Does formyl-methionyl-leucyl-phenylalanine exert a physiological role in labor in women?

被引:7
作者
Buzzi, M
Vesce, F
Ferretti, ME
Fabbri, E
Biondi, C
机构
[1] Univ Ferrara, Dept Biol, Sect Gen Physiol, I-44100 Ferrara, Italy
[2] Univ Ferrara, Dept Biomed Sci & Adv Therapy, Sect Obstet & Gynecol, I-44100 Ferrara, Italy
[3] Univ Bologna, Dept Biol, I-40100 Bologna, Italy
关键词
D O I
10.1095/biolreprod60.5.1211
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
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-butoxycarbonylmethionyl-leucyl-phenylatanine (Boc-MLP), a formyl peptide receptor antagonist, inhibited H-3-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.
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页码:1211 / 1216
页数:6
相关论文
共 24 条
[1]   SEQUENCE IDENTIFICATION OF 2,375 HUMAN BRAIN GENES [J].
ADAMS, MD ;
DUBNICK, M ;
KERLAVAGE, AR ;
MORENO, R ;
KELLEY, JM ;
UTTERBACK, TR ;
NAGLE, JW ;
FIELDS, C ;
VENTER, JC .
NATURE, 1992, 355 (6361) :632-634
[2]   BINDING OF CHEMOTACTIC PEPTIDE TO THE OUTER SURFACE AND TO WHOLE HUMAN-SPERMATOZOA WITH DIFFERENT AFFINITY STATES [J].
BALLESTEROS, LM ;
DELGADO, NM ;
ROSADO, A ;
CORREA, C ;
HERNANDEZPEREZ, O .
GAMETE RESEARCH, 1988, 20 (02) :233-239
[3]   ARACHIDONIC-ACID METABOLISM IN POLYMORPHONUCLEAR LEUKOCYTES .3. EFFECTS OF IONOPHORE-A23187 [J].
BORGEAT, P ;
SAMUELSSON, B .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1979, 76 (05) :2148-2152
[4]   CYTOKINES RELEASED BY GRANULOCYTES ACID MONONUCLEAR-CELLS STIMULATE AMNION CELL PROSTAGLANDIN E(2) PRODUCTION [J].
BRY, K ;
HALLMAN, M ;
LAPPALAINEN, U .
PROSTAGLANDINS & OTHER LIPID MEDIATORS, 1994, 48 (06) :389-399
[5]   MITOCHONDRIAL N-FORMYLMETHIONYL PROTEINS AS CHEMOATTRACTANTS FOR NEUTROPHILS [J].
CARP, H .
JOURNAL OF EXPERIMENTAL MEDICINE, 1982, 155 (01) :264-275
[6]  
Cochrane CG, 1990, CELLULAR MOL MECHANI, P83
[7]   G-PROTEIN-REGULATED PHOSPHOLIPASE-C, PHOSPHOLIPASE-D AND PHOSPHOLIPASE-A(2)-MEDIATED SIGNALING IN NEUTROPHILS [J].
COCKCROFT, S .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1113 (02) :135-160
[8]   FURTHER-STUDIES ON THE STRUCTURAL REQUIREMENTS FOR SYNTHETIC PEPTIDE CHEMOATTRACTANTS [J].
FREER, RJ ;
DAY, AR ;
RADDING, JA ;
SCHIFFMANN, E ;
ASWANIKUMAR, S ;
SHOWELL, HJ ;
BECKER, EL .
BIOCHEMISTRY, 1980, 19 (11) :2404-2410
[9]   UP-REGULATION OF OXYTOCIN RECEPTORS IN RABBIT AMNION BY ADENOSINE-3',5'-MONOPHOSPHATE [J].
HINKO, A ;
SOLOFF, MS .
ENDOCRINOLOGY, 1993, 132 (01) :126-132
[10]   Interleukin (IL)-6 and IL-8 production by human amnion: Regulation by cytokines, growth factors, glucocorticoids, phorbol esters, and bacterial lipopolysaccharide [J].
Keelan, JA ;
Sato, T ;
Mitchell, MD .
BIOLOGY OF REPRODUCTION, 1997, 57 (06) :1438-1444