Title : Alteration of
asparagine-linked glycosylation in serum
transferrin of patients with hepatocellular carcinoma
Abstract :
- The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared
- Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination
- Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients
- Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin , hemopexin , alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. asparagine-linked, , -, The asparagine-linked sugar chains, asparagine
- 1. chains, , transferrin, chains, -
- 2. desialylated, , transferrin, -, -
- 2. released, , transferrin, Sugar chains, -
- 3. fucosylated, , -, a fucosylated trimannosyl core, -
- 4. fucosylated, , transferrin, -, -
- 4. glycoprotein, , alpha 1-antitrypsin, -, -
- 4. glycoprotein, , alpha 2-HS glycoprotein, -, -
- 4. glycoprotein, , glycoprotein, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):