Contreras Azalia, Vitale John, Hutchins-Carroll Virginia, Carroll Edward J, Oppenheimer Steven B
Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330-8303, USA.
Zygote. 2008 Nov;16(4):355-61. doi: 10.1017/S096719940800484X. Epub 2008 Oct 17.
Hyalin is a large glycoprotein, consisting of the hyalin repeat domain and non-repeated regions, and is the major component of the hyaline layer in the early sea urchin embryo of Strongylocentrotus purpuratus. The hyalin repeat domain has been identified in proteins from organisms as diverse as bacteria, sea urchins, worms, flies, mice and humans. While the specific function of hyalin and the hyalin repeat domain is incompletely understood, many studies suggest that it has a functional role in adhesive interactions. In part I of this series, we showed that hyalin isolated from the sea urchin S. purpuratus blocked archenteron elongation and attachment to the blastocoel roof occurring during gastrulation in S. purpuratus embryos, (Razinia et al., 2007). The cellular interactions that occur in the sea urchin, recognized by the U.S. National Institutes of Health as a model system, may provide insights into adhesive interactions that occur in human health and disease. In part II of this series, we showed that S. purpuratus hyalin heterospecifically blocked archenteron-ectoderm interaction in Lytechinus pictus embryos (Alvarez et al., 2007). In the current study, we have isolated hyalin from the sea urchin L. pictus and demonstrated that L. pictus hyalin homospecifically blocks archenteron-ectoderm interaction, suggesting a general role for this glycoprotein in mediating a specific set of adhesive interactions. We also found one major difference in hyalin activity in the two sea urchin species involving hyalin influence on gastrulation invagination.
透明蛋白是一种大型糖蛋白，由透明蛋白重复结构域和非重复区域组成，是紫海胆早期海胆胚胎中透明层的主要成分。透明蛋白重复结构域已在细菌、海胆、蠕虫、苍蝇、小鼠和人类等多种生物的蛋白质中被鉴定出来。虽然透明蛋白和透明蛋白重复结构域的具体功能尚未完全了解，但许多研究表明它在黏附相互作用中具有功能性作用。在本系列的第一部分中，我们表明从紫海胆中分离出的透明蛋白会阻止紫海胆胚胎原肠形成过程中发生的原肠伸长和与囊胚腔顶壁的附着（拉齐尼亚等人，2007年）。海胆中发生的细胞相互作用被美国国立卫生研究院视为一种模型系统，可能为人类健康和疾病中发生的黏附相互作用提供见解。在本系列的第二部分中，我们表明紫海胆透明蛋白会异源特异性地阻止花斑海胆胚胎中原肠-外胚层的相互作用（阿尔瓦雷斯等人，2007年）。在当前的研究中，我们从花斑海胆中分离出了透明蛋白，并证明花斑海胆透明蛋白会同源特异性地阻止原肠-外胚层的相互作用，这表明这种糖蛋白在介导一组特定的黏附相互作用中具有普遍作用。我们还发现这两种海胆在透明蛋白活性方面存在一个主要差异，即透明蛋白对原肠胚内陷的影响。
