Petrova Rosica S, Schey Kevin L, Donaldson Paul J, Grey Angus C
School of Medical Sciences, University of Auckland, Auckland, New Zealand.
Departments of Biochemistry and Ophthalmology, Vanderbilt University, Nashville, TN, USA.
Exp Eye Res. 2015 Mar;132:124-35. doi: 10.1016/j.exer.2015.01.011. Epub 2015 Jan 13.
The expression of the water channel protein aquaporin (AQP)-5 in adult rodent and human lenses was recently reported using immunohistochemistry, molecular biology, and mass spectrometry techniques, confirming a second transmembrane water channel that is present in lens fibre cells in addition to the abundant AQP0 protein. Interestingly, the sub-cellular distribution and level of post-translational modification of both proteins changes with fibre cell differentiation and location in the adult rodent lens. This study compares the sub-cellular distribution of AQP0 and AQP5 during embryonic and postnatal fibre cell development in the mouse lens to understand how the immunolabelling patterns for both AQPs observed in adult lens are first established. Immunohistochemistry was used to map the cellular and sub-cellular distribution of AQP5 and AQP0 throughout the lens in cryosections from adult (6 weeks-8 months) and postnatal (0-2 weeks) mouse lenses and in sections from paraffin embedded mouse embryos (E10-E19). All sections were imaged by fluorescence confocal microscopy. Using antibodies directed against the C-terminus of each AQP, AQP5 was abundantly expressed early in development, being found in the cytoplasm of cells of the lens vesicle and surrounding tissues (E10), while AQP0 was detected later (E11), and only in the membranes of elongating primary fibre cells. During the course of subsequent embryonic and postnatal development the pattern of cytoplasmic AQP5 and membranous AQP0 labelling was maintained until postnatal day 6 (P6). From P6 AQP5 labelling became progressively more membranous initially in the lens nucleus and then later in all regions of the lens, while AQP0 labelling was abruptly lost in the lens nucleus due to C-terminal truncation. Our results show that the spatial distribution patterns of AQP0 and AQP5 observed in the adult lens are established during a narrow window of postnatal development (P6-P15) that precedes eye opening and coincides with regression of the hyaloid vascular system. Our results support the hypothesis that, in the older fibre cells, insertion of AQP5 into the fibre cell membrane may compensate for any change in the functionality of AQP0 induced by truncation of its C-terminal tail.
最近有研究运用免疫组织化学、分子生物学和质谱技术报道了水通道蛋白水通道蛋白(AQP)-5在成年啮齿动物和人类晶状体中的表达情况,证实除了大量存在的AQP0蛋白外,晶状体纤维细胞中还存在第二种跨膜水通道。有趣的是,在成年啮齿动物晶状体中,这两种蛋白的亚细胞分布和翻译后修饰水平会随着纤维细胞的分化和位置变化而改变。本研究比较了AQP0和AQP5在小鼠晶状体胚胎期和出生后纤维细胞发育过程中的亚细胞分布,以了解成年晶状体中观察到的两种水通道蛋白的免疫标记模式是如何首次建立的。免疫组织化学用于绘制AQP5和AQP0在成年(6周 - 8个月)和出生后(0 - 2周)小鼠晶状体冰冻切片以及石蜡包埋小鼠胚胎(E10 - E19)切片整个晶状体中的细胞和亚细胞分布。所有切片均通过荧光共聚焦显微镜成像。使用针对每种水通道蛋白C末端的抗体,AQP5在发育早期大量表达,在晶状体泡细胞和周围组织的细胞质中可见(E10),而AQP0稍后(E11)才被检测到,且仅在伸长的初级纤维细胞膜中出现。在随后的胚胎期和出生后发育过程中,细胞质中AQP5和膜上AQP0的标记模式一直保持到出生后第6天(P6)。从P6开始,AQP5标记最初在晶状体核中逐渐更多地出现在膜上,随后在晶状体的所有区域均如此,而AQP0标记由于C末端截短在晶状体核中突然消失。我们的结果表明,成年晶状体中观察到的AQP0和AQP5的空间分布模式是在出生后发育的一个狭窄窗口(P6 - P15)期间建立的,该窗口先于睁眼且与玻璃体血管系统的退化同时发生。我们的结果支持这样的假说,即在较老的纤维细胞中,AQP5插入纤维细胞膜可能补偿了由于其C末端尾巴截短而导致的AQP0功能的任何变化。