The effect of 2,3-diphosphoglycerate on oxygen consumption burst in thrombin-stimulated platelets

Principe, Domenico Del; Menichelli, A; Damiano, Anna Maria; Coppola, L; Bastianon, V.

doi:10.1016/0009-8981(77)90204-2

Cited by 2 publications

(2 citation statements)

References 12 publications

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“…The in vitro inhibitory effects of 2,3-DPG, 3-PG. and 3-PGA on platelet aggregation and on TXB2 formation induced by ADP, epinephrine, norepineph rine, collagen and thrombin [11] are phe nomena of extreme importance and can ex plain in part the prevention of massive intra vascular platelet aggregation during sickle cell hemolytic crises. There are other hemo lytic conditions, however, such as the hemo lytic uremic syndrome, which are character ized by thrombocytopenia and microangio pathic hemolytic anemia [12].…”

Section: Discussionmentioning

confidence: 99%

Structure-Function Relationship of 3-Phosphoglycerate Analogues with Platelet Aggregation and Thromboxane A<sub>2</sub> Formation

Iatridis¹,

Hadd²,

Kotrotsou³

et al. 1987

Pathophysiol Haemos Thromb

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We have studied the effects of 2,3-diphosphoglycerate (2,3-DPG), 3-phospho-glycerate (3-PG), 3-phosphoglyceraldehyde (3-PGA), 2-phosphoglycerate (2-PG) and β-glycerol phosphate (β-GP) on platelet aggregation and on thromboxane B₂ (TXB₂) formation. The results show that 2,3-DPG, 3-PG, and 3-PGA inhibited platelet aggregation and TXB₂ formation induced by norepinephrine, ADP, epinephrine, and collagen; but they also induced platelet aggregation and TXB₂ formation in the presence of subthreshold concentrations of Na arachidonate. 2-PG and β-GP were inactive. The results also show that there is a structure-function relationship between 2,3-DPG, 3-PG, and 3-PGA with platelet aggregation phenomena and prostaglandin synthesis.

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Section: Discussionmentioning

confidence: 99%

Structure-Function Relationship of 3-Phosphoglycerate Analogues with Platelet Aggregation and Thromboxane A<sub>2</sub> Formation

Iatridis¹,

Hadd²,

Kotrotsou³

et al. 1987

Pathophysiol Haemos Thromb

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show abstract

“…Thrombin (Fibrindex, Ortho) was used: it offered the purity require ments for these studies, as shown by means of analytical isotachophoresis (8) and electrophoresis on cellogel. When greater amounts of enzyme were necessary, zymothrombin (Baldacci) was used after purification by chromatography on SP Sephadex G-50 (9 (3,4).…”

Section: Methodsmentioning

confidence: 99%

The In Vitro Inhibitory Effect on Thrombin by 2,3-Diphosphoglycerate

Principe¹,

Strappini²,

Vecchio³

et al. 1981

Thromb Haemost

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SummaryThrombin, incubated with 2,3-diphosphoglycerate (150 nmol 2,3-DPG/1 NIH thrombin unit) lost up to 70% of its clotting activity, whereas the esterase activity remained unchanged. No fibrinopeptide release by thrombin was observed in the presence of 2,3-DPG. The fibrin polymerization was normal. By chromatography on Amberlite IRC-50, α-thrombin was eluted at pH 8.0. In presence of 2,3-DPG, α-thrombin was not eluted. Likely, 2,3-DPG can interfere with thrombin.

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The effect of 2,3-diphosphoglycerate on oxygen consumption burst in thrombin-stimulated platelets

Cited by 2 publications

References 12 publications

Structure-Function Relationship of 3-Phosphoglycerate Analogues with Platelet Aggregation and Thromboxane A<sub>2</sub> Formation

Structure-Function Relationship of 3-Phosphoglycerate Analogues with Platelet Aggregation and Thromboxane A<sub>2</sub> Formation

The In Vitro Inhibitory Effect on Thrombin by 2,3-Diphosphoglycerate

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