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Annexin 1 (ANX-A1) exerts antimigratory actions in several models of acute and chronic inflammation. This is related to its ability to mimic the effect of endogenous ANX-A1 that is externalized on neutrophil adhesion to the postcapillary endothelium. In the present study we monitored ANX-A1 expression and localization in intravascular and emigrated neutrophils, using a classical model of rat peritonitis. For this purpose, a pair of antibodies raised against the ANX-A1 N-terminus (ie, able to recognize intact ANX-A1) or the whole protein (ie, able to interact with all ANX-A1 isoforms) was used by immunofluorescence and immunocytochemistry analyses. The majority ( approximately 50%) of ANX-A1 on the plasma membrane of intravascular neutrophils was intact. Extravasation into the subendothelial matrix caused loss of this pool of intact protein (to approximately 6%), concomitant with an increase in total amount of the protein; only approximately 25% of the total protein was now recognized by the antibody raised against the N-terminus (ie, it was intact). In the cytoplasm of these cells, ANX-A1 was predominantly associated with large vacuoles, possibly endosomes. In situ hybridization confirmed de novo synthesis of ANX-A1 in the extravasated cells. In conclusion, biochemical pathways leading to the externalization, proteolysis, and synthesis of ANX-A1 are activated during the process of neutrophil extravasation.

Original publication

DOI

10.1016/S0002-9440(10)64002-3

Type

Journal article

Journal

Am J Pathol

Publication Date

02/2001

Volume

158

Pages

603 - 615

Keywords

Animals, Annexin A1, Carrageenan, Cell Adhesion, Cell Movement, Dose-Response Relationship, Drug, Endothelium, Vascular, Gene Expression Regulation, Immunohistochemistry, In Situ Hybridization, Inflammation, Male, Mesentery, Microscopy, Electron, Neutrophils, Peritonitis, RNA, Messenger, Rats, Rats, Sprague-Dawley