Fascin - An actin binding and bundling protein in the testis and its role in ectoplasmic specialization dynamics.

Spermatogenesis Pub Date : 2015-02-23 eCollection Date: 2015-01-01 DOI:10.1080/21565562.2014.1002733
N Ece Gungor-Ordueri, C Yan Cheng
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引用次数: 2

Abstract

In the mammalian testis such as in rats, a unique actin-rich cell-cell adherens junction (AJ) known as ectoplasmic specialization (ES) is found in the seminiferous epithelium. ES is conspicuously found between Sertoli cells near the basement membrane known as the basal ES, which together with tight junction (TJ), gap junction, and desmosome constitute the blood-testis barrier (BTB). The BTB, in turn, anatomically divides the seminiferous epithelium into the basal and the adluminal (apical) compartment. On the other hand, ES is also found at the Sertoli-spermatid interface known as apical ES which is the only anchoring device for developing step 8-19 spermatids during spermiogenesis. One of the most typical features of the ES is the array of actin microfilament bundles that lie perpendicular to the Sertoli cell plasma membrane and are sandwiched in-between the cisternae of endoplasmic reticulum and the Sertoli cell plasma membrane. While these actin filament bundles confer the adhesive strength of Sertoli cells at the BTB and also spermatids in the adluminal compartment, they must be rapidly re-organized from their bundled to unbundled/branched configuration and vice versa to provide plasticity to the ES so that preleptotene spermatocytes and spermatids can be transported across the immunological barrier and the adluminal compartment, respectively, during the epithelial cycle of spermatogenesis. Fascin is a family of actin microfilament cross-linking and bundling proteins that is known to confer bundling of parallel actin microfilaments in mammalian cells. A recent report has illustrated the significance of a fascin protein called fascin 1 in actin microfilaments at the ES, pertinent to its role in spermatogenesis (Gungor-Ordueri et al. Am J Physiol Endocrinol Metab 307, E738-753, 2004 (DOI:10.1152/ajpendo.00113.2014). In this Commentary, we critically evaluate these findings in light of the role of fascin in other mammalian cells, providing some insightful information for future investigations.

Abstract Image

筋膜蛋白-睾丸中的肌动蛋白结合和捆绑蛋白及其在外质特化动力学中的作用。
在哺乳动物睾丸中,如大鼠,在精原上皮中发现了一种独特的富含肌动蛋白的细胞-细胞粘附连接(AJ),称为外质特化(ES)。ES明显存在于基底膜附近的支持细胞之间,称为基底ES,它与紧密连接(TJ)、间隙连接和桥粒一起构成血睾丸屏障(BTB)。BTB在解剖上又将精原上皮分为基室和顶室。另一方面,在精子形成过程中,支持细胞与精子的界面也发现了ES,称为顶端ES,这是精子形成过程中第8-19步精子发育的唯一锚定装置。ES最典型的特征之一是肌动蛋白微丝束阵列垂直于支持细胞膜,夹在内质网池和支持细胞膜之间。虽然这些肌动蛋白丝束赋予了BTB上的支持细胞和输卵管腔内的精子细胞的粘附强度,但它们必须从束状结构迅速重组为非束状/支状结构,反之亦然,从而为ES提供可塑性,以便在精子发生的上皮周期中,preleptotene精母细胞和精子细胞能够分别通过免疫屏障和输卵管腔运输。筋膜蛋白是一个肌动蛋白微丝交联和捆绑蛋白家族,已知在哺乳动物细胞中赋予平行肌动蛋白微丝捆绑。最近的一份报告表明,在ES肌动蛋白微丝中,一种被称为筋膜蛋白1的筋膜蛋白的重要性与其在精子发生中的作用有关(gungore - ordueri等)。[J] .中国生物医学工程学报,2016,33(4):357 - 357。在这篇评论中,我们结合其他哺乳动物细胞中筋膜蛋白的作用对这些发现进行了批判性的评价,为未来的研究提供了一些有见解的信息。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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