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(Journal of Leukocyte Biology. 2001;70:306-312.)
© 2001 by Society for Leukocyte Biology

A novel bioactive 31-amino acid endothelin-1 is a potent chemotactic peptide for human neutrophils and monocytes

Ping Cui, Kenji Tani^*, Hiroko Kitamura, Yuushi Okumura, Mihiro Yano, Daisuke Inui, Toshiaki Tamaki, Saburo Sone^* and Hiroshi Kido

Division of Enzyme Chemistry, Institute for Enzyme Research,
^* Third Department of Internal Medicine, and
Department of Pharmacology, School of Medicine, The University of Tokushima, Tokushima, Japan

Correspondence: Hiroshi Kido, Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Kuramoto-cho 3-18-15, Tokushima 770-8503, Japan. E-mail: kido{at}ier.tokushima-u.ac.jp

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 Ca²⁺ 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.

Key Words: chemotaxis • endothelin-1(1-31) • endothelin-1(1-21) • Ca²⁺ mobilization

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