Na+/H+ exchangers in the human eccrine sweat duct
D Granger1, M Marsolais, J Burry
1Université de Montréal, GEPROM, C.P. 6128, Succursale Centre-ville, Montréal, Québec, Canada H3C 3J7.
Insights
The Na+/H+ exchanger 1 (NHE1) is present in human eccrine sweat ducts, particularly at the basolateral membrane. This exchanger plays a crucial role in regulating intracellular pH within the sweat duct.
Area of Science:
- Physiology
- Molecular Biology
- Cell Biology
Background:
- The Na+/H+ exchanger 1 (NHE1) is a key protein involved in cellular pH homeostasis.
- Its role in the human eccrine sweat duct, a critical component of thermoregulation and electrolyte balance, remains largely uncharacterized.
Purpose of the Study:
- To investigate the presence and functional role of Na+/H+ exchanger isoform 1 (NHE1) in the human eccrine sweat duct.
- To elucidate the contribution of NHE1 to intracellular pH regulation in this tissue.
Main Methods:
- Immunohistochemical analysis using an anti-NHE1 antibody to localize NHE1 expression in human eccrine sweat ducts.
- In vitro perfusion of isolated straight sweat duct portions to assess Na+/H+ mediated proton transport under various conditions, including EIPA treatment and ion removal.
Main Results:
- NHE1 was localized to the basolateral and lateral membranes of eccrine sweat duct cells, but not the luminal membrane.
- Basolateral EIPA induced significant intracellular acidification, while luminal EIPA had no effect.
- Removal of bath sodium resulted in stronger acidification, and manipulation of luminal sodium and chloride levels suggested functional activity of NHE1 at the intercellular junction.
Conclusions:
- NHE1 is expressed in the human eccrine sweat duct, primarily at the basolateral and lateral membranes.
- Functional studies confirm that NHE1 is actively involved in regulating intracellular pH within the sweat duct epithelium.
- These findings highlight the importance of NHE1 in maintaining cellular homeostasis in eccrine sweat glands.
Abstract:
Using an anti-NHE1 antibody, we demonstrate the presence of a Na+/H+ exchanger of isoform 1 (NHE1) in the human eccrine sweat duct. A strong staining was observed at the basolateral membrane of the outer cell layer (NHE1basal), at the junction between inner and outer cells layers (NHE1inter), and along the lateral membranes (NHE1later) of all cells of the duct. At the luminal membrane, no staining was demonstrated either for NHE1 or NHE3. To investigate Na+/H+ mediated proton transport, straight sweat duct portions were isolated and perfused in vitro under HCO3-free conditions. In the presence of basolateral 5-ethyl-N-isopropyl amiloride (EIPA), an acidification of 0.29 +/- 0.03 pH units was observed, whereas no effect was observed with luminal EIPA. Bath sodium removal generated a stronger acidification (0.41 +/- 0.09 pH units). Removal of luminal sodium (in the absence or presence of basolateral EIPA), or low luminal chloride, led to an alkalinization, presumably due to a decrease in intracellular sodium, strongly suggesting functional activity of NHE1inter. We therefore conclude that in the sweat duct, NHE1 plays a major role in intracellular pH regulation.
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