Open AccessImportance of glycosylation in the interaction of Tamm‐Horsfall protein with collectin‐11 and acute kidney injury
Author(s) -
Gong Kunjing,
Xia Min,
Wang Yaqin,
Bai Lufeng,
Ying Wantao,
Zhu Fengxue,
Chen Yuqing
Publication year - 2020
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/jcmm.15046
Subject(s) - collectin , fucosylation , fucose , lectin , glycosylation , mannan binding lectin , complement system , glycoprotein , glycan , mannose , acute kidney injury , chemistry , lectin pathway , in vitro , biochemistry , biology , alternative complement pathway , medicine , immunology , receptor , innate immune system , antibody
Both Tamm‐Horsfall protein (THP) and collectin‐11 (CL‐11) are important molecules in acute kidney injury (AKI). In this study, we measured the change of glycosylation of THP in patients with AKI after surgery, using MALDI‐TOF MS and lectin array analysis. The amount of high‐mannose and core fucosylation in patients with AKI were higher than those in healthy controls. In vitro study showed that THP could bind to CL‐11 with affinity at 9.41 × 10 −7 mol/L and inhibited activation of complement lectin pathway. The binding affinity decreased after removal of glycans on THP. Removal of fucose completely ablated the binding between the two proteins. While removal of high‐mannose or part of the N‐glycan decreased the binding ability to 30% or 60%. The results indicated that increase of fucose on THP played an important role via complement lectin pathway in AKI.