TY - JOUR
T1 - Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells
AU - Levinovitz, A.
AU - Muhlhoff, J.
AU - Isenmann, S.
AU - Vestweber, D.
N1 - Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1993
Y1 - 1993
N2 - E-selectin is an inducible endothelial cell adhesion molecule for neutrophils which functions as a Ca2+-dependent lectin. Using a recombinant, antibody-like form of mouse E-selectin, we have searched for glycoprotein ligands on mouse neutrophils and the neutrophil progenitor cell line 32D cl 3. We have identified a 150-kD glycoprotein as the only protein which could be affinity-isolated with soluble E-selectin from [35S]methionine/[35S]cysteine-labeled 32D cl 3 cells. Binding of this protein was strictly Ca2+-dependent, was blocked by a cell adhesion- blocking mAb against mouse E-selectin, and required the presence of sialic acid on the 150-kD ligand. This glycoprotein was also affinity-isolated from mature neutrophils, in addition to a minor component at 250 kD, but could not be isolated from several other non-myeloid cell lines. The 150-kD glycoprotein was the only protein from 32D cl 3 cells, which was detectable by silverstaining after a one-step affinity-isolation.
AB - E-selectin is an inducible endothelial cell adhesion molecule for neutrophils which functions as a Ca2+-dependent lectin. Using a recombinant, antibody-like form of mouse E-selectin, we have searched for glycoprotein ligands on mouse neutrophils and the neutrophil progenitor cell line 32D cl 3. We have identified a 150-kD glycoprotein as the only protein which could be affinity-isolated with soluble E-selectin from [35S]methionine/[35S]cysteine-labeled 32D cl 3 cells. Binding of this protein was strictly Ca2+-dependent, was blocked by a cell adhesion- blocking mAb against mouse E-selectin, and required the presence of sialic acid on the 150-kD ligand. This glycoprotein was also affinity-isolated from mature neutrophils, in addition to a minor component at 250 kD, but could not be isolated from several other non-myeloid cell lines. The 150-kD glycoprotein was the only protein from 32D cl 3 cells, which was detectable by silverstaining after a one-step affinity-isolation.
UR - http://www.scopus.com/inward/record.url?scp=0027483361&partnerID=8YFLogxK
U2 - 10.1083/jcb.121.2.449
DO - 10.1083/jcb.121.2.449
M3 - Article
C2 - 7682218
AN - SCOPUS:0027483361
SN - 0021-9525
VL - 121
SP - 449
EP - 459
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 2
ER -