PMID- 11207202
OWN - NLM
STAT- MEDLINE
DCOM- 20010531
LR  - 20190513
IS  - 0006-3363 (Print)
IS  - 0006-3363 (Linking)
VI  - 64
IP  - 3
DP  - 2001 Mar
TI  - Formyl-methionyl-leucyl-phenylalanine induces prostaglandin E2 release from human 
      amnion-derived WISH cells by phospholipase C-mediated [Ca+]i rise.
PG  - 865-70
AB  - The presence of binding sites for formyl-methionyl-leucyl-phenylalanine (fMLP), 
      its effect on prostaglandin E (PGE) release, and the signal transduction pathway 
      activated by the peptide were investigated in human amnion-derived WISH cells. 
      Our results demonstrate that specific binding sites for fMLP are present on WISH 
      cells and that the peptide induces a significant increase of prostaglandin (PG)E2 
      release. The kinetic properties of binding are similar to those previously found 
      in amnion tissue prior to the onset of labor, i.e., only one population of 
      binding sites with low affinity for the peptide is present. Binding of 3H-fMLP in 
      WISH cells is inhibited by N-t-butoxycarbonyl-methionyl-leucyl-phenylalanine, an 
      fMLP receptor antagonist, with an IC50 value very close to that shown by 
      nonlaboring amnion. The fMLP-induced PGE2 output is inhibited by indomethacin, 
      quinacrine, and U-73122, inhibitors of cyclooxygenase, phospholipase A2, and 
      phospholipase C, respectively. As regards the transduction pathway activated by 
      fMLP, we demonstrate that phospholipase C activation, followed by an increase of 
      intracellular calcium concentration ([Ca2+]i), is involved in response to the 
      peptide. Our results add further evidence to the role of proinflammatory agents 
      in the determination of labor. Furthermore, because WISH cells appear to behave 
      like nonlaboring amnion tissue, they represent the ideal candidate for in vitro 
      investigation of the events triggering the mechanism of delivery.
FAU - Biondi, C
AU  - Biondi C
AD  - Department of Biology, Section of General Physiology, University of Ferrara, 
      44100-I Ferrara, Italy. clm@dns.unife.it
FAU - Pavan, B
AU  - Pavan B
FAU - Ferretti, M E
AU  - Ferretti ME
FAU - Corradini, F G
AU  - Corradini FG
FAU - Neri, L M
AU  - Neri LM
FAU - Vesce, F
AU  - Vesce F
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biol Reprod
JT  - Biology of reproduction
JID - 0207224
RN  - 0 (Cyclooxygenase Inhibitors)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Estrenes)
RN  - 0 (Oligopeptides)
RN  - 0 (Pyrrolidinones)
RN  - 112648-68-7 
      (1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione)
RN  - 59880-97-6 (N-Formylmethionine Leucyl-Phenylalanine)
RN  - 67247-12-5 (t-butyloxycarbonyl-methionyl-leucyl-phenylalanine)
RN  - EC 3.1.4.- (Type C Phospholipases)
RN  - H0C805XYDE (Quinacrine)
RN  - K7Q1JQR04M (Dinoprostone)
RN  - SY7Q814VUP (Calcium)
RN  - XXE1CET956 (Indomethacin)
SB  - IM
MH  - Amnion/*drug effects/enzymology/metabolism
MH  - Binding Sites
MH  - Calcium/*metabolism/physiology
MH  - Cell Line
MH  - Cyclooxygenase Inhibitors/pharmacology
MH  - Dinoprostone/biosynthesis/*metabolism
MH  - Enzyme Inhibitors/pharmacology
MH  - Estrenes/pharmacology
MH  - Humans
MH  - Indomethacin/pharmacology
MH  - Microscopy, Confocal
MH  - N-Formylmethionine Leucyl-Phenylalanine/metabolism/*pharmacology
MH  - Oligopeptides/pharmacology
MH  - Pyrrolidinones/pharmacology
MH  - Quinacrine/pharmacology
MH  - Radioimmunoassay
MH  - Signal Transduction/drug effects/physiology
MH  - Type C Phospholipases/antagonists & inhibitors/*physiology
EDAT- 2001/02/24 11:00
MHDA- 2001/06/02 10:01
CRDT- 2001/02/24 11:00
PHST- 2001/02/24 11:00 [pubmed]
PHST- 2001/06/02 10:01 [medline]
PHST- 2001/02/24 11:00 [entrez]
AID - 10.1095/biolreprod64.3.865 [doi]
PST - ppublish
SO  - Biol Reprod. 2001 Mar;64(3):865-70. doi: 10.1095/biolreprod64.3.865.