scholarly journals The endothelin-converting enzyme from human umbilical vein is a membrane-bound metalloprotease similar to that from bovine aortic endothelial cells.

1992 ◽  
Vol 89 (18) ◽  
pp. 8606-8610 ◽  
Author(s):  
K. Ahn ◽  
K. Beningo ◽  
G. Olds ◽  
D. Hupe
Keyword(s):  
Endothelial Cells ◽  
Umbilical Vein ◽  
Converting Enzyme ◽  
Aortic Endothelial Cells ◽  
Human Umbilical Vein ◽  
Bovine Aortic Endothelial Cells ◽  
Endothelin Converting Enzyme ◽  
Membrane Bound ◽  
Aortic Endothelial

H2 receptor-mediated responses of aortic endothelial cells to histamine

1992 ◽  
Vol 262 (1) ◽  
pp. H220-H224 ◽  
Author(s):  
G. Hekimian ◽  
S. Cote ◽  
J. Van Sande ◽  
J. M. Boeynaems
Keyword(s):  
Endothelial Cells ◽  
Inositol Phosphates ◽  
Umbilical Vein ◽  
Bovine Aortic Endothelial Cell ◽  
Camp Content ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
H2 Antagonist ◽  
Umbilical Vein Endothelial Cells ◽  
Aortic Endothelial

It is well known that umbilical vein endothelial cells express H1 receptors that mediate the various responses of these cells to histamine, including accumulation of inositol phosphates, rise of cytosolic Ca2+, increased permeability to macromolecules, and release of prostacyclin. In bovine aortic endothelial cells, histamine did not increase the level of inositol phosphates nor the release of prostacyclin. In contrast, it increased the adenosine 3',5'-cyclic monophosphate (cAMP) content of these cells. That response was obtained in the 1 to 100 microM range of concentrations and reached a maximum within 2 min of histamine addition. It was mimicked by the H2-specific agonist dimaprit, inhibited by the H2 antagonist ranitidine, and insensitive to the H1 antagonist mepyramine. Histamine reduced the permeability to albumin of bovine aortic endothelial cell monolayers; this paradoxical effect is likely to be mediated by the rise in cAMP, which is known to enhance the barrier property of the endothelium. In conclusion, bovine aortic endothelial cells are responsive to histamine, and this response is mediated by H2 and not H1 receptors.

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