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桥粒结合抗体KM48识别一种不同于桥粒钙黏蛋白Dsg 1-3和Dsc 1-3的细胞外抗原。

Desmosome-binding antibody KM48 recognises an extracellular antigen different from desmosomal cadherins Dsg 1-3 and Dsc 1-3.

作者信息

Duhieu Stéphane, Laperdrix Céline, Hashimoto Takashi, Le Bitoux Marie-Aude, Haftek Marek

机构信息

Department of Dermatology, Hôpital Edouard Herriot, Université Claude Bernard, EA3732/CNRS, Lyon 1, France.

出版信息

Eur J Dermatol. 2005 Mar-Apr;15(2):80-4.

Abstract

Desmosomes are the most prominent and mechanically important epidermal intercellular junctions. Transmembrane proteins of desmosomes, desmogleins and desmocollins, are responsible for extracellular binding and, thus, are important for interkeratinocyte cohesion. We show here, using three different approaches, that the extracellular "cores" of epidermal desmosomes contain a highly glycosylated antigen, different from desmosomal cadherins. This protein, recognised by KM48 monoclonal antibody, is likely to be involved in the processes of keratinocyte differentiation, desmosome turnover and epidermal cohesion.

摘要

桥粒是最显著且在机械方面最重要的表皮细胞间连接。桥粒的跨膜蛋白,桥粒芯糖蛋白和桥粒胶蛋白,负责细胞外结合,因此对于角质形成细胞间的黏附很重要。我们在此使用三种不同方法表明,表皮桥粒的细胞外“核心”含有一种高度糖基化的抗原,不同于桥粒钙黏蛋白。这种被KM48单克隆抗体识别的蛋白质可能参与角质形成细胞分化、桥粒更新和表皮黏附过程。

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