Abstract
Acute-on-chronic hepatitis B liver failure (ACHBLF) is an increasingly recognized distinct disease entity encompassing an acute deterioration of liver function in patients with cirrhosis, so little is known about the alterations of protein glycopatterns in serum with its development. We aimed to identify the alterations of serum glycopatterns in ACHBLF and probe the possibility of them as novel potential biomarkers for diagnosis of ACHBLF. As a result, there were 18 lectins (e.g., WFA, GSL-II, and PNA) to give significantly alterations of serum glycopatterns in ACHBLF compared with healthy controls (HC) (all p ≤ 0.0386). Meanwhile, among these lectins, there were 12 lectins (e.g., WFA, GAL-II, and EEL) also exhibited significantly alterations of serum glycopatterns in ACHBLF compared with HBV-infected chronic hepatitis (cHB) (all p ≤ 0.0252). The receiver-operating characteristic (ROC) curve analysis indicated there were 5 lectins (PHA-E + L, BS-I, ECA, ACA, and BPL) had the greatest discriminatory power for distinguishing ACHBLF and HC or cHB, respectively (all p ≤ 0.00136). We provided a new basic insight into serum glycopatterns in ACHBLF and investigated the correlation of alterations in serum glycopatterns as novel potential biomarkers for diagnosis of ACHBLF.
Highlights
Protein glycosylation is one of the most complex post-translational modifications (PTMs), because of the large number of enzymatic steps involved, with significant effects on protein folding, stability and activity[9,10]
Lectin signal patterns were classified into three categories to evaluate whether the glycopatterns of the sera glycoproteins were altered in Acute-on-chronic hepatitis B liver failure (ACHBLF): (1) results showing significant increases in normalized fluorescent intensities (NFIs), (2) results showing significant decreases in NFIs, and (3) results showing almost even level in NFIs
All based on fold change in pairs with the NFIs of each lectin from healthy controls (HC), cHB, and ACHBLF are showed in Supplementary Table S1
Summary
Protein glycosylation is one of the most complex post-translational modifications (PTMs), because of the large number of enzymatic steps involved, with significant effects on protein folding, stability and activity[9,10]. Lectins have long been used to characterize cell-surface glycans because of their substantial selectivity[14,15]. Several lectins, such as ConA, LCA, LTL, PHA-E and PHA-L, are generally used to study altered glycan structures in chronic liver diseases[16]. The aim of the current study was to investigate the correlation of alterations in serum glycosylation related to ACHBLF, and systematically compare different or similar alterations of serum glycopatterns between healthy controls (HC), HBV-infected chronic hepatitis (cHB), and ACHBLF, as well as assess the distribution and localization of specific glycosidic residues in HC and ACHBLF tissues by fluorescence-based lectin histochemistry, and probe the possibility of serum glycopatterns as novel potential biomarkers for diagnosis of ACHBLF
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