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DC Field | Value | Language |
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dc.contributor.author | Udompatanakorn C. | |
dc.contributor.author | Yada N. | |
dc.contributor.author | Matsuo K. | |
dc.date.accessioned | 2021-04-05T03:01:18Z | - |
dc.date.available | 2021-04-05T03:01:18Z | - |
dc.date.issued | 2020 | |
dc.identifier.issn | 15412016 | |
dc.identifier.other | 2-s2.0-85090613971 | |
dc.identifier.uri | https://ir.swu.ac.th/jspui/handle/123456789/11856 | - |
dc.identifier.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85090613971&doi=10.1097%2fPAI.0000000000000802&partnerID=40&md5=b7e9a226e73f0fe9b80ceb437d939ccf | |
dc.description.abstract | Aquaporin 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.subject | anti aquaporin 3 antibody | |
dc.subject | aquaporin 3 | |
dc.subject | aquaporin antigen recognition | |
dc.subject | formaldehyde | |
dc.subject | glycerol | |
dc.subject | membrane protein | |
dc.subject | unclassified drug | |
dc.subject | AA1 80 | |
dc.subject | AA180 228 | |
dc.subject | AA250 c terminus | |
dc.subject | adult | |
dc.subject | aged | |
dc.subject | amino terminal sequence | |
dc.subject | antigen recognition | |
dc.subject | Article | |
dc.subject | cancer staging | |
dc.subject | carboxy terminal sequence | |
dc.subject | controlled study | |
dc.subject | dysplasia | |
dc.subject | female | |
dc.subject | gingiva | |
dc.subject | high grade epithelial dysplasia | |
dc.subject | human | |
dc.subject | human tissue | |
dc.subject | hydration | |
dc.subject | immunohistochemistry | |
dc.subject | lymph node metastasis | |
dc.subject | male | |
dc.subject | mouth cavity | |
dc.subject | mouth floor | |
dc.subject | mouth mucosa | |
dc.subject | mouth squamous cell carcinoma | |
dc.subject | paraffin embedding | |
dc.subject | priority journal | |
dc.subject | tongue | |
dc.title | Assessing the Expression of Aquaporin 3 Antigen-Recognition Sites in Oral Squamous Cell Carcinoma | |
dc.type | Article | |
dc.rights.holder | Scopus | |
dc.identifier.bibliograpycitation | Applied Immunohistochemistry and Molecular Morphology. Vol 28, No.8 (2020), p.611-620 | |
dc.identifier.doi | 10.1097/PAI.0000000000000802 | |
Appears in Collections: | Scopus 1983-2021 |
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