Identification of human endomucin‐1 and ‐2 as membrane‐bound O‐sialoglycoproteins with anti‐adhesive activity 1

FEBS Letters

Haraguchi, Tokuko²  Nakamura, Tomoyuki³  Tashiro, Kei⁴  Kinoshita, Makoto¹  Noda, Makoto¹  Hiraoka, Yasushi²  Ihara, Masafumi¹ 

[1] Department of Molecular Oncology, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo, Kyoto 606-8501, Japan;Structural Biology Section, Kansai Advanced Research Center, Communications Research Laboratory, Iwaoka, Nishi-ku, Kobe 651-2401, Japan;Department of Medical Chemistry, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo, Kyoto 606-8501, Japan;Center for Molecular Biology and Genetics, Kyoto University, Yoshida Konoe, Sakyo, Kyoto 606-8501, Japan

关键词: Signal sequence trap;    Sialomucin;    Vascular endothelium;    Anti-adhesion;   

DOI  :  10.1016/S0014-5793(01)02520-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Using a signal sequence trap method and database search, we identified a series of human cDNAs encoding two structurally related type I membrane proteins of ∼25 kDa with multiple glycosylation motifs. These genes, termed endomucin-1/-2, are expressed in several human tissues including heart, kidney, and lung. Exogenously expressed human endomucin-1/-2 proteins were modified into 80–120 kDa glycoproteins, which were susceptible to O-sialoglycoprotein endopeptidase digestion. Transient overexpression of endomucin-1/-2 reduced the number of adhesion plaques and reduced cell attachment to the substrate. This phenotype was suppressed by laminin or the protein kinase inhibitor staurosporine. Our findings suggest that human endomucin-1/-2 negatively regulate cell adhesion to the extracellular matrix.

【 授权许可】

Unknown