Rat kidney glycerylphosphorylcholine diesterase

Baldwin, J. J.; Cornatzer, W. E.

doi:10.1016/0005-2760(68)90146-x

Cited by 55 publications

(27 citation statements)

References 18 publications

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“…GroPCho diesterase is reported to be also active on GroPEtn [21,24]. The lack of specificity of this enzyme for its substrate headgroup seems to offer a straightforward interpretation of the fact that both GroPCho and GroPEtn levels decrease to the same extent in TNFtreated tumors [9], as well as of the parallel decreases of PC and PE, observed in the present study.…”

Section: Correlation Between Lipid Degradation Andsupporting

confidence: 55%

Alterations of lipid composition in Friend leukemia cell tumors in mice treated with tumor necrosis factor‐α

et al. 1990

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Lipid analyses were carried out on transplantable murine Friend leukemia cell tumors, 6 h after intratumoral administration of tumor necrosis factor-a (TNF). The levels of the major phospholipid classes were uniformly decreased to about 70% of control values; free fatty acids were increased to about 1705%; diacylglycerol was decreased to about 50% and triacylglycerol, the main lipid component, was not significantly altered. These results analysed in the light of concomitant alterations in the levels of phospholipid precursors and catabolites (determined in previous s1P NMR studies) and histological modifications demonstrated that at early stages of TNF-induced inhibition of tumor growth (a) phospholipid catabolism was significantly enhanced; (b) morphological changes were apparently correlated with alterations in the levels of phosphatidylcholine and its catabolic products.

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Section: Correlation Between Lipid Degradation Andsupporting

confidence: 55%

Alterations of lipid composition in Friend leukemia cell tumors in mice treated with tumor necrosis factor‐α

et al. 1990

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“…In addition, it would be difficult to quantitate using a nonradioactive substrate. Estimations of GPC choline phosphodiesterase activity of renal tissue were based upon specific enzymatic quantitation of L-a-glycerylphosphate, the co-product [3]. Rat cortical homogenates incubated with GPC were reported to produce equimolar amounts of glyceryl, inorganic phosphate and choline [ 121 with an activity of about 180 nmol/mg protein per h. This level of activity is approximately i6-fold lower than that presented in this report (table 1).…”

Section: Discussionmentioning

confidence: 67%

“…GPC choline phosphodiesterase activity (EC 3.1. 4.2) liberates free choline and L-a-glycerylphosphate and its presence has been well documented in several tissues including kidney [2,3]. The existence of an additional hydrolytic activity, originally detected in brain tissue, GPC phosphorylcholine phosphodiesterase (EC 3.1.4.38) produces phosphorylcholine and glyceryl from GPC [4].…”

Section: Glycerylphosphorylcholinementioning

confidence: 99%

GPC phosphodiesterase and phosphomonoesterase activities of renal cortex and medulla of control, antidiuresis and diuresis rats

Kanfer

McCartney

1989

FEBS Letters

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Glycerylphosphorylcholine (GPC) concentration was reported to be elevated in renal medulla of experimental animals deprived of water. The activities of GPC phosphodiesterases were similar in homogenates and membrane subfractions of renal cortex prepared from control, diuresis and antidiuresis rats. There were no differences in these preparations' ability to hydrolyze phosphorylcholine. In contrast, there was a nearly 50% reduction of non‐specific phosphomonoesterase activity, using p‐nitrophenylphosphate as substrate and membrane subfractions prepared from the antidiuresis animals. It is suggested that as a consequence, a pathway for the formation from L‐α‐glycerylphosphate is activated.

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“…After 10 min incubation, the reaction product (phosphatidylcholine) was estimated radiometrically following thin-layer chromatography separation of the lipid extract. The inhibitors to which the enzyme was S. Sipione et al/FEBS Letters 384 (1996) [19][20][21][22][23][24] exposed were N-ethylmaleimide and p-chloromercuribenzoate, under conditions described in the legend to Fig. 3.…”

Section: Enzyme Assaysmentioning

confidence: 99%

“…GroPEtnPDE assays was carried out by the spectrophotometric method described by Baldwin and Cornatzer [22].…”

Section: Enzyme Assaysmentioning

confidence: 99%

Phosphatidylcholine synthesis‐related enzyme activities of bovine brain microvessels exhibit susceptibility to peroxidation

et al. 1996

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In microvessels isolated from bovine brain, microsomal enzyme activities involved in phosphatidylcholine biosynthesis and degradation were determined. The microvessels possessed acyl-CoA:l-acyl-sn-glycero-3-phosphoeholine (AT) and glycerophosphocholine phosphodiesterase (GroPChoPDE) activity at a higher level compared with bovine and rat brain or rat liver microsomes whereas they expressed CTP:phosphocholine cytidylyltransferase (CT) and choline phosphotransferase (CPT) activity at a lower level. Each enzyme has been characterized in terms of response to inldbitors or activators revealing properties very similar to those in brain and liver microsomes. In the homogenate prepared from t-butylhydroperoxide-treated microvessels (10 min exposure to 10 ~ up to 1 mM concentrations), AT and CPT activities exhibited a significant dose-dependent inhibition. In contrast, GroPChoPDE activity was unaffected. CT was inhibited only at 1 mM concentration. Short treatment of microvessels with Fe 2÷ (20 ~Vl)-ascorbate (0.25 mM) or 100 ~VI linoleate hydroperoxide did not have any effect on the activity of the four enzymes. Strong inhibition of all enzymes was noted when the linoleate hydroperoxide system was fortified by Fe 2÷ ions (100 ttM). AT inactivation was also found when oxidized low density lipoprotein was preincubated with microvessels. On the other hand, oxidized LDL left unchanged CPT and GroPChoPDE activities whereas it promoted a slight stimulation of cytidylyltransferase activity. Overall, the results suggest a link between oxygen radical generation and the perturbation of the microvessel membrane structure in which the four enzymes are incorporated, coupled to a direct sulfhydryl protein modification.

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Rat kidney glycerylphosphorylcholine diesterase

Cited by 55 publications

References 18 publications

Alterations of lipid composition in Friend leukemia cell tumors in mice treated with tumor necrosis factor‐α

Alterations of lipid composition in Friend leukemia cell tumors in mice treated with tumor necrosis factor‐α

GPC phosphodiesterase and phosphomonoesterase activities of renal cortex and medulla of control, antidiuresis and diuresis rats

Phosphatidylcholine synthesis‐related enzyme activities of bovine brain microvessels exhibit susceptibility to peroxidation

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