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Isolation and identification of mannose‐binding proteins and estimation of their abundance in sera from hepatocellular carcinoma patients
Author(s) -
Yang Ganglong,
Chu Wei,
Zhang Hua,
Sun Xiuxuan,
Cai Tanxi,
Dang Liuyi,
Wang Qinzhe,
Yu Hanjie,
Zhong Yaogang,
Chen Zhuo,
Yang Fuquan,
Li Zheng
Publication year - 2013
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201200018
Subject(s) - hepatocellular carcinoma , glycan , mannose , computational biology , biology , blot , glycoprotein , microbiology and biotechnology , chemistry , cancer research , biochemistry , gene
The interaction of glycan‐binding proteins ( GBP s) and glycans plays a significant biological role that ranges from cell–cell recognition to cell trafficking, and glycoprotein targeting. The anomalies of GBP s related to the types and/or quantities were not clearly known in cancer incidence. It is imperative to identify and annotate the GBP s related with the canceration. Here the mannose‐binding proteins ( MBP s) from the clinical sera were isolated and identified by the mannose‐magnetic particle conjugates and the high‐accuracy MS analysis. Seventy‐five MBP s from normal donors’ sera and 79 MBP s from hepatocellular carcinoma patients’ sera were identified and annotated. By using the stringent criteria of exponentially modified protein abundance index (em PAI ) quantification, 12 MBP s were estimated to be significantly upregulated (emPAI ratio > 4) and nine MBP s were estimated to be significantly downregulated (emPAI ratio < 0.25) in the hepatocellular carcinoma sera. Real‐time quantitative PCR , W estern blotting, and protein microarrays were also used to confirm the altered MBP s expression level and the specific binding between the isolated MBP s and mannose. The sequence recognition motifs and structure preference of the isolated MBP s were characterized. The functional enrichment analysis revealed that over 57% of the isolated MBP s were binding protein and the upregulated MBP s were involved in cell death, tumor progression, and macromolecular complex remodeling.