Vesterdorf Kristine, Blache Dominique, Maloney Shane K
School of Anatomy, Physiology and Human Biology M309, The University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia.
UWA Institute of Agriculture (Animal Production) M085, The University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia.
J Therm Biol. 2014 Jul;43:61-9. doi: 10.1016/j.jtherbio.2014.04.003. Epub 2014 May 14.
The nasal respiratory mucosa is the primary site for evaporative water loss in panting species, necessitating the movement of water across the nasal epithelium. Aquaporins (AQP) are protein channels that facilitate water movement in various fluid transporting tissues of non-panting species. Whether the requirement for enhanced capacity for transepithelial water movement in the nasal respiratory mucosa of panting species has led to differences in AQP localization is unknown. Using immunohistochemistry, we report the localization of AQP1, 3, and 5 in the nasal respiratory mucosa of sheep being exposed to ambient temperatures of ~21 °C or ~38 °C for 4.5 h before death (n=3/treatment). Exposure to either treatment resulted in panting. While exposure to ~38 °C resulted in a higher respiratory frequency (mean difference: 82 breaths min(-1); P<0.001) than exposure to ~21 °C, there was no difference in the localization of AQPs. Connective tissue and vascular endothelial cells expressed AQP1. Glandular acini expressed AQP1 and apically localized AQP5, which was also present in glandular duct cells. Ciliated columnar epithelial cells expressed AQP5 apically and AQP3 basolaterally. Basal cells expressed AQP3. The distribution and co-localization of AQPs in the ovine nasal respiratory mucosa is different to that reported in non-panting species and may reflect the physiological demands associated with enhanced respiratory evaporation. We propose that AQP1, 3, and 5 may constitute a transepithelial water pathway via glandular secretions and across the surface epithelium, which provides a possible means for rapid and controllable water movement in the nasal respiratory mucosa of a panting species.
在喘气动物中,鼻腔呼吸黏膜是水分蒸发散失的主要部位,这就需要水分穿过鼻上皮细胞。水通道蛋白(AQP)是一类蛋白质通道,可促进非喘气动物各种液体运输组织中的水分移动。目前尚不清楚喘气动物鼻呼吸黏膜对上皮细胞水分运输能力增强的需求是否导致了水通道蛋白定位的差异。我们采用免疫组织化学方法,报告了在死亡前4.5小时暴露于约21℃或约38℃环境温度下的绵羊鼻呼吸黏膜中AQP1、3和5的定位情况(每组n = 3)。两种处理均导致动物喘气。虽然暴露于约38℃时的呼吸频率高于暴露于约21℃时(平均差异:82次/分钟;P < 0.001),但水通道蛋白的定位没有差异。结缔组织和血管内皮细胞表达AQP1。腺泡表达AQP1,且AQP5定位于腺泡顶端,腺管细胞中也有AQP5。纤毛柱状上皮细胞顶端表达AQP5,基底外侧表达AQP3。基底细胞表达AQP3。绵羊鼻呼吸黏膜中水通道蛋白的分布和共定位与非喘气动物中报道的不同,可能反映了与增强呼吸蒸发相关的生理需求。我们认为,AQP1、3和5可能通过腺体分泌物并穿过表面上皮细胞构成一条上皮细胞间的水运输途径,这为喘气动物鼻呼吸黏膜中水分的快速可控移动提供了一种可能的方式。