Ero1α is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of αIIbβ3
M Swiatkowska, G Padula, L Michalec… - Journal of biological …, 2010 - ASBMB
Recent evidence supports a role of protein-disulfide isomerase (PDI) in redox-controlled
remodeling of the exofacial domains of α IIb β 3 in blood platelets. The aim of this study was
to explain whether Ero1α can be responsible for extracellular reoxidation of the PDI active
site. We showed that Ero1α can be found on platelets and is rapidly recruited to the cell
surface in response to platelet agonists. It is physically associated with PDI and α IIb β 3, as
suggested by colocalization analysis in confocal microscopy and confirmed by …
remodeling of the exofacial domains of α IIb β 3 in blood platelets. The aim of this study was
to explain whether Ero1α can be responsible for extracellular reoxidation of the PDI active
site. We showed that Ero1α can be found on platelets and is rapidly recruited to the cell
surface in response to platelet agonists. It is physically associated with PDI and α IIb β 3, as
suggested by colocalization analysis in confocal microscopy and confirmed by …
