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Does Formyl-Methionyl-Leucyl-Phenylalanine Exert a Physiological Role in Labor in Women?¹

^a Department of Biology, Section of General Physiology, University of Ferrara, 44100-I Ferrara, Italy ^b Department of Biomedical Sciences and Advanced Therapy, Section of Obstetrics and Gynecology, University of Ferrara, 44100-Ferrara, Italy ^c Department of Biology, University of Bologna, 40100 Bologna, Italy

The classical chemotactic receptor for N-formyl peptides has traditionally been associated with polymorphonuclear and mononuclear phagocytes; however, several recent reports indicate that this receptor is also expressed in non-myeloid cells. In this study we have investigated the presence of binding sites for formyl-methionyl-leucyl-phenylalanine (fMLP) in human amniotic membranes of laboring and nonlaboring women; we have also evaluated the effect of the peptide on prostaglandin E (PGE) release from the same tissue. Our results demonstrate the presence of specific, saturable binding sites for ³H-fMLP; Scatchard plot analysis suggests the presence of both high- and low-affinity binding sites in laboring amnion, while only the low-affinity receptors were evident in nonlaboring tissue. N-t-butoxycarbonyl-methionyl-leucyl-phenylalanine (Boc-MLP), a formyl peptide receptor antagonist, inhibited ³H-fMLP binding in both preparations. In addition, fMLP was able to significantly increase PGE synthesis in perifused amnion fragments from laboring and nonlaboring women. This effect was counteracted by Boc-MLP treatment. The presence of specific binding sites for fMLP in amniotic tissue and their differing expression in laboring versus nonlaboring membranes, together with the action of the peptide on PGE synthesis, all suggest a physiological role for fMLP in labor.

¹ Supported by grants from Ministero dell'Università e della Ricerca Scientifica e Tecnologica (40% and 60%) and from Azienda Ospedaliera di Ferrara, Arcispedale Sant'Anna.

² Correspondence: Carla Biondi, Department of Biology, Section of General Physiology, University of Ferrara, via L. Borsari, 46, 44100-I Ferrara, Italy. FAX: 0532 207143; clm{at}dns.unife.it

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