Neutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression.
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 expressi...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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2001
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| _version_ | 1797081332243759104 |
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| author | Oliani, S Paul-Clark, M Christian, H Flower, R Perretti, M |
| author_facet | Oliani, S Paul-Clark, M Christian, H Flower, R Perretti, M |
| author_sort | Oliani, S |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T01:13:03Z |
| format | Journal article |
| id | oxford-uuid:8db37ec5-4fd6-4819-8bd5-d6cc4b201144 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:13:03Z |
| publishDate | 2001 |
| record_format | dspace |
| spelling | oxford-uuid:8db37ec5-4fd6-4819-8bd5-d6cc4b2011442022-03-26T22:52:52ZNeutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8db37ec5-4fd6-4819-8bd5-d6cc4b201144EnglishSymplectic Elements at Oxford2001Oliani, SPaul-Clark, MChristian, HFlower, RPerretti, MAnnexin 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. |
| spellingShingle | Oliani, S Paul-Clark, M Christian, H Flower, R Perretti, M Neutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression. |
| title | Neutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression. |
| title_full | Neutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression. |
| title_fullStr | Neutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression. |
| title_full_unstemmed | Neutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression. |
| title_short | Neutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression. |
| title_sort | neutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression |
| work_keys_str_mv | AT olianis neutrophilinteractionwithinflamedpostcapillaryvenuleendotheliumaltersannexin1expression AT paulclarkm neutrophilinteractionwithinflamedpostcapillaryvenuleendotheliumaltersannexin1expression AT christianh neutrophilinteractionwithinflamedpostcapillaryvenuleendotheliumaltersannexin1expression AT flowerr neutrophilinteractionwithinflamedpostcapillaryvenuleendotheliumaltersannexin1expression AT perrettim neutrophilinteractionwithinflamedpostcapillaryvenuleendotheliumaltersannexin1expression |