TY - JOUR
T1 - Adsorption kinetics of high mobility group box 1 protein in a polyacrylonitrile hemofiltration membrane
AU - Nakamura, Tomoyuki
AU - Moriyama, Kazuhiro
AU - Shimomura, Yasuyo
AU - Kato, Yu
AU - Kuriyama, Naohide
AU - Hara, Yoshitaka
AU - Yamada, Shingo
AU - Nishida, Osamu
N1 - Publisher Copyright:
© 2020 International Society for Apheresis, Japanese Society for Apheresis, and Japanese Society for Dialysis Therapy
PY - 2021/2
Y1 - 2021/2
N2 - The high mobility group box 1 protein (HMGB1) is recognized as a prototypical endogenous danger cytokine in sepsis. We previously reported that a polyacrylonitrile (AN69ST) membrane rapidly adsorbed HMGB1. Herein, an in vitro hemofiltration system was designed to assess the HMGB1 adsorption capacity, adsorption sites, and adsorption mechanism of the AN69ST membrane. HMGB1 was repeatedly added seven times during hemofiltration. A rapid decrease in circulating HMGB1 was observed after every addition with no sign of saturation. Presence of HMGB1 on the filter membrane was observed on both membrane surfaces and within the bulk layer using a high concentration of HMGB1 by immunoelectron microscopy. We hypothesized that the addition of heparin to the membrane surface or filtration rate would contribute to the adsorption mechanism. We could not measure the influence of heparin and filtration. Although the membrane was too large to saturate under the μg/mL HMGB1 conditions, our results show that the AN69ST membrane has a robust absorption capacity that could be used to treat sepsis.
AB - The high mobility group box 1 protein (HMGB1) is recognized as a prototypical endogenous danger cytokine in sepsis. We previously reported that a polyacrylonitrile (AN69ST) membrane rapidly adsorbed HMGB1. Herein, an in vitro hemofiltration system was designed to assess the HMGB1 adsorption capacity, adsorption sites, and adsorption mechanism of the AN69ST membrane. HMGB1 was repeatedly added seven times during hemofiltration. A rapid decrease in circulating HMGB1 was observed after every addition with no sign of saturation. Presence of HMGB1 on the filter membrane was observed on both membrane surfaces and within the bulk layer using a high concentration of HMGB1 by immunoelectron microscopy. We hypothesized that the addition of heparin to the membrane surface or filtration rate would contribute to the adsorption mechanism. We could not measure the influence of heparin and filtration. Although the membrane was too large to saturate under the μg/mL HMGB1 conditions, our results show that the AN69ST membrane has a robust absorption capacity that could be used to treat sepsis.
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U2 - 10.1111/1744-9987.13489
DO - 10.1111/1744-9987.13489
M3 - Article
C2 - 32216030
AN - SCOPUS:85083700928
SN - 1744-9979
VL - 25
SP - 66
EP - 72
JO - Therapeutic Apheresis and Dialysis
JF - Therapeutic Apheresis and Dialysis
IS - 1
ER -