Immunolocalization of aquaporin-5 expression in sweat gland cells from normal and anhidrotic horses.
Abstract: Western blot analysis showed that sweat gland cells from freely sweating horses expressed the water channel aquaporin-5 (AQP-5). Immunohistochemistry revealed a strong AQP-5-like activity reaction at the apical membrane of the glandular secretory cells, which was absent from the surrounding myoepithelium and all other skin structures. In anhidrotic horses, AQP-5 was also found at the apical membrane of the luminal sweat gland cells, but the level of expression reduced with the length of time that the animal had displayed anhidrosis. The level of AQP-5 expression was substantially reduced in animals with long-term anhidrosis, hence implicating water channel impairment as a possible factor in the development of this disorder.
Publication Date: 2006-01-18 PubMed ID: 16412116DOI: 10.1111/j.1365-3164.2005.00498.xGoogle Scholar: Lookup
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- Journal Article
Summary
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The researchers of this article identified a water channel protein called aquaporin-5 (AQP-5) in the sweat gland cells of healthy horses, but discovered its expression decreased in horses with anhidrosis, a condition in which they cannot sweat normally. The reduced presence of AQP-5 in horses suffering from long-term anhidrosis might imply that impaired water channel functionality can contribute to the disorder.
Research Objective and Approach
- The researchers attempted to identify and trace the expression of aquaporin-5(AQP-5), a protein that regulates the movement of water through cell membranes, in the sweat gland cells of normal and anhidrotic horses.
- This study was conducted using Western blot analysis, which is a technique to detect specific proteins in a sample, as well as immunohistochemistry, a process which uses antibodies to visually tag a specific protein in a tissue sample.
Findings
- The researchers found out that in healthy horses that sweat normally, AQP-5 was present in the sweat gland cells. Specifically, this protein was strongly present at the apical membrane of the glandular secretory cells.
- However, in anhidrotic horses (horses that cannot sweat properly), the researchers discovered that although AQP-5 was also present at the apical membrane of the sweat gland cells, its expression level was lessened and it further diminished alongside the duration of the anhidrosis condition.
Implications
- The study suggests that impairment in the water channels, reflected by a decreased expression of AQP-5, could be a potential contributory factor in the development of anhidrosis in horses. This implies the potential role of AQP-5 in modulating the process of sweating.
- The findings of this study can direct future research towards exploring the therapeutic potential of influencing AQP-5 levels in managing anhidrosis in horses, as well as the role of similar water channel proteins in human sweating and related disorders.
Cite This Article
APA
Bovell DL, Lindsay SL, Corbett AD, Steel C.
(2006).
Immunolocalization of aquaporin-5 expression in sweat gland cells from normal and anhidrotic horses.
Vet Dermatol, 17(1), 17-23.
https://doi.org/10.1111/j.1365-3164.2005.00498.x Publication
Researcher Affiliations
- Department of Biological and Biomedical Science, Glasgow Caledonian University, Glasgow, G4 0BA, UK. d.bovell@gcal.ac.uk
MeSH Terms
- Animals
- Aquaporin 5 / isolation & purification
- Aquaporin 5 / metabolism
- Blotting, Western / veterinary
- Case-Control Studies
- Horse Diseases / metabolism
- Horse Diseases / pathology
- Horses
- Hypohidrosis / metabolism
- Hypohidrosis / pathology
- Hypohidrosis / veterinary
- Immunohistochemistry / veterinary
- Sweat Glands / metabolism
Citations
This article has been cited 2 times.- Hew-Butler T, Hummel J, Rider BC, Verbalis JG. Characterization of the effects of the vasopressin V2 receptor on sweating, fluid balance, and performance during exercise. Am J Physiol Regul Integr Comp Physiol 2014 Aug 15;307(4):R366-75.
- Calamita G, Delporte C. Aquaporins in Glandular Secretion. Adv Exp Med Biol 2023;1398:225-249.
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