Kininogen binding protein p33/gC1qR is localized in the vesicular fraction of endothelial cells

FEBS Letters

Dedio, Jürgen¹  Müller-Esterl, Werner¹ 

[1] Institute for Physiological Chemistry and Pathobiochemistry, Johannes Gutenberg University at Mainz, D-55099 Mainz, Germany

关键词: Kininogen binding protein;    p33;    gC1qR;    Kinin;    Complement;   

DOI  :  10.1016/S0014-5793(96)01339-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The endothelial protein p33/gC1qR is thought to mediate the assembly of components of the kinin-forming and complement-activating pathways on the surface of cardiovascular cells. FACS analysis of intact human umbilical vein endothelial cells using specific antibodies to p33 revealed a minor fluorescence on the cell surface whereas permeabilized cells showed a bright fluorescence indicative of an intracellular localization of p33. Immunostaining of fixed cells confirmed the predominant intracellular localization of p33. Fractionation studies demonstrated that the vesicular but not the membrane fraction of EA.hy926 cells is rich in p33. We conclude that externalization of p33 must precede its complex formation with target proteins on the endothelial cell surface.

【 授权许可】

Unknown