6533b826fe1ef96bd1283c43
RESEARCH PRODUCT
Kininogen binding protein p33/gC1qR is localized in the vesicular fraction of endothelial cells
Werner Müller-esterlJürgen Dediosubject
Kininogen bindingp33Kininogen binding proteinCellBiophysicsComplementFluorescent Antibody TechniqueBiologyBiochemistryUmbilical veinMitochondrial ProteinsStructural BiologyGeneticsmedicineHumansMolecular BiologyCells CulturedMembrane GlycoproteinsImmune SeraCell BiologyKininFlow CytometryKininFluorescenceReceptors ComplementCell biologyEndothelial stem cellSpecific antibodyHyaluronan Receptorsmedicine.anatomical_structuregC1qREndothelium VascularCarrier ProteinsImmunostainingdescription
AbstractThe 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1996-12-16 | FEBS Letters |