Decreased core-fucosylation contributes to malignancy in gastric cancer

Autor: Qing You, Meng Fang, Chang-Hong Yi, Xin-yun Xu, Xing Gu, Ping-Ting Zhou, Yun-Peng Zhao, Chunfang Gao, Jun Ji, Hao Wang, Cheng Cheng
Jazyk: angličtina
Rok vydání: 2014
Předmět:
Male
Pathology
Colorectal cancer
Glycobiology
Cancer Treatment
lcsh:Medicine
Biochemistry
Cell Movement
Molecular Cell Biology
Medicine and Health Sciences
lcsh:Science
Glycomics
Fucosylation
alpha-L-Fucosidase
Multidisciplinary
medicine.diagnostic_test
Middle Aged
Fucosyltransferases
Immunohistochemistry
Blood proteins
Blot
Cell Motility
Oncology
Cell Processes
Disease Progression
Female
Research Article
medicine.medical_specialty
Biophysics
Biology
Cell Growth
Western blot
Downregulation and upregulation
Polysaccharides
Stomach Neoplasms
Diagnostic Medicine
Cell Line
Tumor
Gastrointestinal Tumors
Biomarkers
Tumor
medicine
Humans
Stomach Ulcer
Cell Proliferation
Demography
Fucose
Glycoproteins
Wound Healing
lcsh:R
Biology and Life Sciences
Cancers and Neoplasms
Cell Biology
medicine.disease
Molecular biology
N-Acetylneuraminic Acid
Gastric Cancer
Case-Control Studies
Cancer cell
lcsh:Q
Zdroj: PLoS ONE, Vol 9, Iss 4, p e94536 (2014)
PLoS ONE
ISSN: 1932-6203
Popis: The object of the study is to identify N-glycan profiling changes associated with gastric cancer and explore the impact of core-fucosylation on biological behaviors of human gastric cancer cells. A total of 244 subjects including gastric cancer, gastric ulcer and healthy control were recruited. N-glycan profiling from serum and total proteins in gastric tissues was analyzed by DNA sequencer-assisted fluorophore-assisted capillary electrophoresis. The abundance of total core-fucosylated residues and the expression of enzymes involved in core-fucosylation were analyzed with lectin blot, quantitative reverse transcription-polymerase chain reaction, western blot, Immunohistochemical staining and lectin-histochemical staining. The recombinant plasmids of GDP-fucose transporter and α-1,6-fucosyltransferase (Fut8) were constructed and transfected into gastric cancer cell lines BGC-823 and SGC-7901. CCK-8 and wound healing assay were used to assess the functional impact of core-fucosylation modulation on cell proliferation and migration. Characteristic serum N-glycan profiles were found in gastric cancer. Compared with the healthy control, a trianntenary structure abundance, peak 9 (NA3Fb), was increased significantly in gastric cancer, while the total abundance of core-fucosylated residues (sumfuc) was decreased. Core-fucosylated structures, peak6(NA2F) and peak7(NA2FB) were deceased in gastric tumor tissues when compared with that in adjacent non-tumor tissues. Consistently, lens culinaris agglutinin (LCA)-binding proteins were decreased significantly in sera of gastric cancer, and protein level of Fut8 was decreased significantly in gastric tumor tissues compared with that in adjacent non-tumor tissues. Upregulation of GDP-Tr and Fut8 could inhibit proliferation, but had no significant influence on migration of BGC-823 and SGC-7901 cells. Core-fucosylation is down regulated in gastric cancer. Upregulation of core-fucosylation could inhibit proliferation of the human gastric cancer cells.
Databáze: OpenAIRE
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