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(American Journal of Pathology. 2001;158:603-615.)
© 2001 American Society for Investigative Pathology

Regular Article

Neutrophil Interaction with Inflamed Postcapillary Venule Endothelium Alters Annexin 1 Expression

Sonia M. Oliani^*, Mark J. Paul-Clark^*, Helen C. Christian, Roderick J. Flower^* and Mauro Perretti^*

From The William Harvey Research Institute,^*
London, United Kingdom; the Department of Human Anatomy and Genetics,
University of Oxford, Oxford, United Kingdom; and the Department of Biology,
Instituto de Biociências, Letras e Ciências Exatas–Universidade Estadual Paulista, São Paulo, Brazil

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 (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 6%), concomitant with an increase in total amount of the protein; only 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.

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