Title : Glutaredoxin 1 up-regulates deglutathionylation of α4 integrin and thereby restricts neutrophil mobilization from bone marrow.

Pub. Date : 2019 Feb 22

PMID : 30598505






5 Functional Relationships(s)
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1 Although alpha4 integrin is known to be a potential target of reactive oxygen species (ROS)-induced cysteine glutathionylation, the physiological significance and underlying regulatory mechanism of this event remain elusive. Reactive Oxygen Species immunoglobulin (CD79A) binding protein 1 Mus musculus
2 Although alpha4 integrin is known to be a potential target of reactive oxygen species (ROS)-induced cysteine glutathionylation, the physiological significance and underlying regulatory mechanism of this event remain elusive. Reactive Oxygen Species immunoglobulin (CD79A) binding protein 1 Mus musculus
3 Here, using in vitro and in vivo biochemical and cell biology approaches, we show that physiological ROS-induced glutathionylation of alpha4 integrin in neutrophils increases the binding of neutrophil-associated alpha4 integrin to vascular cell adhesion molecule 1 (VCAM-1) on human endothelial cells. Reactive Oxygen Species immunoglobulin (CD79A) binding protein 1 Mus musculus
4 Here, using in vitro and in vivo biochemical and cell biology approaches, we show that physiological ROS-induced glutathionylation of alpha4 integrin in neutrophils increases the binding of neutrophil-associated alpha4 integrin to vascular cell adhesion molecule 1 (VCAM-1) on human endothelial cells. Reactive Oxygen Species immunoglobulin (CD79A) binding protein 1 Mus musculus
5 Taken together, our results establish ROS-elicited glutathionylation and its modulation by Grx1 as pivotal regulatory mechanisms controlling alpha4 integrin affinity and neutrophil mobilization from the bone marrow under physiological conditions. Reactive Oxygen Species immunoglobulin (CD79A) binding protein 1 Mus musculus