NDLI: Prothrombin is activated on vascular endothelial cells by factor Xa and calcium.

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Selective cleavage in the avian retroviral long terminal repeat sequence by the endonuclease associated with the alpha beta form of avian reverse transcriptase.

Engineering of site-directed antisera against vertebrate calmodulin by using synthetic peptide immunogens containing an immunoreactive site.

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Different 3' end points of deletions causing delta beta-thalassemia and hereditary persistence of fetal hemoglobin: implications for the control of gamma-globin gene expression in man.

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Identification of a transposon Tn3 sequence required for transposition immunity.

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Structural similarities between the development-specific protein S from a gram-negative bacterium, Myxococcus xanthus, and calmodulin.

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Nucleotide sequence of the structural gene for diphtheria toxin carried by corynebacteriophage beta.

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Prothrombin is activated on vascular endothelial cells by factor Xa and calcium.

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Prothrombin is activated on vascular endothelial cells by factor Xa and calcium.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Rodgers, G. M. Shuman, M. A.
Abstract	Vascular endothelial cells derived from adult bovine aorta (ABAE) treated with factor Xa and calcium were found to activate prothrombin. In contrast, nonvascular cells (human foreskin fibroblasts, bovine corneal endothelial cells, or human fetal lung cells) had either no or very little effect on prothrombin activation. In the presence of 6 X 10(5) ABAE cells, 20 ng of factor Xa converted 90 micrograms of prothrombin into 80 units of thrombin after 45 min at 37 degrees C. Exogenous factor V was not required for prothrombin activation, but thrombin generation was enhanced 2- to 4-fold by the addition of factor V (500-2,500 ng/ml). Treatment of ABAE cells with anti-bovine factor V IgG markedly inhibited prothrombin activation by factor Xa and calcium. In cells grown in serum-free medium for 3 months, the amount of factor V activity was equivalent to that found in cells grown with serum, which suggests that these cells probably synthesize factor V. Sparse ABAE cells increased prothrombin activation by factor Xa 6-fold compared to activation in confluent cells. Although previous thrombin treatment of ABAE cells did not enhance prothrombin activation, addition of dansyl arginine-4-ethyl piperidine amide markedly inhibited activation of 125I-labeled prothrombin by factor Xa, indicating that thrombin formation is necessary for optimal prothrombin activation. These data indicate that aortic endothelium may provide a physiologically important surface for activation of prothrombin as well as a mechanism for optimal formation of clots at sites of vascular injury.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	80
Language	English
Publisher	National Academy of Sciences
Publisher Date	1983-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium Pharmacology Factor X Metabolism Muscle, Smooth, Vascular Physiology Prothrombin Animals Aorta Cell Line Endothelium Enzyme Activation Factor V Factor Xa Kinetics Pregnancy Umbilical Veins Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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