Plasma proteins to work on sepsis; making the functions of inter-α inhibitors clear
August 16(Thu), 2018
A collaborative research project consisting of a group led by Professor Masahiro Nishibori from the Department of Pharmacology at the Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University and Brown University in the U.S. found that functions of inter-α inhibitor proteins, one of the plasma proteins, get expressed through a leukocyte’s morphology and function controls. This research result was published in the American science journal Blood Advances in its August 14th issue.
This research group has already reported in the past that another plasma protein called histidine-rich glycoprotein (HRG) has an antiseptic effect. In this research, the group found that inter-α inhibitor proteins control the functions of neutrophils in a slightly different way from HRG.
Both inter-α inhibitor proteins and HRG are glycoproteins that are produced in the liver and secreted into the blood. They may play a similar function, but their functions are recognized to be different with regard to the control of cytoskeletal arrangement and expression of cell-surface molecules. Therefore, the possibility of the blood-vessel homeostasis being maintained by combining several plasma proteins with different functions to control interactions of circulating neutrophils and vascular endothelial cells was strongly suggested. It is possible that this mechanism would be broken in the case of sepsis. Further research to develop treatment for sepsis is anticipated.
Journal: Blood Advances
Authors: Soe Soe Htwe, Hidenori Wake, Keyue Liu, Kiyoshi Teshigawara, Barbara S. Stonestreet, Yow-Pin Lim, Masahiro Nishibori
Title: Inter-alpha inhibitor proteins maintain neutrophils in a resting state by regulating shape and reducing ROS production
Year of Publication: 2018
Okayama University Silicon Valley Office (OUSVO)
Contact: Mototaka Senda, Ph.D.