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A novel bioactive 31‐amino acid endothelin‐1 is a potent chemotactic peptide for human neutrophils and monocytes
Author(s) -
Cui Ping,
Tani Kenji,
Kitamura Hiroko,
Okumura Yuushi,
Yano Mihiro,
Inui Daisuke,
Tamaki Toshiaki,
Sone Saburo,
Kido Hiroshi
Publication year - 2001
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.70.2.306
Subject(s) - chemotaxis , biology , monocyte , receptor , peptide , biochemistry , receptor antagonist , interleukin 8 , inflammation , antagonist , immunology
Endothelin (ET)‐1(1‐31) is a novel 31‐amino acid‐length peptide derived from big ET‐1 by chymase or other chymotrypsin‐type proteases and is a major ET derivative in human neutrophils. In this study, we revealed that ET‐1(1‐31), but not big ET, exhibited chemotactic activities toward human neutrophils and monocytes as an inflammatory mediator, although the effects were less potent than those of formyl‐methionyl‐leucyl‐phenylalanine or interleukin‐8. However, the chemotactic effects of ET‐1(1‐31) were much greater than those of the 21‐amino acid ET‐1, ET‐1(1‐21). Checkerboard analyses revealed that the effects are chemotactic rather than chemokinetic. The effects of ET‐1(1‐31) are not mediated by interleukin‐8 or monocyte chemoattractant protein‐1. The chemotactic effects and an increase in intracellular‐free Ca 2+ caused by ET‐1(1‐31) were significantly inhibited by BQ123, an ET A receptor antagonist, but not by BQ788, an ET B receptor antagonist, suggesting that ET‐1(1‐31) mediates chemotaxis through an ET A or ET A ‐like receptor.