[HTML][HTML] The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its extracellular domain and triggers its intramembrane proteolysis by presenilin/γ …
A Mambole, D Baruch, P Nusbaum, S Bigot… - Journal of biological …, 2008 - ASBMB
The highly negatively charged membrane sialoglycoprotein leukosialin, CD43, is shed
during neutrophil activation. This is generally thought to enhance cell adhesion. We here
describe two novel consequences of this shedding, during neutrophil activation by phorbol
esters or by chemoattractants after TNF-α priming. CD43 proteolysis was investigated by
Western blotting, using a polyclonal antibody to CD43 intracellular domain. Our data
emphasize the importance of a juxtamembranous cleavage of about 50% of membrane …
during neutrophil activation. This is generally thought to enhance cell adhesion. We here
describe two novel consequences of this shedding, during neutrophil activation by phorbol
esters or by chemoattractants after TNF-α priming. CD43 proteolysis was investigated by
Western blotting, using a polyclonal antibody to CD43 intracellular domain. Our data
emphasize the importance of a juxtamembranous cleavage of about 50% of membrane …
