<i>O</i>‐GlcNAcylation in oral squamous cell carcinoma

Kongkaew, Tassaporn; Aung, Win Pa Pa; Supanchart, Chayarop; Makeudom, Anupong; Langsa-ard, Sarawat; Sastraruji, Thanapat; Chaiyarit, Ponlatham; Krisanaprakornkit, Suttichai

doi:10.1111/jop.12680

Cited by 6 publications

(7 citation statements)

References 27 publications

(78 reference statements)

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“…17,20,21,24,26,43 However, from our recent study of O-GlcNAcylation in oral cancer, the O-GlcNAc levels have not been found to be signi cantly enhanced upon increased histopathologic severities of oral squamous cell carcinoma, nor have the OGT or the OGA expressions. 44 Consistent with these ndings, the O-GlcNAc levels, the OGT or the OGA expressions were not found to be different between the two distinct clinical severities of osteosarcoma. Therefore, involvement of O-GlcNAcylation along with OGT and OGA expressions in the pathogenesis of osteosarcoma still requires further investigations.…”

Section: Discussionsupporting

confidence: 73%

Relationship Between O-GlcNAcase Expression and Prognosis of Patients With Osteosarcoma

Sombutthaweesri

Chamusri

et al. 2021

Applied Immunohistochemistry &Amp; Molecular Morphology

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Background: Several studies have demonstrated a role of O-GlcNAcylation (O-GlcNAc) in tumorigenesis of various carcinomas by modi cation of tumor-associated proteins. However, its implication in the pathogenesis of osteosarcoma remains unclear. This study aimed to investigate the levels of O-GlcNAc and the expressions of O-linked N-acetylglucosamine transferase (OGT) and O-GlcNAcase (OGA) in human osteosarcoma tissues and to nd correlations between the levels or expressions and several clinicopathologic parameters.Methods: Immunohistochemistry was conducted in 109 formalin-xed, para n-embedded bone tissue sections that were derived from 109 rst diagnosed osteosarcoma patients, including Enneking stage IIB (n=70) and III (n=39). Correlations between the imunoreactive score (IRS) and clinicopathologic parameters, overall survival, and metastasis-free survival were evaluated.Results: A positive correlation was found between the IRS of OGA and the percentage of postchemotherapeutic tumor necrosis (r=0.308; P=0.017). Univariate analysis revealed signi cantly lower OGA IRS in metastatic patients (P=0.020) and poor chemotherapeutic-responder patients (P=0.001). By multivariate analysis, presence of tumor metastasis (P=0.002) and lower OGA IRS (P=0.004) was signi cantly associated with shorter overall survival. Subgroup analysis in stage IIB osteosarcoma (n=70) demonstrated that male gender (P=0.019), presence of tumor recurrence (P=0.026), poor chemotherapeutic responder (P=0.022), and lower OGA IRS (P=0.019) were signi cantly correlated with short metastasis-free survival. But, lower OGA IRS was the only independent predictor for short metastasis-free survival (P=0.006).Conclusions: O-GlcNAc pathway, especially OGA, involved in pathogenesis and aggressiveness of osteosarcoma. Low level of OGA expression may be used as a poor prognostic indicator. BackgroundO-GlcNAcylation (O-GlcNAc) is a post-translational modi cation of proteins associated with regulation of various protein functions by an addition of N-acetylglucosamine (GlcNAc) to the hydroxyl group of serine or threonine residues of the target proteins. This modi cation is a dynamic and reversible process, strictly regulated by two important enzymes, O-linked N-acetylglucosamine transferase (OGT) and O-GlcNAcase (OGA), which add and remove the GlcNAc moieties, respectively. 1-5 O-GlcNAc is involved in many cellular processes, such as signal transduction, transcription, cell cycle control, and epigenetic control of gene expressions in response to stress and nutrient imbalance. 6,7 In this regard, O-GlcNAc homeostasis needs to be maintained in order to achieve proper cellular functions.Aberrations of O-GlcNAc are associated with the pathogenesis of many human diseases, including diabetes, neurodegenerative diseases and cancers. 6,[8][9][10][11] With respect to cancer pathogenesis and progression, several key players, such as p53, c-Myc, Forkhead box M1 (FoxM1) etc., have been shown to

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Section: Discussionsupporting

confidence: 73%

Relationship Between O-GlcNAcase Expression and Prognosis of Patients With Osteosarcoma

Sombutthaweesri

Chamusri

et al. 2021

Applied Immunohistochemistry &Amp; Molecular Morphology

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“…The clinical and histopathologic features of these specimens have previously been reported [24]. As controls, 10 specimens of oral tissues were collected from 10 orally and systemically healthy and non‐smoking participants, during surgical removal of third molars with bony impaction at the Oral and Maxillofacial Surgery Clinic, Faculty of Dentistry, Chiang Mai University [25]. The approval certificates (#54/2014 and #21/2017) for the use of the OSCC and oral tissues specimens in this study were granted by the Human Experimentation Committee, Chiang Mai University.…”

Section: Methodsmentioning

confidence: 99%

“…For quantitative analysis, three representative fields at ×400 magnification were captured from each section using a CCD camera (Axiocam ICc5; Carl Zeiss) attached to a microscope (Axio Imager.Z2 m; Carl Zeiss). The immunohistochemical (IHC) scores (range: 0–7) were determined using ImageJ program version 1.48 (National Institutes of Health) by combining the percentage of positively stained cells (ie, those with scores of 0–4) and the staining intensity (of those with scores of 0–3), as previously described [25]. The positive controls were OSCC sections previously shown to have immunostaining reactivity against p‐EGFR tyr1173 , p‐AKT ser473 , and ADAM 9 antibodies [24,25], while the negative controls were OSCC sections incubated in normal blocking serum without addition of these antibodies.…”

Section: Methodsmentioning

confidence: 99%

Involvement of the A disintegrin and metalloproteinase 9 in oral cancer cell invasion

Buranaphatthana

Makeudom

et al. 2021

European J Oral Sciences

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The aims of this study were to determine the functional roles of the transmembrane glycoprotein, Disintegrin and metalloproteinase domain-containing protein 9 (ADAM 9), in the phosphorylation of epidermal growth factor receptor (EGFR) and AKT and in the aggressiveness of oral cancer cells. Immunohistochemistry and immunoblotting were conducted to determine expression of ADAM 9 and the levels of EGFR phosphorylated at the tyrosine 1173 residue (p-EGFR tyr1173 ) and AKT phosphorylated at the serine 473 residue (p-AKT ser473 ) in oral cancer tissues and in the oral cancer cell lines HN5, HN6, HN15, and HN008. Small interfering RNA (siRNA) was used to inhibit expression of ADAM9 mRNA, and thus production of ADAM9 protein, in oral cancer cells. ADAM9-knockdown cells were examined for p-EGFR tyr1173 and p-AKT ser473 levels and used for cell proliferation and invasion assays. A positive correlation among overexpression of ADAM 9, p-EGFR tyr1173 , and p-AKT ser473 was found in oral cancer tissues.

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“…In addition, HIF-1α inhibitors can suppress the autophagy of OSCC by decreasing the expression of O-GlcNAc and O-GlcNAc transferase (OGT) and increasing the expression of O-GlcNAcase (OGA) 120 . However, in another study, the levels of O-GlcNAcylation did not increase significantly in OSCC tissues, which was also not connected with the histological grading of OSCC 121 .…”

Section: O-glcnac Mediates Hnscc Autophagymentioning

confidence: 77%

Changes in Protein Glycosylation in Head and Neck Squamous Cell Carcinoma

Liao¹,

An²,

Tan³

et al. 2021

J. Cancer

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O‐GlcNAcylation in oral squamous cell carcinoma

Abstract: 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.

Cited by 6 publications

References 27 publications

Relationship Between O-GlcNAcase Expression and Prognosis of Patients With Osteosarcoma

Relationship Between O-GlcNAcase Expression and Prognosis of Patients With Osteosarcoma

Involvement of the A disintegrin and metalloproteinase 9 in oral cancer cell invasion

Changes in Protein Glycosylation in Head and Neck Squamous Cell Carcinoma

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