Serum Sna And Pha-e Affinity Glycoproteomics Of Human Non-metastatic And Metastatic Hepatocellular Carcinoma

Part oneEstablishment of Serum SNA Affinity Glyeoprotein Database from human non-metastatic and metastatic Hepatocellular carcinoma and Its BioinformaticsObjective:The establishment of serum SNA affinity glycosylated protein profile in human non-metastatic and metastatic Hepatocellular carcinoma by using sugar proteomics techniques.Methods:According to2002UICC TNM staging system whether with vascular invasion, distant metastasis and local infiltration, we divided27hepatocellular carcinoma patients into non-metastatic HCC group and24patients into metastatic HCC group. Every9hepatocellular carcinoma patients’s sera are pooled in non-metastatic HCC group. Every8hepatocellular carcinoma patients’s sera are pooled in metastatic HCC group. Using lectin affinity chromatography, the total protein were separated and condensed into two fractions; One was enriched SNA affinity glycoprotein. Comparison of glycan profiling of serum glycoprotein between non-metastatic and metastatic hepatocellular carcinoma by liquid chromatography-tandem Mass spectrometry (LC-MS/MS). Establishment of serum SNA affinity glyeoprotein gatabase from human non-metastatic and metastatic hepatocellular carcinoma and exploring a set of HCC metastasis associated glycoproteins.Results:In all,87glyeoproteins from non-metastatic HCC group and100glyeoproteins from metastatic HCC group were successfully identified, in which22metastasis-associated glyeoproteins. Providing the three principal ategories from GOfact, namely, molecular function, biological process and cellular component. In non-metastatic HCC group,65.7%and74.3%of the identified glycoproteins participate in metabolism and response to stimulus, separately. Most of the identified glycoproteins are located in extracellular region.85.7%and22.2%of the identified glycoproteins have binding activity and catalytic activity, respectively. In metastatic HCC group,66.3%and75%of the identified glycoproteins participate in metabolism and response to stimulus, separately. Most of the identified glycoproteins are located in extracellular region.87.7%and20.5%of the identified glycoproteins have binding activity and catalytic activity, respectively.Conclusion:Lectin affinity chromatography combined with mass spectrometry identification was a high-throughput detection method. Establishment of serum SNA affinity glyeoprotein gatabase from human non-metastatic and metastatic hepatocellular carcinoma was builded the foundation for further research.Part twoEstablishment of Serum PHA-E Affinity Glyeoprotein Database from human non-metastatic and metastatic Hepatocellular carcinoma and Its BioinformaticsObjective:The establishment of serum PHA-E affinity glycosylated protein profile in human non-metastatic and metastatic Hepatocellular carcinoma by using sugar proteomics techniques.Methods:According to2002UICC TNM staging system whether with vascular invasion, distant metastasis and local infiltration, we divided27hepatocellular carcinoma patients into non-metastatic HCC group and24patients into metastatic HCC group. Every9hepatocellular carcinoma patients’s sera are pooled in non-metastatic HCC group. Every8hepatocellular carcinoma patients’s sera are pooled in metastatic HCC group. Using lectin affinity chromatography, the total protein were separated and condensed into two fractions; One was enriched PHA-E affinity glycoprotein. Comparison of glycan profiling of serum glycoprotein between non-metastatic and metastatic hepatocellular carcinoma by liquid chromatography-tandem Mass spectrometry (LC-MS/MS). Establishment of serum PHA-E affinity glyeoprotein gatabase from human non-metastatic and metastatic hepatocellular carcinoma and exploring a set of HCC metastasis associated glycoproteins.Results:In all,62glyeoproteins from non-metastatic HCC group and57glyeoproteins from metastatic HCC group were successfully identified, in which24metastasis-associated glyeoproteins. Providing the three principal ategories from GOfact, namely, molecular function, biological process and cellular component. In non-metastatic HCC group,72.9%and83.3%of the identified glycoproteins participate in metabolism and response to stimulus, separately. Most of the identified glycoproteins are located in extracellular region.88.6%of the identified glycoproteins have binding activity. In metastatic HCC group,67.4%and84.8%of the identified glycoproteins participate in metabolism and response to stimulus, separately. Most of the identified glycoproteins are located in extracellular region.87.8%of the identified glycoproteins have binding activity. Conclusion:Lectin affinity chromatography combined with mass spectrometry identification was a high-throughput detection method. Establishment of serum PHA-E affinity glyeoprotein gatabase from human non-metastatic and metastatic hepatocellular carcinoma was builded the foundation for further research.Novelty1. Our study is the first time to establish the serum SNA and PHA-E affinity glyeoprotein database from human non-metastatic and metastatic hepatocellular carcinoma.2. Lectin affinity chromatography by SNA combined with LC-MS/MS,22metastasis-associated glyeoproteins were successfully identified.3. Lectin affinity chromatography by PHA-E combined with LC-MS/MS,24metastasis-associated glyeoproteins were successfully identified.Potential ApplicationThe study established the serum SNA and PHA-E affinity glyeoprotein database from human non-metastatic and metastatic hepatocellular carcinoma and screened a set of HCC metastasis associated glycoproteins which may serve as new prognostic candidates or potential therapeutic targets for HCC metastasis. The potential value of these specific glycan aberrations as HCC metastasis biomarkers is worth further studying.