Expression and localization of aqua-glyceroporins AQP3 and AQP9 in rat oral epithelia.
Aquaporins (AQPs) are a family of small integral membrane proteins made up of 6 hydrophobic, a-helical, membrane-spanning domains surrounding a highly selective aqueous pore. AQP3, AQP7, and AQP9, termed aqua-glyceroporins, are known to be involved in the transport of water, glycerol, and other small molecules. In this study, we investigated the expression and localization of aqua-glyceroporins in rat oral stratified squamous epithelia of the palate, the buccal mucosa, the inferior aspect of the tongue, and the oral floor by using RT-PCR, immunofluorescence, and immunogold electron microscopy. AQP3 and AQP9 mRNAs were expressed in whole oral epithelium. Immunostaining for AQP3 was recognized in each type of epithelium. The results suggest that AQP3 synthesis begins predominantly in the cytoplasm of the basal cells. During the process of epithelial cell differentiation, AQP3 protein appears to accumulate and be transported to the plasma membrane, from where it is incorporated into the cornified or surface layers. The intracellular localization of AQP3 appears to correlate with the differentiation of keratinocytes, suggesting that it acts as an enhancer of the physiological permeability barrier together with membrane coating granules. The distribution pattern of AQP9 was limited to the marginal areas of the basal and suprabasal layers, which was different from that of AQP3. This difference in distribution between AQP3 and AQP9 suggests that AQP9 in rat oral epithelia acts as a channel by facilitating glycerol uptake from the blood through the endothelial cells of the capillary vessels to the oral stratified squamous epithelium. AQP3 and AQP9 facilitate both transcellular osmotic water flow and glycerol transport as pore-like passive transporters in the keratinocytes of oral epithelia, and may play a key role in not only hydration and the permeability barrier, but also cell proliferation, differentiation, migration, development, and wound healing by generating ATP.
Department of Removable Prosthodontics and Gerodontology, Tokyo Dental College.
Marlene
M
Poveda
Sadamitsu
S
Hashimoto
Yasunobu
Y
Enokiya
Miwako
M
Matsuki-Fukushima
Hodaka
H
Sasaki
Kaoru
K
Sakurai
Masaki
M
Shimono
D000818:Animals; D051400:Aquaporin 3 / Q000032:analysis*; D020346:Aquaporins / Q000032:analysis*; D002454:Cell Differentiation / Q000502:physiology; D002462:Cell Membrane / Q000737:chemistry; D002463:Cell Membrane Permeability / Q000502:physiology; D002610:Cheek; D003593:Cytoplasm / Q000737:chemistry; D042783:Endothelial Cells / Q000378:metabolism; D004847:Epithelial Cells / Q000737:chemistry; D004848:Epithelium / Q000737:chemistry; D005990:Glycerol / Q000097:blood / Q000378:metabolism; D015603:Keratinocytes / Q000737:chemistry; D008297:Male; D009060:Mouth Floor / Q000737:chemistry; D009061:Mouth Mucosa / Q000737:chemistry*; D009995:Osmosis / Q000502:physiology; D010159:Palate / Q000737:chemistry; D051381:Rats; D014059:Tongue / Q000737:chemistry
C496029:Aqp3 protein, rat; C491637:Aqp9 protein, rat; D020346:Aquaporins; D051400:Aquaporin 3; D005990:Glycerol