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埃米林(Emilin),一种弹性纤维的成分,优先位于弹性蛋白 - 微原纤维界面。

Emilin, a component of elastic fibers preferentially located at the elastin-microfibrils interface.

作者信息

Bressan G M, Daga-Gordini D, Colombatti A, Castellani I, Marigo V, Volpin D

机构信息

Istituto di Istologia ed Embriologia, Università di Padova, Italy.

出版信息

J Cell Biol. 1993 Apr;121(1):201-12. doi: 10.1083/jcb.121.1.201.

Abstract

The fine distribution of the extracellular matrix glycoprotein emilin (previously known as glycoprotein gp115) (Bressan, G. M., I. Castellani, A. Colombatti, and D. Volpin. 1983. J. Biol. Chem. 258: 13262-13267) has been studied at the ultrastructural level with specific antibodies. In newborn chick aorta the protein was exclusively found within elastic fibers. In both post- and pre-embedding immunolabeling emilin was mainly associated with regions where elastin and microfibrils are in close contact, such as the periphery of the fibers. This localization of emilin in aorta has been confirmed by quantitative evaluation of the distribution of gold particles within elastic fibers. In other tissues, besides being associated with typical elastic fibers, staining for emilin was found in structures lacking amorphous elastin, but where the presence of tropoelastin has been demonstrated by immunoelectron microscopy. This was particularly evident in the oxitalan fibers of the corneal stroma, in the Descemet's membrane, and in the ciliary zonule. Analysis of embryonic aorta revealed the presence of emilin at early stages of elastogenesis, before the appearance of amorphous elastin. Immunofluorescence studies have shown that emilin produced by chick embryo aorta cells in culture is strictly associated with elastin and that the process of elastin deposition is severely altered by the presence of antiemilin antibodies in the culture medium. The name of the protein was derived from its localization at sites where elastin and microfibrils are in proximity (emilin, elastin microfibril interface located protein).

摘要

利用特异性抗体在超微结构水平上研究了细胞外基质糖蛋白埃米林(Emilin,以前称为糖蛋白gp115)(布雷桑,G.M.,I.卡斯特拉尼,A.科隆巴蒂和D.沃尔平。1983年。《生物化学杂志》258:13262 - 13267)的精细分布。在新生雏鸡主动脉中,该蛋白仅存在于弹性纤维内。在包埋后和包埋前免疫标记中,埃米林主要与弹性蛋白和微原纤维紧密接触的区域相关,如纤维的周边。通过对弹性纤维内金颗粒分布的定量评估,已证实埃米林在主动脉中的这种定位。在其他组织中,除了与典型的弹性纤维相关外,在缺乏无定形弹性蛋白但免疫电子显微镜已证实存在原弹性蛋白的结构中也发现了埃米林染色。这在角膜基质的氧化弹性纤维、后弹力层和睫状小带中尤为明显。对胚胎主动脉的分析显示,在无定形弹性蛋白出现之前的弹性生成早期阶段就存在埃米林。免疫荧光研究表明,培养的鸡胚主动脉细胞产生的埃米林与弹性蛋白紧密相关,并且培养基中抗埃米林抗体的存在会严重改变弹性蛋白的沉积过程。该蛋白的名称源于其在弹性蛋白和微原纤维相邻部位的定位(埃米林,位于弹性蛋白微原纤维界面的蛋白)。

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