P-Selectin Glycoprotein Ligand-1 Forms Dimeric Interactions with E-Selectin but Monomeric Interactions with L-Selectin on Cell Surfaces

• Published in: PloS one Vol. 8; no. 2; p. e57202
• Main Authors: Zhang, Yan, Jiang, Ning, Zarnitsyna, Veronika I., Klopocki, Arkadiusz G., McEver, Rodger P., Zhu, Cheng
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 25.02.2013; Public Library of Science (PLoS)
• Subjects: Adhesion; Adhesive bonding; Analysis; Animals; Aorta; Binding; Biology; Biomedical engineering; Bond ratings; Bond strength; CD162 antigen; Cell adhesion & migration; Cell Membrane - metabolism; Cell surface; Chemical bonds; CHO Cells; Cricetinae; Cricetulus; Dimerization; E-selectin; E-Selectin - metabolism; Endothelial cells; Endothelium; Endothelium, Vascular - cytology; Endothelium, Vascular - metabolism; Epidermal growth factor; Frequency analysis; Glycoconjugates; Glycoproteins; Health aspects; Health sciences; Humans; L-selectin; L-Selectin - metabolism; Leukocytes; Leukocytes (neutrophilic); Ligands; Mechanical engineering; Medical research; Medicine; Membrane Glycoproteins - metabolism; Municipal bonds; Neutrophils; P-selectin; P-selectin glycoprotein ligand 1; Rodents; Selectins; Signaling; Two dimensional analysis; White blood cells; Atlanta Georgia; Georgia; United States > US; Oklahoma
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0057202

Interactions of selectins with cell surface glycoconjugates mediate the first step of the adhesion and signaling cascade that recruits circulating leukocytes to sites of infection or injury. P-selectin dimerizes on the surface of endothelial cells and forms dimeric bonds with P-selectin glycoprotein ligand-1 (PSGL-1), a homodimeric sialomucin on leukocytes. It is not known whether leukocyte L-selectin or endothelial cell E-selectin are monomeric or oligomeric. Here we used the micropipette technique to analyze two-dimensional binding of monomeric or dimeric L- and E-selectin with monomeric or dimeric PSGL-1. Adhesion frequency analysis demonstrated that E-selectin on human aortic endothelial cells supported dimeric interactions with dimeric PSGL-1 and monomeric interactions with monomeric PSGL-1. In contrast, L-selectin on human neutrophils supported monomeric interactions with dimeric or monomeric PSGL-1. Our work provides a new method to analyze oligomeric cross-junctional molecular binding at the interface of two interacting cells.