TY - JOUR
T1 - Exposure of HL-60 human leukaemic cells to 4-hydroxynonenal promotes the formation of adduct(s) with α-enolase devoid of plasminogen binding activity
AU - Gentile, Fabrizio
AU - Pizzimenti, Stefania
AU - Arcaro, Alessia
AU - Pettazzoni, Piergiorgio
AU - Minelli, Rosalba
AU - D'Angelos, Daniela
AU - Mamone, Gianfranco
AU - Ferranti, Pasquale
AU - Toaldo, Cristina
AU - Cetrangolo, Gianpaolo
AU - Formisano, Silvestro
AU - Dianzani, Mario U.
AU - Uchida, Koji
AU - Dianzani, Chiara
AU - Barrera, Giuseppina
N1 - Copyright:
Copyright 2019 Elsevier B.V., All rights reserved.
PY - 2009/9/1
Y1 - 2009/9/1
N2 - HNE (4-hydroxynonenal), the major product of lipoperoxidation, easily reacts with proteins through adduct formation between its three main functional groups and lysyl, histidyl and cysteinyl residues of proteins. HNE is considered to be an ultimate mediator of toxic effects elicited by oxidative stress. It can be detected in several patho-physiological conditions, in which it affects cellular processes by addition to functional proteins. We demonstrated in the present study, by MS and confirmed by immunoblotting experiments, the formation of HNE - α-enolase adduct(s) in HL-60 human leukaemic cells. α-Enolase is a multifunctional protein that acts as a glycolytic enzyme, transcription factor [MBP-1 (c-myc binding protein-1)] and plasminogen receptor. HNE did not affect α-enolase enzymatic activity, expression or intracellular localization, and did not change the expression and localization of MBP-1 either. Confocal and electronic microscopy results confirmed the plasma membrane, cytosolic and nuclear localization of α-enolase in HL-60 cells and demonstrated that HNE was colocalized with α-enolase at the surface of cells early after its addition. HNE caused a dose- and time-dependent reduction of the binding of plasminogen to α-enolase. As a consequence, HNE reduced adhesion of HL-60 cells to HUVECs (human umbilical vein endothelial cells). These results could suggest a new role for HNE in the control of tumour growth and invasion.
AB - HNE (4-hydroxynonenal), the major product of lipoperoxidation, easily reacts with proteins through adduct formation between its three main functional groups and lysyl, histidyl and cysteinyl residues of proteins. HNE is considered to be an ultimate mediator of toxic effects elicited by oxidative stress. It can be detected in several patho-physiological conditions, in which it affects cellular processes by addition to functional proteins. We demonstrated in the present study, by MS and confirmed by immunoblotting experiments, the formation of HNE - α-enolase adduct(s) in HL-60 human leukaemic cells. α-Enolase is a multifunctional protein that acts as a glycolytic enzyme, transcription factor [MBP-1 (c-myc binding protein-1)] and plasminogen receptor. HNE did not affect α-enolase enzymatic activity, expression or intracellular localization, and did not change the expression and localization of MBP-1 either. Confocal and electronic microscopy results confirmed the plasma membrane, cytosolic and nuclear localization of α-enolase in HL-60 cells and demonstrated that HNE was colocalized with α-enolase at the surface of cells early after its addition. HNE caused a dose- and time-dependent reduction of the binding of plasminogen to α-enolase. As a consequence, HNE reduced adhesion of HL-60 cells to HUVECs (human umbilical vein endothelial cells). These results could suggest a new role for HNE in the control of tumour growth and invasion.
KW - 4-Hydroxynonenal (4-HNE)
KW - 4-Hydroxynonenal adducts
KW - Cell adhesion
KW - HL-60 cells
KW - Plasminogen binding
KW - α-Enolase
UR - http://www.scopus.com/inward/record.url?scp=70149101099&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=70149101099&partnerID=8YFLogxK
U2 - 10.1042/BJ20090564
DO - 10.1042/BJ20090564
M3 - Article
C2 - 19508232
AN - SCOPUS:70149101099
SN - 0264-6021
VL - 422
SP - 285
EP - 294
JO - Biochemical Journal
JF - Biochemical Journal
IS - 2
ER -