Expression of aquaporin 3 (AQP3) in normal and neoplastic lung tissues

Liu, Yalan; Matsuzaki, Toshiyuki; Nakazawa, Tadao; Murata, Shin‐ichi; Nakamura, Nobuki; Kondo, Tetsuo; Iwashina, Masanori; Mochizuki, Kazuki; Yamane, Tetsu; Takata, Kuniaki; Katoh, Ryohei

doi:10.1016/j.humpath.2006.07.015

Cited by 87 publications

(73 citation statements)

References 27 publications

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“…Since overexpression of AQP3 could enhance the migration ability of various tumor cells, it also played a role in the clinical progression of tumors. A retrospective analysis of 149 cases of lung cancer specimens showed the level of AQP3 was correlated with the pathological type, differentiation grade and clinical staging (24). Shen et al (25) found that the expression of AQP3 was higher in undifferentiated gastric carcinoma than in well-differentiated tumors, and was associated with lymph node metastasis and lymphatic vessel invasion.…”

Section: Discussionmentioning

confidence: 99%

Critical role of aquaporin-3 in epidermal growth factor-induced migration of colorectal carcinoma cells and its clinical significance

Zhang

et al. 2012

Oncology Reports

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Abstract. Aquaporins (AQPs) are a family of small, integral membrane proteins that have been shown to play an important role in tumor development and metastasis. Several studies have demonstrated that expression of AQP3 contributes to the enhanced migration of epithelial cells and is related to differentiation, metastasis and vascular invasion in lung and gastric cancer. Therefore, we investigated whether AQP3 could enhance human colorectal carcinoma cell migration and we examined the role of AQP3 in the prognosis of colorectal carcinoma. Our results showed that human epidermal growth factor (hEGF) increased the expression of AQP3 and, subsequently, the migration ability of human colorectal carcinoma cells HCT116 in a dose-and time-dependent manner. The enhanced migration ability of HCT116 cells was blocked by the AQP3 inhibitor, CuSO 4 . Overexpression of AQP3 induced by hEGF was inhibited by a PI3K/AKT inhibitor, LY294002, but the ERK inhibitor U0126 had a minor effect on the hEGFinduced AQP3 upregulation. Immunohistochemical staining of the cancer tissues and corresponding normal tissues showed that AQP3 expression in cancer tissue was higher compared to that in normal tissue. The expression intensity of AQP3 was associated with the differentiation, lymph node and distant metastasis of colorectal carcinoma patients. Our results suggest that AQP3 overexpression could facilitate colorectal carcinoma cell migration and AQP3 may be considered a potential indicator and therapeutic target for colon tumor metastasis and prognosis.

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Section: Discussionmentioning

confidence: 99%

Critical role of aquaporin-3 in epidermal growth factor-induced migration of colorectal carcinoma cells and its clinical significance

Zhang

et al. 2012

Oncology Reports

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“…Second, published reports confirmed expression of several enriched genes in BCs of murine trachea and/or human airways. Examples include genes encoding Trp-63, which is required for BC development in the mouse trachea (2), Snai2, Cd109, claudin 1, Icam1, aquaporin 3, and keratins 5, 14, and 17 (3,(17)(18)(19)(20)(21). Finally, immunohistochemistry on sections of mouse trachea and normal human bronchus confirmed BC expression of several genes, including Ngfr (see below).…”

Section: Gfpmentioning

confidence: 97%

Basal cells as stem cells of the mouse trachea and human airway epithelium

Rock¹,

Onaitis

Rawlins³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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“…AQPs are upregulated in a variety of human cancers [12,17,21,30,42], and where studied, AQP expression correlates with higher tumor grade. For example, AQP4 expression is greatly upregulated in diffuse astrocytomas, with more prominent AQP4 expression in the most malignant grade IV astrocytoma (glioblastoma) [30,42].…”

Section: Aqp1 and Tumor Spreadmentioning

confidence: 99%

Aquaporins and cell migration

Papadopoulos

Saadoun

Verkman

2007

Pflugers Arch - Eur J Physiol

375

317

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Aquaporin (AQP) water channels are expressed primarily in cell plasma membranes. In this paper, we review recent evidence that AQPs facilitate cell migration. AQP-dependent cell migration has been found in a variety of cell types in vitro and in mice in vivo. AQP1 deletion reduces endothelial cell migration, limiting tumor angiogenesis and growth. AQP4 deletion slows the migration of reactive astrocytes, impairing glial scarring after brain stab injury. AQP1-expressing tumor cells have enhanced metastatic potential and local infiltration. Impaired cell migration has also been seen in AQP1-deficient proximal tubule epithelial cells, and AQP3-deficient corneal epithelial cells, enterocytes, and skin keratinocytes. The mechanisms by which AQPs enhance cell migration are under investigation. We propose that, as a consequence of actin polymerization/ depolymerization and transmembrane ionic fluxes, the cytoplasm adjacent to the leading edge of migrating cells undergoes rapid changes in osmolality. AQPs could thus facilitate osmotic water flow across the plasma membrane in cell protrusions that form during migration. AQP-dependent cell migration has potentially broad implications in angiogenesis, tumor metastasis, wound healing, glial scarring, and other events requiring rapid, directed cell movement. AQP inhibitors may thus have therapeutic potential in modulating these events, such as slowing tumor growth and spread, and reducing glial scarring after injury to allow neuronal regeneration.

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Expression of aquaporin 3 (AQP3) in normal and neoplastic lung tissues

Cited by 87 publications

References 27 publications

Critical role of aquaporin-3 in epidermal growth factor-induced migration of colorectal carcinoma cells and its clinical significance

Critical role of aquaporin-3 in epidermal growth factor-induced migration of colorectal carcinoma cells and its clinical significance

Basal cells as stem cells of the mouse trachea and human airway epithelium

Aquaporins and cell migration

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