Distinct expression patterns of different subunit Isoforms of the V-ATPase in the rat epididymis
Distinct expression patterns of different subunit Isoforms of the V-ATPase in the rat epididymis
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DOI：
10.1095/biolreprod.105.043752
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发表时间：
2006-01-01
影响因子：
3.6
通讯作者：
Breton, S
中科院分区：
文献类型：
--
作者：
Pietrement, C;Sun-Wada, GH;Breton, S
在附睾和输精管中，液泡H(+) atp酶（v - atp酶）位于狭窄而透明的细胞顶极，需要它来建立酸性腔内pH。低pH对精子的成熟和静止状态下的储存很重要。v - atp酶也参与胞内细胞器的酸化。v - atp酶含有许多亚基，其中一些亚基具有多种同工型。到目前为止，在大鼠附睾中只发现了先前鉴定为131、132和E亚基的ATP6V1B1、ATP6V1B2和ATP6V1E2亚基。在这里，我们报道了V-ATPase亚基异构体ATP6V1A、ATP6V1C1、ATP6V1C2、ATP6V1G1、ATP6V1G3、ATP6V0A1、ATP6V0A2、ATP6V0A4、ATP6V0D1和ATP6V0D2在大鼠附睾和输精管上皮细胞中的定位，之前标记为A、C1、C2、G1、G3、a1、a2、a4、d1和d2。除ATP6V0A2亚型外，狭窄而透明的细胞在所有亚基中都显示出强烈的顶端染色。ATP6V0A2和ATP6V1A亚基在主细胞和窄/透明细胞的TGN密切相关但不完全相同的细胞内结构中检测到，ATP6V0D1亚基在其他V-ATPase亚基明显缺失的情况下在主细胞的顶膜中强烈表达。综上所述，v - atp酶的ATP6V1C、ATP6V1G、ATP6V0A和ATP6V0D的多个亚型存在于附睾和输精管上皮中。我们的结果证实，狭窄和透明的细胞非常适合活跃的质子分泌。此外，V-ATPase的多种功能可以通过利用特定的亚基异构体来建立。在主细胞中，ATP6V0D1异构体可能具有不同于其通过V-ATPase复合物进行质子运输的生理功能。
In the epididymis and vas deferens, the vacuolar H(+)ATPase (V-ATPase), located in the apical pole of narrow and clear cells, is required to establish an acidic luminal pH. Low pH is important for the maturation of sperm and their storage in a quiescent state. The V-ATPase also participates in the acidification of intracellular organelles. The V-ATPase contains many subunits, and several of these subunits have multiple isoforms. So far, only subunits ATP6V1B1, ATP6V1B2, and ATP6V1E2, previously identified as 131, 132, and E subunits, have been described in the rat epididymis. Here, we report the localization of V-ATPase subunit isoforms ATP6V1A, ATP6V1C1, ATP6V1C2, ATP6V1G1, ATP6V1G3, ATP6V0A1, ATP6V0A2, ATP6V0A4, ATP6V0D1, and ATP6V0D2, previously labeled A, C1, C2, G1, G3, a1, a2, a4, d1, and d2, in epithelial cells of the rat epididymis and vas deferens. Narrow and clear cells showed a strong apical staining for all subunits, except the ATP6V0A2 isoform. Subunits ATP6V0A2 and ATP6V1A were detected in intracellular structures closely associated but not identical to the TGN of principal cells and narrow/clear cells, and subunit ATP6V0D1 was strongly expressed in the apical membrane of principal cells in the apparent absence of other V-ATPase subunits. In conclusion, more than one isoform of subunits ATP6V1C, ATP6V1G, ATP6V0A, and ATP6V0D of the V-ATPase are present in the epididymal and vas deferens epithelium. Our results confirm that narrow and clear cells are well fit for active proton secretion. In addition, the diverse functions of the V-ATPase may be established through the utilization of specific subunit isoforms. In principal cells, the ATP6V0D1 isoform may have a physiological function that is distinct from its role in proton transport via the V-ATPase complex.