Kinetics and inhibition of alkaline phosphatases from canine tissues

Belle, H. Van

doi:10.1016/0005-2744(72)90118-0

Cited by 257 publications

(96 citation statements)

References 12 publications

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“…The Cdc28p phosphatase activity was also insensitive to both tartrate and tetramisole (Fig. 1A, lanes 10,11), which inhibit certain broad specificity acid phosphatases and alkaline phosphatases, respectively (AbulFadl and King 1949;Van Belle 1972). Moreover, the dephosphorylation of Cdc28p was blocked completely by the Mg 2+ chelator EDTA and by NaF (Fig.…”

Section: A Type 2c Protein Phosphatase Dephosphorylates Thr-169 Of CDmentioning

confidence: 93%

Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases

Cheng¹,

Ross²,

Kaldis³

et al. 1999

Genes & Development

156

152

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Activating phosphorylation of cyclin-dependent protein kinases (CDKsEukaryotic cell cycle progression is controlled by the sequential activation and inactivation of cyclin-dependent protein kinases (CDKs). To coordinate the cell cycle machinery, extracellular and intracellular signals regulate CDK activities through a variety of mechanisms, including association with regulatory subunits (cyclins, inhibitors, and assembly factors), subcellular localization, transcriptional regulation, selective proteolysis, and reversible protein phosphorylation

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Section: A Type 2c Protein Phosphatase Dephosphorylates Thr-169 Of CDmentioning

confidence: 93%

Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases

Cheng¹,

Ross²,

Kaldis³

et al. 1999

Genes & Development

156

152

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“…In slot blots biotinylated CaM (BioCaM) interacts with high affinity with bovine brain (data not shown). Further analysis with levamisole and L(/)tartrate, established inhibitors of alkaline (55) and CaN in a Ca 2/ -dependent manner (results not shown). By probing blots from the DEAE-cellulose eluate with acid phosphatase (56), also exclude any identity of the three pNPP-phosphatases with any of these phospha-BioCaM (Fig.…”

Section: Immunobinding Assaysmentioning

confidence: 94%

Occurrence of apara-Nitrophenyl Phosphate-Phosphatase with Calcineurin-like Characteristics inParamecium tetraurelia

Kissmehl

Treptau

Kottwitz

et al. 1997

Archives of Biochemistry and Biophysics

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“…5). In the presence of levamisole, an inhibitor of alkaline phosphatase (54,55), the delay of retardation of mineral formation caused by the addition of 40 M ATP was reduced with the increase of levamisole concentration from 0 to 4 mM (Fig. 6), suggesting that TNAP may be involved in the ATP-induced retardation of mineralization.…”

Section: Characteristic Of Atp-induced Retardation Of Mineralmentioning

confidence: 96%

Phosphodiesterase Activity of Alkaline Phosphatase in ATP-initiated Ca2+ and Phosphate Deposition in Isolated Chicken Matrix Vesicles

Zhang

Balcerzak

Radisson

et al. 2005

Journal of Biological Chemistry

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Inorganic pyrophosphate is a potent inhibitor of bone mineralization by preventing the seeding of calcium-phosphate complexes. Plasma cell membrane glycoprotein-1 and tissue nonspecific alkaline phosphatase were reported to be antagonistic regulators of mineralization toward inorganic pyrophosphate formation (by plasma cell membrane glycoprotein-1) and degradation (by tissue nonspecific alkaline phosphatase) under physiological conditions. In addition, they possess broad overlapping enzymatic functions. Therefore, we examined the roles of tissue nonspecific alkaline phosphatase within matrix vesicles isolated from femurs of 17-dayold chick embryos, under conditions where these both antagonistic and overlapping functions could be evidenced. Addition of 25 M ATP significantly increased duration of mineralization process mediated by matrix vesicles, while supplementation of mineralization medium with levamisole, an alkaline phosphatase inhibitor, reduces the ATP-induced retardation of mineral formation. Phosphodiesterase activity of tissue nonspecific alkaline phosphatase for bis-p-nitrophenyl phosphate was confirmed, the rate of this phosphodiesterase activity is in the same range as that of phosphomonoesterase activity for p-nitrophenyl phosphate under physiological pH. In addition, tissue nonspecific alkaline phosphatase at pH 7.4 can hydrolyze ADPR. On the basis of these observations, it can be concluded that tissue nonspecific alkaline phosphatase, acting as a phosphomonoesterase, could hydrolyze free phosphate esters such as pyrophosphate and ATP, while as phosphodiesterase could contribute, together with plasma cell membrane glycoprotein-1, in the production of pyrophosphate from ATP.

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Kinetics and inhibition of alkaline phosphatases from canine tissues

Cited by 257 publications

References 12 publications

Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases

Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases

Occurrence of apara-Nitrophenyl Phosphate-Phosphatase with Calcineurin-like Characteristics inParamecium tetraurelia

Phosphodiesterase Activity of Alkaline Phosphatase in ATP-initiated Ca2+ and Phosphate Deposition in Isolated Chicken Matrix Vesicles

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