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LTB4 IS A SIGNAL RELAY MOLECULE DURING NEUTROPHIL CHEMOTAXIS
Published
Author(s)
Philippe V. Afonso, Mirkka Janka-Junttila, Young Jong Lee, Colin P. McCann, Charlotte M. Oliver, Khaled A. Aamer, Wolfgang Losert, Marcus T. Cicerone, Carol A. Parent
Abstract
Neutrophil recruitment to inflammation sites purportedly depends on sequential waves of chemoattractants. Current models propose that LTB4, a secondary chemoattractant secreted by neutrophils in response to primary chemoattractants such as formyl-peptides, is only important in initiating the inflammation process. In this study, we demonstrate that LTB4 plays a central role in neutrophil activation and migration to formyl-peptides. We show that LTB4 production dramatically amplifies formyl-peptide-mediated neutrophil polarization and chemotaxis by regulating specific signaling pathways acting upstream of actin polymerization and MyoII phosphorylation. Importantly, by analyzing the migration of neutrophils isolated from WT mice and mice lacking the formyl receptor 1, we demonstrate that LTB4 acts as a signal to relay information from cell-to-cell over long distances. Together, our findings imply that LTB4 is a signal relay molecule that exquisitely regulates neutrophils chemotaxis to the core of inflammation sites throughout the inflammation process.
Afonso, P.
, Janka-Junttila, M.
, Lee, Y.
, McCann, C.
, Oliver, C.
, Aamer, K.
, Losert, W.
, Cicerone, M.
and Parent, C.
(2012),
LTB4 IS A SIGNAL RELAY MOLECULE DURING NEUTROPHIL CHEMOTAXIS, Developmental Cell, [online], https://doi.org/10.1016/j.devcel.2012.02.003, https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=909240
(Accessed October 13, 2025)