Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin

Abstract

Abstract:In cervical cancer, glycosylation has been suggested as being involved in both its carcinogenesis and invasive capacity. In this work, we analyzed mucin type O-glycosylation in biopsies of invasive cervical cancer in FIGO stage II B through histochemistry using lectins specific for O-glycosidically linked glycans. Our results reveal that the lectin Machaerocereus eruca (MeA, specific for Gal in a Fuca1,2 (GalNAca1,3) Galb1,4) showed increased recognition of tumoral cells and tumoral stroma tissue compared to other lectins with similar specificity; healthy cervical tissue was negative for MeA. Trypsin treatment of recognized tissues abolished MeA's recognition; moreover, interaction of MeA was inhibited with oligosaccharides from mucin. As demonstrated by Western blot of 2-D electrophoresis, MeA recognized ten glycoproteins in the range from 122 to 42 kDa in cervical cancer lysates. The LC-ESI-MS/MS analysis of the MeAs' recognized peptides revealed that the latter matched mainly with the amino acid sequences of lamin A/C, vimentin, elongation factor 2, keratin 1, and beta actin. Our results suggest that MeA recognizes a complex of over-expressed O-glycosidically-linked proteins that play a relevant role in cervical cancer's invasive capacity. O-glycosylation participates in the disassembly of intercellular junctions favoring cancer progression.

Prediction of the immunological and prognostic value of five signatures related to fatty acid metabolism in patients with cervical cancer

“…regulating immune response and controlling cell metabolism (42,43). In addition, in the G2 phase, de novo synthesis is enhanced to synthesize lipids, which ensures the membrane material needed for mitosis and promotes cell proliferation (44).…”

“…As a glycoprotein on the cell surface, N-Glycon directly affects cell signal transduction and is the diagnostic target of malignant transformation in the early stage of CC ( 39 – 41 ). O-glycan can be used as a biological marker of proliferation, senescence and metastasis of CC cells by regulating immune response and controlling cell metabolism ( 42 , 43 ). In addition, in the G2 phase, de novo synthesis is enhanced to synthesize lipids, which ensures the membrane material needed for mitosis and promotes cell proliferation ( 44 ).…”

Mucin Glycans: A Target for Cancer Therapy

“…HPV can lead to the occurrence of cervical cancer (CESC). Solórzano et al conducted O-glycan analysis of mucins in CESC infected with HPV, and the results showed that HPV infection can cause abnormal fucosylation of mucins, which can affect the invasion of CESC cells [137]. Ahmad et al found that during HCV/HBV infection, the binding of O-glycans at the Ser204 site of insulin-like growth factor to cellular growth factor is reduced, which can lead to the occurrence of HCC [138].…”

A comparative glycoproteome study of developing endosperm in the hexose-deficient miniature1 (mn1) seed mutant and its wild type Mn1 in maize

“…Although some proteins that showed at least one predicted N -glycosylation site, they may have been reported with other types of glycosylation. For example, the proteasome alpha subunit (spot 433) has been reported to be O-glycosylated in mouse (Overath et al, 2012); elongation factor 2 (spot 480) is an O-glycosylated protein in human cervical cancer cells (Solórzano et al, 2012), triosaphosphate isomerase (Spots 626 and 649) (Love and Hanover, 2005); and protein Z showed O-glycosylation in human plasma (Spiro, 2002). O-glycosylation occurs in a great variety of proteins that are involved in key nuclear and cytoplasmic activities.…”