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Změna glykosylace na sérových glykoproteinech u pacientek s rakovinou vaječníku pravděpodobně přispívá k patogenezi nemoci
[Glycosylation changes of serum glycoproteins in ovarian cancer may contribute to disease pathogenesis]
R. Šaldová, P. M. Dudd, J. Káš
Jazyk čeština Země Česko
- MeSH
- alfa-1-antichymotrypsin krev metabolismus MeSH
- alfa-makroglobuliny metabolismus MeSH
- galaktosa nedostatek MeSH
- glykosylace MeSH
- haptoglobiny metabolismus MeSH
- imunoglobulin G krev metabolismus MeSH
- kyseliny sialové nedostatek MeSH
- lidé MeSH
- metabolismus sacharidů MeSH
- nádorové biomarkery krev MeSH
- nádory vaječníků imunologie metabolismus MeSH
- proteiny akutní fáze metabolismus MeSH
- Check Tag
- lidé MeSH
- ženské pohlaví MeSH
Ovarian cancer is the most lethal of all gynecological cancers. Although serum biomarker CA125 is routinely used, there is a need for sensitive and specific complementary biomarkers. N-glycosylation changes in ovarian cancer serum glycoproteins include a decrease in galactosylation of IgG and an increase in sialyl Lewis X (SLex) on haptoglobin ß-chain, ?1-acid glycoprotein and ?1- antichymotrypsin. These changes are also present in chronic inflammations but not in malignant melanoma with low levels of inflammation. Acute phase proteins carrying increased amounts of SLex have an increased half-life. Sialylation of acute phase proteins decreases apoptosis favouring survival of cancer cells. Cancer cells produce inflammatory cytokines which influence glycosylation in liver parenchymal cells. The decreased galactosylation and sialylation of IgG increases cytotoxicity of natural killer cells and complement activation via mannosebinding lectin. Altered glycosylation of acute phase proteins and IgG suggests that cancer regulates certain pathways favouring survival of cancer cells.
Glycosylation changes of serum glycoproteins in ovarian cancer may contribute to disease pathogenesis
Lit.: 107
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- $a Lit.: 107
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- $a Ovarian cancer is the most lethal of all gynecological cancers. Although serum biomarker CA125 is routinely used, there is a need for sensitive and specific complementary biomarkers. N-glycosylation changes in ovarian cancer serum glycoproteins include a decrease in galactosylation of IgG and an increase in sialyl Lewis X (SLex) on haptoglobin ß-chain, ?1-acid glycoprotein and ?1- antichymotrypsin. These changes are also present in chronic inflammations but not in malignant melanoma with low levels of inflammation. Acute phase proteins carrying increased amounts of SLex have an increased half-life. Sialylation of acute phase proteins decreases apoptosis favouring survival of cancer cells. Cancer cells produce inflammatory cytokines which influence glycosylation in liver parenchymal cells. The decreased galactosylation and sialylation of IgG increases cytotoxicity of natural killer cells and complement activation via mannosebinding lectin. Altered glycosylation of acute phase proteins and IgG suggests that cancer regulates certain pathways favouring survival of cancer cells.
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