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F2L, a peptide derived from heme-binding protein, inhibits formyl peptide receptor-mediated signaling SCIE SCOPUS

Title
F2L, a peptide derived from heme-binding protein, inhibits formyl peptide receptor-mediated signaling
Authors
Lee, HYLee, SYShin, EHKim, SDKim, JMLee, MSRyu, SHBae, YS
Date Issued
2007-08-10
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Abstract
F2L is an acetylated amino-terminal peptide derived from the cleavage of the human heme-binding protein. Very recently, F2L was identified as an endogenous chemoattractant peptide acting specifically through formyl peptide receptor-like (FPRL)2. In the present study, we report that F2L stimulates chemotactic migration in human neutrophils. However, F2L inhibits formyl peptide receptor (FPR) and FPRL1 activities, resulting in the complete inhibition of intracellular calcium increases, and superoxide generation induced by N-formyl-Met-Leu-Phe, MMK-1, or Trp-Lys-Tyr-Met-Val-D-Met (WKYMVm) in human neutrophils. In terms of the inhibitory role of F2L on FPR- and FPRL-mediated signaling, we found that F2L competitively inhibits the binding of I-125-WKYMVm to its specific receptors, FPR and FPRL1. F2L is the first endogenous molecule that inhibits FPR- and FPRL1-mediated signaling, and is expected to be useful in the study of FPR and FPRL1 signaling and in the development of drugs to treat diseases involving the FPR family of receptors. (c) 2007 Elsevier Inc. All rights reserved.
Keywords
F2L; formyl peptide receptor; neutrophil; superoxide generation; fMLF; WKYMVm; N-FORMYLPEPTIDE RECEPTOR; COUPLED RECEPTOR; DIFFERENTIAL ACTIVATION; NEUTROPHIL ACTIVATION; IDENTIFICATION; 7-TRANSMEMBRANE; MONOCYTES; CELLS; FPRL1; CHEMOTAXIS
URI
https://oasis.postech.ac.kr/handle/2014.oak/23303
DOI
10.1016/j.bbrc.2007.06.001
ISSN
0006-291X
Article Type
Article
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, vol. 359, no. 4, page. 985 - 990, 2007-08-10
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류성호RYU, SUNG HO
Dept of Life Sciences
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