Comparative degradation of adenylnucleotides by cultured endothelial cells and fibroblasts

Dosne, A.M.; Legrand, Chantal; Bauvois, Brigitte; Bodevin, E; Caen, Jacques P.

doi:10.1016/s0006-291x(78)80027-8

Cited by 36 publications

(10 citation statements)

References 17 publications

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“…The significance of this is not clear, although smooth muscle ADPase may become relatively more important after damage to the vessel wall. ADPase activity is present in human venous endothelial cells and skin fibroblasts (22,23) and in porcine aortic smooth muscle cells (6), but apparently not in human venous smooth muscle cells (22) or HeLa cells (unpublished observations).…”

Section: Resultsmentioning

confidence: 96%

Effects of aspirin and dipyridamole on the degradation of adenosine diphosphate by cultured cells derived from bovine pulmonary artery.

Crutchley¹,

Ryan²,

Ryan³

1980

J. Clin. Invest.

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A B S T R A C T To improve understanding of the mechanisms by which ADP is degraded during passage through the pulmonary vascular bed, we examined cultured endothelial and smooth muscle cells of bovine pulmonary artery for their abilities to metabolize [8-"C]ADP. ADP is rapidly converted to AMP and then to adenosine, hypoxanthine, and inosine. Inosine is the major metabolite produced by endothelial cells. Radioactivity (5-10%) is accumulated intracellularly primarily as ATP. Medium containing 50,.M ADP incubated with endothelial cells rapidly loses its ability to aggregate platelets and becomes antiaggregatory under conditions in which prostacyclin is absent. The antiaggregatory activity is probably the result of accumulated adenosine. 10 ,uM dipyridamole inhibits cellular uptake of radioactivity by >90%, and inosine in the medium is largely replaced by adenosine. This is accompanied by increased antiaggregatory activity ofconditioned medium, which can be matched by authentic adenosine at the same concentration. 1 mM aspirin had no effect on the metabolism of ADP by endothelial cells. Our results suggest: (a) Metabolism of ADP during passage through the lung is mainly the result of endothelial ADPase. (b) ADP released from aggregating platelets can be converted to the antiaggregatory substance, adenosine. Dipyridamole may exert some of its antithrombotic actions by preventing the intracellular uptake ofadenosine, thereby increasing its concentration near the site ofthrombus formation. (c) The ability ofthe vessel wall to degrade ADP should not be compromised by the use of aspirin as an antithrombotic drug. (d) Endothelium may retain some of its antithrombogenicity when prostacyclin generation is impaired.

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Section: Resultsmentioning

confidence: 96%

Effects of aspirin and dipyridamole on the degradation of adenosine diphosphate by cultured cells derived from bovine pulmonary artery.

Crutchley¹,

Ryan²,

Ryan³

1980

J. Clin. Invest.

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“…Endothelial cells are known to produce enzymes that activate plasminogen (1, 2), procoagulant molecules such as tissue factor (36), and factors that influence platelet function and vascular tone (3)(4)(5)(6)(7). We now report the capacity of this cell type to activate HF.…”

Section: Resultsmentioning

confidence: 99%

“…The compatibility of the intact endothelial cell surface with blood and its constituent procoagulant proteins is a central and necessary condition for maintenance ofvascular homeostasis. Although the mechanism of this compatibility has not been fully elucidated, it is clear that the production by endothelial cells of fibrinolytic enzymes (1,2), prostacyclin (3), and other factors that influence platelet function (4,5) or vascular tone (6) may play a significant role in ensuring vessel patency. The endothelial cell surface is equally important in hemostasis and the induction of thrombus formation inasmuch as damage to this layer is associated with attachment of platelets and the initiation of coagulation (7).…”

Section: Introductionmentioning

confidence: 99%

Activation of Rabbit Hageman Factor by Homogenates of Cultured Rabbit Endothelial Cells

Wiggins¹,

Loskutoff²,

Cochrane³

et al. 1980

J. Clin. Invest.

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“…Endothelial cells were obtained from human umbilical vein and cultured in medium 199 (GIBCO Laboratories, Grand Island, N.Y.) supplemented with 20% fetal calf serum (Hy-Clone; Sterile Systems Inc., Logan, Utah) (19). These cells were characterized by the presence of Weibel-Palade bodies and the synthesis of factor VIII-related antigen (7) and by their ability to degrade ADP (8). At confluency, i.e., 6 to 8 days after seeding, the cell cultures (3 x 105 to 4 x 105 cells per 4-cm2 dish) were washed 4 times with medium 199 containing 3.5 g of human nonpyrogenic albumin (Centre National de Transfusion, Paris, France) per liter and then incubated in medium 199 with LPS (from Salmonella enteritidis; Difco Laboratories, Detroit, Mich.) or MDP (Choay Chimie Reactifs, Paris, France).…”

Section: Methodsmentioning

confidence: 99%

Effect of polymyxin B and colimycin on induction of plasminogen antiactivator by lipopolysaccharide in human endothelial cell culture

Dubor¹,

Dosne²,

Chedid³

1986

Infect Immun

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The effect of lipopolysaccharide (LPS) on the production of fibrinolytic inhibitor by human endothelial cells was determined because results of previous experiments have shown us that it is possible to stimulate this synthesis with muramyl dipeptide. Treatment of these cells with LPS resulted in a marked enhancement of fibrinolytic inhibitor, as estimated in a urokinase-induced fibrinolysis assay. A dose-response curve was obtained for LPS concentrations ranging from 10 to 1,000 ng/ml, thus demonstrating the great sensitivity of these cells. This inhibitor did not reduce plasmin activity and formed complexes with highand low-molecularweight urokinase as visualized by fibrin enzymography on sodium dodecyl sulfate-polyacrylamide electrophoretic gels. The molecular weight of this inhibitor was estimated to be 54 to 58 kilodaltons. These findings led us to conclude that LPS stimulates formation of a plasminogen antiactivator. This LPS effect could be suppressed by polymyxin B and colimycin. The stimulatory effect of muramyl dipeptide required doses which were at least 1,000 times greater than those of LPS and was not decreased by polymyxin B. These results show the possibility of independent modulation of plasminogen antiactivator production at the endothelial level, which could be important in endotoxemia. Under these conditions colimycin might have an additional advantage for clinical use because of its ability to prevent fibrinolytic inhibition.

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Comparative degradation of adenylnucleotides by cultured endothelial cells and fibroblasts

Cited by 36 publications

References 17 publications

Effects of aspirin and dipyridamole on the degradation of adenosine diphosphate by cultured cells derived from bovine pulmonary artery.

Effects of aspirin and dipyridamole on the degradation of adenosine diphosphate by cultured cells derived from bovine pulmonary artery.

Activation of Rabbit Hageman Factor by Homogenates of Cultured Rabbit Endothelial Cells

Effect of polymyxin B and colimycin on induction of plasminogen antiactivator by lipopolysaccharide in human endothelial cell culture

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