Primary granule release from human neutrophils is potentiated by soluble fibrinogen through a mechanism depending on multiple intracellular signaling pathways

American Journal of Physiology. Cell Physiology
Florin TulucSatya P Kunapuli

Abstract

N-Formyl-methionyl-leucyl-phenylalanine (fMLP) is a potent activator of neutrophil degranulation. The intracellular signaling mechanisms involved in the potentiating effect of fibrinogen on fMLP-induced primary granule release from human neutrophils were investigated. Fibrinogen caused a significant leftward shift of the concentration-response curve of fMLP-induced elastase release. An antibody against Mac-1 (CD11b/CD18) prevented the potentiating effect of fibrinogen, suggesting that soluble fibrinogen potentiates fMLP-induced degranulating effect by a mechanism mediated by the integrin Mac-1. Fibrinogen enhanced fMLP-induced tyrosine phosphorylation in human neutrophils and markedly enhanced the phosphorylation of mitogen-activated protein kinases (MAPK) caused by fMLP. However, U0126, an inhibitor of p44/42 MAPK activation, or SB-203580, an inhibitor of p38 MAPK, did not alter the effect of fibrinogen on fMLP-induced elastase release. Wortmannin, a phosphatidylinositol 3-kinase (PI3K) kinase inhibitor, and genistein, a nonspecific tyrosine kinase inhibitor, strongly inhibited fMLP-induced elastase release both in the presence and in the absence of fibrinogen. An Akt/PKB inhibitor failed to alter the potentiating effect of fi...Continue Reading

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Citations

Jan 1, 2005·Indian Journal of Clinical Biochemistry : IJCB·Mohammad Muzaffar MirMohammad Salahuddin
Jan 21, 2011·The Journal of Biological Chemistry·Ya-Ping KoMagnus Höök
Nov 25, 2005·Artificial Organs·Ann Elisabeth Asberg, Vibeke Videm
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Aug 25, 2021·Seminars in Thrombosis and Hemostasis·Katherine J KearneyFraser L Macrae

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