Sialylation of intracellular proteins of thyroid lesions

Krześlak, Anna; Gaj, Zuzanna; Pomorski, Lech; Lipińska, Anna

doi:10.3892/or.17.5.1237

Cited by 11 publications

(13 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has been suggested that hyperproliferation of thyroid cancer cells might be related to an overall increasei nO -GlcNAcl evels. [41] Consistent with this hypothesis, we observed qualitatively highers tainingi nt he cancerous tissue (papillary carcinoma) compared to the normal thyroid tissue ( Figure 4A), which was confirmed by the quantification of mean fluorescence intensity (MFI) of the full tissue specimens and coverage area percentageo fO -GlcNAcs ignal ( Figure S9). Interestingly,i n the healthy tissue, O-GlcNAc staining wasl ocated primarilyi n the nucleus, whereas adiffuse cytoplasmic signal was observed for cancerous specimens.…”

Section: Resultssupporting

confidence: 80%

A Chemoenzymatic Histology Method for O‐GlcNAc Detection

et al. 2017

View full text Add to dashboard Cite

Modification of nuclear and cytoplasmic proteins by the addition or removal of O-GlcNAc dynamically impacts multiple biological processes. Here, we present the development of a chemoenzymatic histology method for the detection of O-GlcNAc in tissue specimens. We applied this method to screen murine organs, uncovering specific O-GlcNAc distribution patterns in different tissue structures. We then utilized our histology method for O-GlcNAc detection in human brain specimens from healthy donors and donors with Alzheimer’s disease and found higher levels of O-GlcNAc in specimens from healthy donors. We also performed an analysis using a multiple cancer tissue array, uncovering different O-GlcNAc levels between healthy and cancerous tissues, as well as different O-GlcNAc cellular distributions within certain tissue specimens. This chemoenzymatic histology method therefore holds great potential for revealing the biology of O-GlcNAc in physiopathological processes.

show abstract

Section: Resultssupporting

confidence: 80%

A Chemoenzymatic Histology Method for O‐GlcNAc Detection

et al. 2017

View full text Add to dashboard Cite

show abstract

“…There is evidence that the intracellular glycosylation changes occurring during carcinogenesis are independent of those that occur on the cell surface or in the blood. Krzeslak et al (32) observed that the sialylation levels of intracellular proteins in thyroid lesions, particularly follicular and papillary carcinomas, were significantly lower than those in non-neoplastic lesions. However, there have been no subsequent confirmatory studies.…”

Section: Discussionmentioning

confidence: 99%

Aberrant sialylation and fucosylation of intracellular proteins in cervical tissue are critical markers of cervical carcinogenesis

Kim

et al. 2013

Oncology Reports

View full text Add to dashboard Cite

Numerous studies have suggested that increased sialylation and fucosylation levels are signs of cancer progression. The majority of studies have focused on cell surface and bloodstream glycosylation changes associated with cancer progression, while little attention has been paid to changes in the glycosylation of cytosolic proteins. We compared the mannosylation, sialylation and fucosylation levels of cytosolic proteins obtained from human cervical tissues without neoplastic lesions vs. with cancer, using lectin blot and enzyme-linked lectin assay (ELLA) systems. There were no quantitative differences in mannosylation levels between the cytosolic proteins of normal and cancer tissues. However, we found markedly reduced sialylation (P<0.001) and fucosylation (P<0.01) in the proteins of cancer tissues. The ELLA system for detecting sialylation had extremely high sensitivity (91-100%) and specificity (82-100%) in distinguishing normal and cancer tissues. Thus, the changes in the glycosylation of cytosolic proteins during carcinogenesis of the cervix are quite different from previous observations concerning glycoconjugates in the bloodstream or on the cell surface. We suggest that changes in the glycosylation of intracellular proteins may be useful markers of the development of cervical cancer.

show abstract

“…MiR-218 inhibited the invasion and migration of colon cancer cells by targeting the PI3K/Akt/mTOR signaling pathway [51]. High glucose promoted tumor invasion and increased metastasisassociated protein expression in human lung epithelial cells by upregulating heme oxygenase-1 via reactive oxygen species or the TGF-ß1/PI3K/Akt signaling pathway [52]. Upregulation of O-GlcNAcylation promoted proliferation in thyroid anaplastic cancer cells via increasing Akt1 activity [53].…”

Section: Figmentioning

confidence: 99%

Potential role of O‐GlcNAcylation and involvement of PI3K/Akt1 pathway in the expression of oncogenic phenotypes of gastric cancer cells in vitro

Zhang

Chen

2015

Biotech and App Biochem

View full text Add to dashboard Cite

O-GlcNAcylation is a monosaccharide modification by a residue of N-acetylglucosamine (GlcNAc) attached to serine or threonine moieties on nuclear and cytoplasmic proteins. O-GlcNAcylation is dynamically regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). Increasing evidence suggests that O-GlcNAcylation is involved in a variety of human cancers. However, the exact role of O-GlcNAcylation in tumor progression remains unclear. Here, we show that O-GlcNAcylation accelerates oncogenic phenotypes of gastric cancer. First, cell models with increased or decreased O-GlcNAcylation were constructed by OGT overexpression, downregulation of OGA activity with specific inhibitor Thiamet-G, or silence of OGT. MTT assays indicated that O-GlcNAcylation increased proliferation of gastric cancer cells. Soft agar assay and Transwell assays showed that O-GlcNAcylation significantly enhanced cellular colony formation, migration, and invasion in vitro. Akt1 activity was stimulated by upregulation of phosphorylation at Ser473 mediated by elevated O-GlcNAcylation. The enhanced cell invasion by Thiamet-G treatment was suppressed by PI3K inhibitor LY294002. Although the cell invasion induced by Thiamet-G was reduced by Akt1 shRNA, it was still higher in comparison with that to the control (cells with Akt1 shRNA alone). And Akt1 overexpression promoted Thiamet-G-induced cell invasion. These results suggested that O-GlcNAcylation enhanced oncogenic phenotypes possibly partially involving PI3K/Akt signaling pathway.

show abstract

Sialylation of intracellular proteins of thyroid lesions

Cited by 11 publications

References 23 publications

A Chemoenzymatic Histology Method for O‐GlcNAc Detection

A Chemoenzymatic Histology Method for O‐GlcNAc Detection

Aberrant sialylation and fucosylation of intracellular proteins in cervical tissue are critical markers of cervical carcinogenesis

Potential role of O‐GlcNAcylation and involvement of PI3K/Akt1 pathway in the expression of oncogenic phenotypes of gastric cancer cells in vitro

Contact Info

Product

Resources

About