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A novel anti‐inflammatory peptide from human lipocortin 5
Author(s) -
Perretti Mauro,
Becherucci Cristina,
Mugridge Kenneth G.,
Solito Egle,
Silvestri Sergio,
Parente Luca
Publication year - 1991
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.1476-5381.1991.tb09788.x
Subject(s) - peptide , annexin a1 , phospholipase a2 , chemistry , melittin , phospholipase , phospholipase a , bombesin , endocrinology , arachidonic acid , peptide sequence , annexin , biochemistry , medicine , pharmacology , biology , enzyme , neuropeptide , in vitro , receptor , gene
1 A novel anti‐inflammatory peptide (residues 204–212) of human recombinant lipocortin 5 (hrLC5) found on the high similarity region with uteroglobin is described. 2 Peptide 204–212 dose‐dependently inhibited the contractions of rat isolated stomach strips elicited by porcine pancreatic phospholipase A 2 (PLA 2 ). Contractions caused by arachidonic acid (AA), prostaglandin E 2 (PGE 2 ) and 5‐hydroxytryptamine were not affected. No direct enzyme inhibition was observed in a radiochemical assay. 3 PGE 2 release by both human fibroblasts and rat macrophages was reduced by peptide 204–212 in a dose‐dependent manner. 4 The development of carrageenin‐induced oedema in rats was significantly inhibited by the local administration of peptide 204–212. 5 The pattern and potency of the biological effects of peptide 204–212 are similar to those of antiflammin 2, a lipocortin 1‐derived peptide. 6 It is suggested that peptide 204–212 may represent the active site responsible for the anti‐inflammatory properties of lipocortin 5.