The synthetic peptide, His-Phe-Tyr-Leu-Pro-Met, is a chemoattractant for Jukat T cells.
- Author:
Youn Dong KIM
1
;
Yoe Sik BAE
;
Jun Chul PARK
;
Pann Ghill SUH
;
Sung Ho RYU
Author Information
1. Division of Molecular and Life Sciences, Pohang University of Science and Technology, Korea.
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
chemotaxis;
peptide;
G-protein coupled receptor
- MeSH:
1-Phosphatidylinositol 3-Kinase/metabolism;
Androstadienes/pharmacology;
Calcium/metabolism;
Cell Line;
Chemokines, CXC/*pharmacology;
Chemotaxis, Leukocyte/drug effects/*physiology;
Dose-Response Relationship, Drug;
Genistein/pharmacology;
Human;
Jurkat Cells;
Oligopeptides;
Peptide Fragments/chemical synthesis/metabolism/*physiology;
Pertussis Toxin;
Phospholipase C/metabolism;
Protein-Tyrosine Kinase/metabolism;
Signal Transduction/drug effects;
T-Lymphocytes/*drug effects;
Virulence Factors, Bordetella/pharmacology
- From:Experimental & Molecular Medicine
2001;33(4):257-262
- CountryRepublic of Korea
- Language:English
-
Abstract:
His-Phe-Tyr-Leu-Pro-Met (HFYLPM) is a synthetic peptide that stimulates Jurkat T cells resulting in intracellular calcium ([Ca2+]i) increase in a pertussis toxin (PTX)-sensitive manner. We have examined the physiological role of the peptide in T cell activity by comparative investigation of intracellular signaling pathways accompanied with HFYLPM-induced T cell chemotaxis with a well-known chemokine, stromal cell-derived factor-1 (SDF-1)-induced signalings. Wortmannin and genistein inhibited both of HFYLPM- and SDF-1-induced Jurkat T cell chemotaxis indicating that phosphoinositide-3-kinase and tyrosine kinase activity were required for the processes. However, U-73122 and BAPTA/AM preferentially blocked HFYLPM- but not SDF-1-induced T cell chemotaxis. It indicates that phospholipase C/calcium signaling is necessary for only chemotaxis by HFYLPM. One of the well-known cellular molecules involving chemotaxis, extracellular signal-regulated protein kinase (ERK), was activated by SDF-1 but not by HFYLPM ruling out a possible role of ERK on the peptide-mediated chemotaxis. These results indicate that the synthetic peptide, HFYLPM, stimulates T cell chemotaxis showing unique signaling and provide a useful tool for the study of T cell activation mechanism.
