The metabolism of adenosine 3′,5′-cyclic phosphate. II. Some properties of adenosine-3′,5′-cyclic-phosphate phosphodiesterase from the rat kidney

Douša, Tomáš; Rychlík, Ivan

doi:10.1016/0005-2787(70)90485-5

Cited by 27 publications

(2 citation statements)

References 18 publications

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“…Isolation of brush-border fragments (Wilfong & Neville, 1970) and histochemistry Baumann et al, 1964) have indicated that in the rat kidney alkaline phosphatase is located in the brush borders of the tubules. Breakdown of 3':5'-cyclic AMP occurred predominantly in the supernatant fraction from the kidney, confirming the observations of Dousa & Rychlik (1970) and Jard & Bernard (1970). This cellular distribution of adenosine 3': 5'-cyclic phosphate 3'-phosphohydrolase and the observation that the hydrolysis of inositol 1: 2-cyclic phosphate by rat kidney homogenates was not affected by theophylline indicated a separate identity of the two phosphodiesterases.…”

Section: Discusionsupporting

confidence: 89%

“…This cellular distribution of adenosine 3': 5'-cyclic phosphate 3'-phosphohydrolase and the observation that the hydrolysis of inositol 1: 2-cyclic phosphate by rat kidney homogenates was not affected by theophylline indicated a separate identity of the two phosphodiesterases. Theophylline is a potent inhibitor of kidney adenosine 3': 5'-cyclic phosphate 3'-phosphohydrolase (Jard & Bernard, 1970;Dousa & Rychlik, 1970). For completeness adenosine 2':3'-cyclic phosphate was examined as a substrate in these studies on the primary cell fractions.…”

Section: Discusionmentioning

confidence: 99%

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A comparison of d-inositol 1:2-cyclic phosphate 2-phosphohydrolase with other phosphodiesterases of kidney

Dawson

Clarke

1973

Biochemical Journal

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1. The ability to hydrolyse various phosphodiesterase substrates was examined in subcellular fractions of rat kidney and in serial slices of the kidneys of mouse, rat, guinea pig and ox cut from the cortex perimeter inwards. 2. d-Inositol 1:2-cyclic phosphate 2-phosphohydrolase could be clearly distinguished from phosphodiesterases which hydrolyse 2':3'- and 3':5'-cyclic AMP and p-nitrophenyl thymidine 5'-phosphate (phosphodiesterase I). The hydrolysis of sn-glycero-3-phosphorylcholine showed a distribution identical with that of particle-bound d-inositol 1:2-cyclic phosphate 2-phosphodiesterase, but there was a 30-fold difference in the ratio of enzyme activities between the rat and guinea pig. 3. In rat and mouse kidney, d-inositol 1:2-cyclic phosphate 2-phosphohydrolase is virtually all membrane bound and in the outer cortex, whereas in guinea-pig kidney the enzyme is almost entirely soluble and located throughout the kidney tissue. Some properties of the soluble enzyme are described. 4. Distribution and histochemical studies indicated that in the rat and mouse, phosphodiesterase I is associated with the brush borders of the straight portion (pars recta) of the proximal tubule, whereas inositol 1:2-cyclic phosphate 2-phosphohydrolase and probably glycerylphosphorylcholine diesterase are associated with the brush borders of the convoluted part of the tubule (pars convoluta).

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Section: Discusionsupporting

confidence: 89%

Section: Discusionmentioning

confidence: 99%

A comparison of d-inositol 1:2-cyclic phosphate 2-phosphohydrolase with other phosphodiesterases of kidney

Dawson

Clarke

1973

Biochemical Journal

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Differential effects of cytochalasin B and caffeine on control of DNA synthesis in normal and transformed cells

O’Neill

1979

Journal Cellular Physiology

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Evidence is presented which suggests the existence of a t least two growth control points in cultured mammalian cells. These controls are in "parallel" rather than in "series." It is suggested that in normal and some transformed cells the controls are coupled while in SV40 transformed cells and tumor cells they are uncoupled. One control is revealed by cytochalasin B (CB) treatment since in normal and some kinds of transformed cells, CB treatment results in the accumulation or the arrest of cells in G1. In this case, the control is normal or coupled. In DNA tumor virus transformed cells and many cultured tumor cells (excluding human glioblastomas) CB does not arrest cells although it prevents cytoplasmic division. Such cells continue DNA synthesis and nuclear division and become highly multinucleated. The effects of CB are not concentration dependent. Here the control is defective or uncoupled. Another control is revealed by caffeine treatment. Again, normal and some types of transformed cells are accumulated in G1 following caffeine treatment, while SV40 transformed cells and tumor cells continue DNA synthesis unabated. The effects of caffeine in arresting cells are concentration dependent. Similarly the control point revealed by caffeine is coupled in normal cells and altered or uncoupled in some SV40 transformed and tumor cells. Although CB and caffeine do not inhibit DNA synthesis in tumor and SV40 transformed cells when administered separately, they cause G1 accumulation when administered in combination. This observation can be explained by the possibility that some transformed cells can utilize alternate or parallel mechanisms to progress through G1 when one mechanism is blocked (CB or caffeine). When both are blocked the cells become arrested in G1. The human glioblastomas are unique among the cultured human tumors thus far examined since they are partially arrested by CB. However they are like other human tumors in that caffeine does not significantly affect DNA synthesis.Previous observations have shown a differential response to cytochalasin B (CB) or caffeine among normal and transformed cells. In CB treated normal cells nuclear division and DNA synthesis are inhibited in the absence of cytoplasmic cleavage (Wright and Hayflick, '72; Kelly and Sambrook, '73; ONeill, '74; ONeill et al., '75; Hirano and Kurimura, '74). In contrast CB treated DNA virus transformed cells and many kinds of tumor cells show continued DNA synthesis and nuclear division in the absence of cytoplasmic division (Wright and Hayflick, '72;

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Cyclic Nucleotide Phosphodiesterases: Properties, Activators, Inhibitors, Structure–Activity Relationships, and Possible Role in Drug Development

Amer

Kreighbaum

1975

Journal of Pharmaceutical Sciences

205

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The metabolism of adenosine 3′,5′-cyclic phosphate. II. Some properties of adenosine-3′,5′-cyclic-phosphate phosphodiesterase from the rat kidney

Cited by 27 publications

References 18 publications

A comparison of d-inositol 1:2-cyclic phosphate 2-phosphohydrolase with other phosphodiesterases of kidney

A comparison of d-inositol 1:2-cyclic phosphate 2-phosphohydrolase with other phosphodiesterases of kidney

Differential effects of cytochalasin B and caffeine on control of DNA synthesis in normal and transformed cells

Cyclic Nucleotide Phosphodiesterases: Properties, Activators, Inhibitors, Structure–Activity Relationships, and Possible Role in Drug Development

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