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Anti‐inflammatory actions of an N‐terminal peptide from human lipocortin 1
Author(s) -
Cirino G.,
Cicala C.,
Sorrentino L.,
Ciliberto G.,
Arpaia G.,
Perretti M.,
Flower R.J.
Publication year - 1993
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1993.tb12843.x
Subject(s) - annexin a1 , peptide , inflammation , annexin , phospholipase a2 , melittin , chemistry , endocrinology , pharmacology , medicine , biochemistry , enzyme , in vitro
An acetylated polypeptide corresponding to residues 2–26 of human lipocortin 1 was synthesized and the anti‐inflammatory activity assessed in three models of acute inflammation in rat and mouse. In the carrageenin rat paw oedema test, the peptide produced a maximal inhibition of approximately 41% at the 3 h time point with a 10 μg dose. When rat paw oedema was induced by the injection of venom phospholipase A 2 , the peptide produced a significant inhibition (31%) at the top dose of 20 μg per paw. In the mouse air‐pouch model, systemic treatment with the peptide produced a dramatic reduction in cytokine‐induced leukocyte migration with an ID 50 of approximately 40 μg per mouse. The N‐terminal peptide 2–26 shares the actions of lipocortin 1 in these acute models of inflammation.