Leukotriene A4 hydrolase. Inhibition by bestatin and intrinsic aminopeptidase activity establish its functional resemblance to metallohydrolase enzymes-Reference-Cited by-同舟云学术

Leukotriene A4 hydrolase. Inhibition by bestatin and intrinsic aminopeptidase activity establish its functional resemblance to metallohydrolase enzymes

Published:1991-01 Issue:3 Volume:266 Page:1375-1378
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Orning L,Krivi G,Fitzpatrick F A

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference33 articles.

1. Leukotriene B4 stimulates polymorphonuclear leukocyte adhesion to cultured vascular endothelial cells.

2. Leukotriene B4 action on endothelium mediates augmented neutrophil/endothelial adhesion.

3. Thrombin stimulates the adherence of neutrophils to human endothelial cells in vitro.

4. Leukotrienes C4 and D4 stimulate human endothelial cells to synthesize platelet-activating factor and bind neutrophils.

5. Leukotriene B, a potent chemokinetic and aggregating substance released from polymorphonuclear leukocytes

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