Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/11856
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dc.contributor.authorUdompatanakorn C.
dc.contributor.authorYada N.
dc.contributor.authorMatsuo K.
dc.date.accessioned2021-04-05T03:01:18Z-
dc.date.available2021-04-05T03:01:18Z-
dc.date.issued2020
dc.identifier.issn15412016
dc.identifier.other2-s2.0-85090613971
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/11856-
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85090613971&doi=10.1097%2fPAI.0000000000000802&partnerID=40&md5=b7e9a226e73f0fe9b80ceb437d939ccf
dc.description.abstractAquaporin 3 (AQP3) serves as a water and glycerol transporter facilitating epithelial cell hydration. Recently, the involvement of AQP3 in cancers has been reported. However, the immunohistochemical expression of AQP3 in carcinomas remains controversial. We hypothesized that differences in aquaporin 3 antigen recognition (AQP3 AR) may influence their expressions. Thus, our study aimed to assess the immunostaining patterns of 3 AQP3 AR sites in oral squamous cell carcinoma (OSCC) and to compare the adjacent areas of high-grade epithelial dysplasia (HG-ED) and normal oral mucosa (NOM). The study group included formalin-fixed OSCC samples (n=51) with adjacent regions of HG-ED (n=12) and NOM (n=51). The tissues were stained with anti-AQP3 antibodies (AR sites at amino acid (AA) 250-C terminus, AA180-228, and N terminus AA1-80) by immunohistochemistry. Our results showed that strong membranous immunostaining was observed for AQP3 AR sites at the AA250-C terminus and AA180-228 in all the samples for NOM and weak AQP3 immunostaining for both the AR sites in all the 12 samples for HG-ED. The invasive front of OSCC samples showed that AQP3 AR at the AA250-C terminus decreased in 42/51 samples (82.4%) and AA180-228 in 47/51 samples (92.2%). Conversely, in the AQP3 AR site at N terminus AA1-80, all samples of the NOM showed negative or slightly positive staining in the cytoplasm of the lower layers. AQP3 expression was increased in 12/12 cases (100%) and 46/51 cases (90.2%) in the HG-ED and invasive front of OSCC, respectively. AQP3 may be used as a biomarker for detecting malignant transformations. AQP3 AR site differences influence their immunohistochemical expression in OSCC. © 2020 Lippincott Williams and Wilkins. All rights reserved.
dc.subjectanti aquaporin 3 antibody
dc.subjectaquaporin 3
dc.subjectaquaporin antigen recognition
dc.subjectformaldehyde
dc.subjectglycerol
dc.subjectmembrane protein
dc.subjectunclassified drug
dc.subjectAA1 80
dc.subjectAA180 228
dc.subjectAA250 c terminus
dc.subjectadult
dc.subjectaged
dc.subjectamino terminal sequence
dc.subjectantigen recognition
dc.subjectArticle
dc.subjectcancer staging
dc.subjectcarboxy terminal sequence
dc.subjectcontrolled study
dc.subjectdysplasia
dc.subjectfemale
dc.subjectgingiva
dc.subjecthigh grade epithelial dysplasia
dc.subjecthuman
dc.subjecthuman tissue
dc.subjecthydration
dc.subjectimmunohistochemistry
dc.subjectlymph node metastasis
dc.subjectmale
dc.subjectmouth cavity
dc.subjectmouth floor
dc.subjectmouth mucosa
dc.subjectmouth squamous cell carcinoma
dc.subjectparaffin embedding
dc.subjectpriority journal
dc.subjecttongue
dc.titleAssessing the Expression of Aquaporin 3 Antigen-Recognition Sites in Oral Squamous Cell Carcinoma
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationApplied Immunohistochemistry and Molecular Morphology. Vol 28, No.8 (2020), p.611-620
dc.identifier.doi10.1097/PAI.0000000000000802
Appears in Collections:Scopus 1983-2021

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