Related Experiment Video
Updated: Aug 8, 2026

An Isolated Semi-intact Preparation of the Mouse Vestibular Sensory Epithelium for Electrophysiology and High-resolution Two-photon Microscopy
Published on: June 13, 2013
Vacuolar-type H+ -ATPase distribution in unstimulated and acetylcholine-activated isolated human eccrine sweat glands
D L Bovell1, M T Clunes, E Roussa
1School of Biological and Biomedical Sciences, Glasgow Caledonian University, UK.
Insights
This study investigated vacuolar-type H+-ATPase (V-ATPase) in human sweat glands. V-ATPase was found in various cell locations, with no changes observed after acetylcholine stimulation.
Area of Science:
- Physiology
- Cell Biology
- Biochemistry
Background:
- The vacuolar-type H+-ATPase (V-ATPase) is a critical proton pump involved in various cellular functions.
- Understanding V-ATPase distribution in human eccrine sweat glands is essential for elucidating sweat production and reabsorption mechanisms.
Purpose of the Study:
- To investigate the cellular localization and distribution of V-ATPase subunits within isolated human eccrine sweat glands.
- To determine if acetylcholine stimulation affects V-ATPase expression in these glands.
Main Methods:
- Immunohistochemical analysis of V-ATPase subunits in isolated human eccrine sweat glands.
- Observation of cellular and subcellular localization (cytoplasm, membranes, intercellular canaliculi).
- Assessment of V-ATPase expression following stimulation with 100 microM acetylcholine.
Main Results:
- V-ATPase was consistently found in the cytoplasm and apical membranes of luminal cells in the reabsorptive duct segment.
- In the secretory coil, V-ATPase exhibited diffuse and perinuclear staining in secretory cells, with expression on apical and basolateral membranes and intercellular canaliculi.
- No significant difference in V-ATPase expression was detected after acetylcholine application.
Conclusions:
- The V-ATPase is present in multiple cellular compartments of human eccrine sweat glands, suggesting diverse roles in ductal and secretory cells.
- Acetylcholine does not appear to modulate V-ATPase expression in these glands under the tested conditions.
- Further research is warranted to fully elucidate the specific functions of V-ATPase in eccrine sweat gland physiology.
Abstract:
The presence and cellular distribution of subunits of the V1 sector of the vacuolar-type H+ -ATPase (V-ATPase) was investigated in isolated human eccrine sweat glands. In every instance, V-ATPase was located in the cytoplasm and apical membranes of the luminal cells of the reabsorptive duct segment. In the secretory coil, both diffuse and perinuclear staining was demonstrated in the secretory cells, with additional expression at the apical and basolateral membranes and on the intercellular canaliculi. There was no detectable difference in V-ATPase expression as a result of prior application of 100 microM acetylcholine.
Related Concept Videos
ATP Driven Pumps I: An Overview
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
ATP Driven Pumps II: P-type Pumps
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
ATP Driven Pumps III: V-type Pumps
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
Accessory Structures of the Skin: Sweat Glands
Sweat glands are classified as merocrine glands; that is, the secretions are excreted by exocytosis through a duct without affecting the cells of the gland. There...
Cholinergic Receptors: Muscarinic
The subtypes M1, M3, and M5 couple with the Gq subunit and activate the phospholipase C (PLC) activity, mobilizing intracellular Ca2+. Activation...
Relaxation of Skeletal Muscles
When an action potential reaches the axon terminal, it depolarizes the membrane and opens voltage-gated sodium channels. Sodium ions enter the cell, further depolarizing the presynaptic membrane. This depolarization causes voltage-gated calcium channels to open.

