O-GlcNAcylation in oral squamous cell carcinoma
© 2018 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd Background: Two post-translational mechanisms commonly demonstrated in various cancers are protein phosphorylation and glycosylation by O-linked β-N-acetylglucosamine (O-GlcNAc). However, only phosphorylation of the epiderm...
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th-cmuir.6653943832-582882018-09-05T04:35:52Z O-GlcNAcylation in oral squamous cell carcinoma Tassaporn Kongkaew Win Pa Pa Aung Chayarop Supanchart Anupong Makeudom Sarawat Langsa-ard Thanapat Sastraruji Ponlatham Chaiyarit Suttichai Krisanaprakornkit Biochemistry, Genetics and Molecular Biology Dentistry Medicine © 2018 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd Background: Two post-translational mechanisms commonly demonstrated in various cancers are protein phosphorylation and glycosylation by O-linked β-N-acetylglucosamine (O-GlcNAc). However, only phosphorylation of the epidermal growth factor receptor (EGFR)/Akt pathway has been reported in oral squamous cell carcinoma (OSCC). Therefore, we aimed to determine both post-translational modifications in OSCC tissues and in oral cancer cells compared to normal tissues and oral keratinocytes and to find correlations of these modifications with histological grading. Methods: Thirty-two OSCC and ten normal formalin-fixed and paraffin-embedded sections were probed with the anti-O-GlcNAc, anti-O-GlcNAc transferase (OGT), anti-phosphorylated-EGFRtyr1173, and anti-phosphorylated-Aktser473antibodies following standard immunohistochemistry. The immunohistochemical (IHC) score was determined using the Fromowitz standard. Whole cell lysates of oral cancer cells and normal oral keratinocytes were immunoblotted with the anti-O-GlcNAc antibody. Results: The median IHC scores of O-GlcNAc or OGT between OSCC and normal tissues were not different, whereas those of phosphorylated-EGFRtyr1173and phosphorylated-Aktser473were significantly higher in OSCC than normal tissues (P <.001 and P <.01, respectively). Similarly, expression of O-GlcNAcylated proteins in oral cancer cells and normal oral keratinocytes did not differ. In the OSCC group, the median IHC scores of O-GlcNAc and OGT were significantly lower than those of phosphorylated-EGFRtyr1173and phosphorylated-Aktser473(P <.01 and P <.001, respectively). The IHC scores of O-GlcNAc or OGT were not determined to correlate with histological grading. Conclusion: Unlike other types of cancers, our findings demonstrate that the levels of O-GlcNAcylation are not significantly increased in OSCC tissues or in oral cancer cells and are not associated with the histological grading of OSCC. 2018-09-05T04:22:11Z 2018-09-05T04:22:11Z 2018-03-01 Journal 16000714 09042512 2-s2.0-85041137618 10.1111/jop.12680 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85041137618&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/58288 |
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Biochemistry, Genetics and Molecular Biology Dentistry Medicine Tassaporn Kongkaew Win Pa Pa Aung Chayarop Supanchart Anupong Makeudom Sarawat Langsa-ard Thanapat Sastraruji Ponlatham Chaiyarit Suttichai Krisanaprakornkit O-GlcNAcylation in oral squamous cell carcinoma |
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© 2018 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd Background: Two post-translational mechanisms commonly demonstrated in various cancers are protein phosphorylation and glycosylation by O-linked β-N-acetylglucosamine (O-GlcNAc). However, only phosphorylation of the epidermal growth factor receptor (EGFR)/Akt pathway has been reported in oral squamous cell carcinoma (OSCC). Therefore, we aimed to determine both post-translational modifications in OSCC tissues and in oral cancer cells compared to normal tissues and oral keratinocytes and to find correlations of these modifications with histological grading. Methods: Thirty-two OSCC and ten normal formalin-fixed and paraffin-embedded sections were probed with the anti-O-GlcNAc, anti-O-GlcNAc transferase (OGT), anti-phosphorylated-EGFRtyr1173, and anti-phosphorylated-Aktser473antibodies following standard immunohistochemistry. The immunohistochemical (IHC) score was determined using the Fromowitz standard. Whole cell lysates of oral cancer cells and normal oral keratinocytes were immunoblotted with the anti-O-GlcNAc antibody. Results: The median IHC scores of O-GlcNAc or OGT between OSCC and normal tissues were not different, whereas those of phosphorylated-EGFRtyr1173and phosphorylated-Aktser473were significantly higher in OSCC than normal tissues (P <.001 and P <.01, respectively). Similarly, expression of O-GlcNAcylated proteins in oral cancer cells and normal oral keratinocytes did not differ. In the OSCC group, the median IHC scores of O-GlcNAc and OGT were significantly lower than those of phosphorylated-EGFRtyr1173and phosphorylated-Aktser473(P <.01 and P <.001, respectively). The IHC scores of O-GlcNAc or OGT were not determined to correlate with histological grading. Conclusion: Unlike other types of cancers, our findings demonstrate that the levels of O-GlcNAcylation are not significantly increased in OSCC tissues or in oral cancer cells and are not associated with the histological grading of OSCC. |
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Journal |
author |
Tassaporn Kongkaew Win Pa Pa Aung Chayarop Supanchart Anupong Makeudom Sarawat Langsa-ard Thanapat Sastraruji Ponlatham Chaiyarit Suttichai Krisanaprakornkit |
author_facet |
Tassaporn Kongkaew Win Pa Pa Aung Chayarop Supanchart Anupong Makeudom Sarawat Langsa-ard Thanapat Sastraruji Ponlatham Chaiyarit Suttichai Krisanaprakornkit |
author_sort |
Tassaporn Kongkaew |
title |
O-GlcNAcylation in oral squamous cell carcinoma |
title_short |
O-GlcNAcylation in oral squamous cell carcinoma |
title_full |
O-GlcNAcylation in oral squamous cell carcinoma |
title_fullStr |
O-GlcNAcylation in oral squamous cell carcinoma |
title_full_unstemmed |
O-GlcNAcylation in oral squamous cell carcinoma |
title_sort |
o-glcnacylation in oral squamous cell carcinoma |
publishDate |
2018 |
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https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85041137618&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/58288 |
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