Fibrinogen-CD11b/CD18 interaction activities the NF-kappa B pathway and delays apoptosis in human neutrophils

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Fibrinogen-CD11b/CD18 interaction activities the NF-kappa B pathway and delays apoptosis in human neutrophils. / Rubel, C; Gomez, S; Fernandez, GC; Isturiz, MA; Caamano, Jorge; Palermo, MS.

In: European Journal of Immunology, Vol. 33, No. 5, 01.05.2003, p. 1429-38.

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Rubel, C ; Gomez, S ; Fernandez, GC ; Isturiz, MA ; Caamano, Jorge ; Palermo, MS. / Fibrinogen-CD11b/CD18 interaction activities the NF-kappa B pathway and delays apoptosis in human neutrophils. In: European Journal of Immunology. 2003 ; Vol. 33, No. 5. pp. 1429-38.

Bibtex

@article{99794b3fbcfb4501af5b2ba8f9f0636f,
title = "Fibrinogen-CD11b/CD18 interaction activities the NF-kappa B pathway and delays apoptosis in human neutrophils",
abstract = "The regulation of neutrophil half-life by members of the coagulation cascade is critical for the resolution of the inflammatory response. We have demonstrated that soluble fibrinogen (sFbg) delays human neutrophil (PMN) apoptosis through a mechanism that involves CD11b interactions, and phosphorylation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase 1/2 (ERK1/2). Since NF-kappaB is a key element in the regulation of apoptotic mechanisms in several immune cells, we investigated whether NF-kappaB is involved in the control of PMN survival by sFbg. We show that sFbg triggers inhibitor protein kappaB (IkappaB-alpha) degradation and NF-kappaB activation. Furthermore, pharmacological inhibition of NF-kappaB abrogates sFbg effects on apoptosis. In addition, specific inhibition of MAPK ERK1/2 significantly reduces NF-kappaB translocation by sFbg, suggesting a relationship between ERK1/2 and NF-kappaB activation. Similar results are obtained when granulocytic-differentiated HL-60 cells are treated with sFbg, making this model highly attractive for integrin-induced gene expression studies. It can be concluded that NF-kappaB participates in the prevention of apoptosis induced by sFbg with the participation of MAPK ERK1/2. These results shed light on the molecular mechanisms that control human granulocyte apoptosis, and suggest that NF-kappaB regulation may be of benefit for the resolution of the inflammatory response.",
keywords = "NF-kappa B, integrin, apoptosis, fibrinogen, neutrophil",
author = "C Rubel and S Gomez and GC Fernandez and MA Isturiz and Jorge Caamano and MS Palermo",
year = "2003",
month = may,
day = "1",
doi = "10.1002/eji.200323512",
language = "English",
volume = "33",
pages = "1429--38",
journal = "European Journal of Immunology",
issn = "0014-2980",
publisher = "Wiley-VCH Verlag",
number = "5",

}

RIS

TY - JOUR

T1 - Fibrinogen-CD11b/CD18 interaction activities the NF-kappa B pathway and delays apoptosis in human neutrophils

AU - Rubel, C

AU - Gomez, S

AU - Fernandez, GC

AU - Isturiz, MA

AU - Caamano, Jorge

AU - Palermo, MS

PY - 2003/5/1

Y1 - 2003/5/1

N2 - The regulation of neutrophil half-life by members of the coagulation cascade is critical for the resolution of the inflammatory response. We have demonstrated that soluble fibrinogen (sFbg) delays human neutrophil (PMN) apoptosis through a mechanism that involves CD11b interactions, and phosphorylation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase 1/2 (ERK1/2). Since NF-kappaB is a key element in the regulation of apoptotic mechanisms in several immune cells, we investigated whether NF-kappaB is involved in the control of PMN survival by sFbg. We show that sFbg triggers inhibitor protein kappaB (IkappaB-alpha) degradation and NF-kappaB activation. Furthermore, pharmacological inhibition of NF-kappaB abrogates sFbg effects on apoptosis. In addition, specific inhibition of MAPK ERK1/2 significantly reduces NF-kappaB translocation by sFbg, suggesting a relationship between ERK1/2 and NF-kappaB activation. Similar results are obtained when granulocytic-differentiated HL-60 cells are treated with sFbg, making this model highly attractive for integrin-induced gene expression studies. It can be concluded that NF-kappaB participates in the prevention of apoptosis induced by sFbg with the participation of MAPK ERK1/2. These results shed light on the molecular mechanisms that control human granulocyte apoptosis, and suggest that NF-kappaB regulation may be of benefit for the resolution of the inflammatory response.

AB - The regulation of neutrophil half-life by members of the coagulation cascade is critical for the resolution of the inflammatory response. We have demonstrated that soluble fibrinogen (sFbg) delays human neutrophil (PMN) apoptosis through a mechanism that involves CD11b interactions, and phosphorylation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase 1/2 (ERK1/2). Since NF-kappaB is a key element in the regulation of apoptotic mechanisms in several immune cells, we investigated whether NF-kappaB is involved in the control of PMN survival by sFbg. We show that sFbg triggers inhibitor protein kappaB (IkappaB-alpha) degradation and NF-kappaB activation. Furthermore, pharmacological inhibition of NF-kappaB abrogates sFbg effects on apoptosis. In addition, specific inhibition of MAPK ERK1/2 significantly reduces NF-kappaB translocation by sFbg, suggesting a relationship between ERK1/2 and NF-kappaB activation. Similar results are obtained when granulocytic-differentiated HL-60 cells are treated with sFbg, making this model highly attractive for integrin-induced gene expression studies. It can be concluded that NF-kappaB participates in the prevention of apoptosis induced by sFbg with the participation of MAPK ERK1/2. These results shed light on the molecular mechanisms that control human granulocyte apoptosis, and suggest that NF-kappaB regulation may be of benefit for the resolution of the inflammatory response.

KW - NF-kappa B

KW - integrin

KW - apoptosis

KW - fibrinogen

KW - neutrophil

UR - http://www.scopus.com/inward/record.url?scp=0038297125&partnerID=8YFLogxK

U2 - 10.1002/eji.200323512

DO - 10.1002/eji.200323512

M3 - Article

C2 - 12731070

VL - 33

SP - 1429

EP - 1438

JO - European Journal of Immunology

JF - European Journal of Immunology

SN - 0014-2980

IS - 5

ER -