open access

Vol 49, No 3 (2011)
ORIGINAL PAPERS
Published online: 2011-10-28
Submitted: 2012-01-05
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Immunodetection of aquaporin 5 in sheep salivary glands related to pasture vegetative cycle

Paola Scocco, Marina Aralla, Andrea Catorci, Carlo Belardinelli, Silvana Arrighi
DOI: 10.5603/FHC.2011.0065
·
Folia Histochem Cytobiol 2011;49(3):458-464.

open access

Vol 49, No 3 (2011)
ORIGINAL PAPERS
Published online: 2011-10-28
Submitted: 2012-01-05

Abstract

Mammalian aquaporins (AQPs) are a family of at least 13 integral membrane proteins expressed in various epithelia, where they function as channels to permeate water and small solutes. AQP5 is widely expressed in the exocrine gland where it is likely involved in providing an appropriate amount of fluid to be secreted with granular contents. As regards AQP5 expression in the salivary glands, literature is lacking concerning domestic animal species. This study was chiefly aimed at immunohistochemically investigating the presence and localization of AQP5 in sheep mandibular and parotid glands. In addition, AQP5 immunoreactivity was comparatively evaluated in animals fed with forage containing different amounts of water related to the pasture vegetative cycle, in order to shed light on the possible response of the gland to environmental modifications. Moderate AQP5-immunoreactivity was shown at the level of the lateral surface of mandibular serous demilune cells, not affected by the pasture vegetative cycle or water content. On the contrary, the parotid gland arcinar cells showed AQP5-immunoreactivity at the level of apical and lateral plasma membrane, which was slight to very strong, according to the pasture vegetative development and interannual climatic variations. AQP5 expression is likely due to its involvement in providing appropriate saliva fluidity. Indeed, the lowest AQP5 immunoreactivity was noticed when food water content increased. (Folia Histochemica et Cytobiologica 2011; Vol. 49, No. 3, pp. 458–464)

Abstract

Mammalian aquaporins (AQPs) are a family of at least 13 integral membrane proteins expressed in various epithelia, where they function as channels to permeate water and small solutes. AQP5 is widely expressed in the exocrine gland where it is likely involved in providing an appropriate amount of fluid to be secreted with granular contents. As regards AQP5 expression in the salivary glands, literature is lacking concerning domestic animal species. This study was chiefly aimed at immunohistochemically investigating the presence and localization of AQP5 in sheep mandibular and parotid glands. In addition, AQP5 immunoreactivity was comparatively evaluated in animals fed with forage containing different amounts of water related to the pasture vegetative cycle, in order to shed light on the possible response of the gland to environmental modifications. Moderate AQP5-immunoreactivity was shown at the level of the lateral surface of mandibular serous demilune cells, not affected by the pasture vegetative cycle or water content. On the contrary, the parotid gland arcinar cells showed AQP5-immunoreactivity at the level of apical and lateral plasma membrane, which was slight to very strong, according to the pasture vegetative development and interannual climatic variations. AQP5 expression is likely due to its involvement in providing appropriate saliva fluidity. Indeed, the lowest AQP5 immunoreactivity was noticed when food water content increased. (Folia Histochemica et Cytobiologica 2011; Vol. 49, No. 3, pp. 458–464)
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Keywords

AQP5; sheep; salivary glands; pasture vegetative cycle; immunohistochemistry

About this article
Title

Immunodetection of aquaporin 5 in sheep salivary glands related to pasture vegetative cycle

Journal

Folia Histochemica et Cytobiologica

Issue

Vol 49, No 3 (2011)

Pages

458-464

Published online

2011-10-28

DOI

10.5603/FHC.2011.0065

Bibliographic record

Folia Histochem Cytobiol 2011;49(3):458-464.

Keywords

AQP5
sheep
salivary glands
pasture vegetative cycle
immunohistochemistry

Authors

Paola Scocco
Marina Aralla
Andrea Catorci
Carlo Belardinelli
Silvana Arrighi

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