factor NEAT to the nucleus which is essential for the induction of cytokine synthesis in T-lymphocytes. 

Palmer, J.M., Induction of phosphatase activity in thin slices of Jerusalem artichoke tissue by treatment with indoleacetic acid, Planta, 93, 53-99, 1970. 

Actually it is doubtful that the antiviral properties of polyanions are based only on the interferon induction (46), since several groups have also demonstrated other activities of polyanions. Thus, e.g. poly(vinylsulfonate) has been found to interact with nucleic acids, thus inhibiting their acylation or methylation (47). Tempel (48) has shown that in mice phosphatases can be activated with poly(vinylsulfonate). 

TNAP is expressed in human hepatocytes, and bile acids increase its activity [93] and secretion in the bile [94]. TNAP in rat hepatocytes is predominantly localized in the bile canalicular domain of the plasma membrane [95, 96], but can be addressed to the baso-lateral membrane in the presence of high levels of bile acid [97]. In contrast, mouse hepatocytes do not express TNAP [98]. In humans, liver TNAP may be expressed both at the sinusoidal and biliary pole of the hepatocyte. This explains why a significant proportion of TNAP activity in the circulation of healthy individuals originates from the liver. TNAP serum levels are of major clinical relevance as a marker of cholestasis. AP levels increase due to retrograde reflux of biliary alkaline phosphatase, enhanced hepatic synthesis and enzyme release into the serum, and induction of the intestinal alkaline phosphatase form [94, 99, 100]. 

Armstrong et al. (1995) [4] showed that ABA induced anion efflux is independent of ABIl in tobacco. However, phosphorylation and dephosphorylation events are involved in control of anion efflux. Kinase antagonists or removal of ATP inhibits ABA induced slow anion channels in V faba guard cells suggesting that an ATP-dependent protein kinase is necessary for anion efflux. Down-regulation by removal of ATP can be reversed by the phosphatase inhibitor okadaic acid. Thus, the induction of slow anion channels by ABA is mediated by an ATP-dependent protein kinase and inhibited by a phosphatase. The phosphatase is distinct from ABIl which is not inhibited by okadaic acid [7], Furthermore,... 

Rodan, S.B., Wesolowski, G., Hilton, D.J., Nicola, N.A. and Rodan, G.A. (1990) Leukemia inhibitory factor binds with high affinity to preosteoblastic RCT-1 cells and potentiates the retinoic acid induction of alkaline phosphatase. Endocrinology 127 1602-1608. 

Fig. 33.11. Regulation of acetyl Co A carboxylase. This enzyme is regulated allosterically, both positively and negatively, by phosphorylation (circled P) and dephosphorylation, and by diet-induced induction (circled t). It is active in the dephosphorylated state when citrate causes it to polymerize. Dephosphorylation is catalyzed by an insulin-stimulated phosphatase. Low energy levels, via activation of an AMP-dependent protein kinase, cause the enzyme to be phosphorylated and inactivated. The ultimate product of fatty acid synthesis, palmitate, is converted to its CoA derivative palmityl CoA, which inhibits the enzyme. A high-calorie diet increases the rate of transcription of the gene for acetyl CoA carboxylase, whereas a low-calorie diet reduces transcription of this gene.

S Aonuma, T Ushijima, M Nakayasu, H Shima, T Sugimura, M Nagao. Mutation induction by okadaic acid, a protein phosphatase inhibitor in CHL cells, but not in S. Typhimurium. Mutat. Res. 250 375-381, 1991. 

Kiguchi, K., Differential induction of apoptosis in human breast tumor cells by okadaic acid and related inhibitors of protein phosphatases 1 and 2A, Cell Growth Differ., 5, 995, 1994. 

Li, D.W.-C. et al., Okadaic acid-induced lens epithelbial cell apoptosis requires inhibition of phosphatase-1 and is associated with induction of gene expression including p53 and bax, Eur. J. Biochem., 257, 351, 1998. 

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