The cellular localization of Na+/H+ exchanger 1, cystic fibrosis transmembrane conductance regulator, potassium channel, epithelial sodium channel γ and vacuolar-type H+-ATPase in human eccrine sweat glands

The secretory portions of human eccrine sweat glands secrete isotonic fluid into the lumen and then the primary fluid is rendered hypotonic during its passage to the skin surface. During the processes of sweat secretion and absorption, many enzymes and proteins play important roles. In the study, th...

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Published inActa histochemica Vol. 116; no. 8; pp. 1237 - 1243
Main Authors Li, Haihong, Zhang, Xiang, Zeng, Shaopeng, Chen, Lu, Li, Xuexue, Lin, Changmin, Zhang, Mingjun, Shu, Shenyou, Xie, Sitian, He, Yunpu, Yang, Lvjun, Tang, Shijie, Fu, Xiaobing
Format Journal Article
LanguageEnglish
Published Germany Elsevier GmbH 01.10.2014
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Summary:The secretory portions of human eccrine sweat glands secrete isotonic fluid into the lumen and then the primary fluid is rendered hypotonic during its passage to the skin surface. During the processes of sweat secretion and absorption, many enzymes and proteins play important roles. In the study, the cellular localizations of Na+/H+ exchanger 1 (NHE1), cystic fibrosis transmembrane conductance regulator (CFTR), potassium channel (KC), epithelial sodium channel γ (γENaC) and vacuolar-type H+-ATPase (V-ATPase) in human eccrine sweat glands and epidermis were detected using immunofluorescence labeling. The results revealed that in the secretory coils, the basolateral membranes showed evidence of CFTR, NHE1 and KC activities, the apical membranes showed the activities of KC and NHE1, and the nucleus showed γEaNC and V-ATPase activities; in the duct, the peripheral and luminal ductal cells showed evidence of CFTR, NHE1 and KC, the apical membranes showed the activities of CFTR and NHE1, and the nucleus showed γEaNC, V-ATPase and KC activities. The cellular localization of these proteins in eccrine sweat glands is helpful to better understand the mechanisms of sweat secretion and absorption.
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ISSN:0065-1281
1618-0372
DOI:10.1016/j.acthis.2014.07.005