The expression of water channel proteins during human salivary gland development: a topographic study of aquaporins 1, 3 and 5

Paula, Fernanda de; Teshima, Tathyane Harumi Nakajima; Hsieh, Ricardo; Souza, Milena Monteiro de; Coutinho‐Camillo, Cláudia Malheiros; Nico, Marcello Menta Simonsen; Lourenço, Sílvia Vanessa

doi:10.1007/s10735-017-9731-6

Cited by 22 publications

(37 citation statements)

References 42 publications

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“…In our study, AQP5 was expressed on the membranes of MEC mucous cells. In normal salivary glands, AQP5 was identified in acinar structures, as previously described [24,25,27,48]. In vitro evaluation also demonstrated the presence of AQP5 in MEC cells.…”

Section: Discussionsupporting

confidence: 71%

“…In contrast, studies of adult human glands demonstrated AQP1 in the myoepithelial cells that surround acini and intercalated ducts [25][26][27]. The presence of AQP1 in vascular endothelium and myoepithelial cells suggests that its expression may be important for water transport from the vascular lumen to the salivary gland, participating in the formation of the salivary fluid [24]. AQP1 is the only AQP expressed in myoepithelial cells [25][26][27].…”

Section: Discussionmentioning

confidence: 97%

“…De Paula et al [24] demonstrated AQP1 expression in acini, as well as in capillaries and supposed myoepithelial cells of developing human salivary glands. In contrast, studies of adult human glands demonstrated AQP1 in the myoepithelial cells that surround acini and intercalated ducts [25][26][27].…”

Section: Discussionmentioning

confidence: 99%

“…AQP1 is the only AQP expressed in myoepithelial cells [25][26][27]. Because the main function of myoepithelial cells is contractile rather than secretory, it is reasoned that high water permeability enables osmotic water flow through the "basket" of myoepithelial cells into the lateral intercellular spaces of the acinus, thereby facilitating saliva production [24,25].…”

Section: Discussionmentioning

confidence: 99%

“…In vitro evaluation also demonstrated AQP3 in MEC cells. De Paula et al [24] observed AQP3 on the basolateral surfaces of acinar structures and suggested that it plays specific roles during salivary gland development and fluid secretion. AQP3 was observed in adult glands [25][26][27]39,40] and in the basolateral surfaces of acinar and ductal structures in minor salivary glands [41].…”

Section: Discussionmentioning

confidence: 99%

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Aquaporin 1, 3, and 5 Patterns in Salivary Gland Mucoepidermoid Carcinoma: Expression in Surgical Specimens and an In Vitro Pilot Study

Stamboni

Gomes

Souza

et al. 2020

IJMS

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Salivary gland aquaporins (AQPs) are essential for the control of saliva production and maintenance of glandular structure. However, little is known of their role in salivary gland neoplasia. Salivary gland tumors comprise a heterogeneous group of lesions, featuring variable histological characteristics and diverse clinical behaviors. Mucoepidermoid carcinoma (MEC) is the most common salivary gland malignancy. The aim of this study was to evaluate the expression of AQP1, AQP3, and AQP5 in 24 MEC samples by immunohistochemistry. AQP1 expression was observed in vascular endothelium throughout the tumor stroma. AQP3 was expressed in epidermoid and mucosal cells and AQP5 was expressed in mucosal cells of MEC. These proteins were expressed in the human MEC cell line UH-HMC-3A. Cellular ultrastructural aspects were analyzed by electron microscopy to certificate the tumor cell phenotype. In summary, our results show that, despite the fact that these molecules are important for salivary gland physiology, they may not play a distinct role in tumorigenesis in MEC. Additionally, the in vitro model may offer new possibilities to further investigate mechanisms of these molecules in tumor biology and their real significance in prognosis and possible target therapies.

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Section: Discussionsupporting

confidence: 71%

Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 3 more Smart Citations

Aquaporin 1, 3, and 5 Patterns in Salivary Gland Mucoepidermoid Carcinoma: Expression in Surgical Specimens and an In Vitro Pilot Study

Stamboni

Gomes

Souza

et al. 2020

IJMS

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Distribution of alpha‐synuclein in rat salivary glands

Nishitani,

Mitoh,

Yajima

et al. 2024

The Anatomical Record

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Expression of alpha‐synuclein (Syn), a presynaptic neuronal protein, was immunohistochemically examined in intact rat submandibular, sublingual, and lingual glands. The submandibular gland contained abundant periductal Syn‐immunoreactive (−ir) nerve fibers. Abundant Syn‐ir varicosities were present in acini of the sublingual and serous lingual glands. By confocal laser scanning microscopy, Syn‐ir nerve fibers around smooth muscle actin (SMA)‐ir cells alone were infrequent; however, those around aquaporin‐5 (AQP5)‐ir cells alone and both SMA‐ and AQP5‐ir cells were abundant in the sublingual and serous lingual glands. SMA‐ir cells were occasionally immunoreactive for toll‐like receptor 4, a Syn receptor. Syn‐ir nerve fibers contained tyrosine hydroxylase (TH) in the submandibular gland and choline acetyltransferase (ChAT) in all examined salivary glands. In the superior cervical (SCG), submandibular, and intralingual ganglia, sympathetic and parasympathetic neurons co‐expressed Syn with TH and ChAT, respectively. SCG neurons innervating the submandibular gland contained mostly Syn. In the thoracic spinal cord, 14.7% of ChAT‐ir preganglionic sympathetic neurons co‐expressed Syn. In the superior salivatory nucleus, preganglionic parasympathetic neurons projecting to the lingual nerve co‐expressed Syn and ChAT. The present findings indicate that released Syn acts on myoepithelial cells. Syn in pre‐ and post‐ganglionic neurons may regulate neurotransmitter release and salivary volume and composition.

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