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晶状体、心脏和肝脏中缝隙连接蛋白之间的同源性。

Homologies between gap junction proteins in lens, heart and liver.

作者信息

Kistler J, Christie D, Bullivant S

机构信息

Department of Cellular and Molecular Biology, University of Auckland, New Zealand.

出版信息

Nature. 1988 Feb 25;331(6158):721-3. doi: 10.1038/331721a0.

Abstract

The cells in the mammalian lens are electrically and metabolically coupled with each other by a network of gap junctions. These are clusters of transmembrane channels by which the fibre cells situated deeper in the lens communicate through the epithelium with the aqueous humour, the source of nutrients for the lens. Hence gap junctions are important for lens transparency. The gap junction proteins in the mammalian lens have not yet been identified with certainty. A putative fibre gap junction protein of relative molecular mass 26,000 (26K) is not related to those from other tissues, such as the liver 28K junction component. Another lens membrane protein with Mr 70K (MP70) has also been localized in the lens fibre gap junctions. Here we demonstrate by amino-terminal sequence analysis that MP70 and its in vivo-processed form, MP38 (ref. 8), belong to a wider family of gap junction proteins. With this new data on the lens, homologies between gap junction proteins now extend to organs derived from all three embryonal layers, endoderm (liver), mesoderm (heart) and ectoderm (lens).

摘要

哺乳动物晶状体中的细胞通过缝隙连接网络在电学和代谢上相互耦联。这些是跨膜通道簇,晶状体中较深层的纤维细胞通过它们与作为晶状体营养来源的房水进行上皮间的沟通。因此,缝隙连接对晶状体的透明度很重要。哺乳动物晶状体中的缝隙连接蛋白尚未得到确切鉴定。一种相对分子质量为26,000(26K)的假定纤维缝隙连接蛋白与其他组织中的蛋白无关,如肝脏的28K连接成分。另一种分子量为70K的晶状体膜蛋白(MP70)也定位于晶状体纤维缝隙连接中。在这里,我们通过氨基末端序列分析证明,MP70及其体内加工形式MP38(参考文献8)属于更广泛的缝隙连接蛋白家族。基于晶状体的这一新数据,缝隙连接蛋白之间的同源性现在扩展到源自所有三个胚胎层的器官,即内胚层(肝脏)、中胚层(心脏)和外胚层(晶状体)。

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