Anti‐adhesive property of P‐selectin glycoprotein ligand‐1 (PSGL‐1) due to steric hindrance effect |
| |
Authors: | Saori Umeki Ryoichi Suzuki Yasuo Ema Masayuki Shimojima Yorihiro Nishimura Masaru Okuda Takuya Mizuno |
| |
Institution: | 1. The United Graduate School of Veterinary Science, Yamaguchi University, Yamaguchi, Japan;2. Laboratory of Veterinary Internal Medicine, Joint Faculty of Veterinary Medicine, Yamaguchi University, 1677‐1 Yoshida, Yamaguchi 753‐8515, Japan;3. Laboratory of Veterinary Microbiology, Joint Faculty of Veterinary Medicine, Yamaguchi University, 1677‐1 Yoshida, Yamaguchi 753‐8515, Japan;4. Department of Virology II, National Institute of Infectious Diseases, Tokyo, Japan |
| |
Abstract: | P‐selectin glycoprotein ligand‐1 (PSGL‐1) is an adhesive molecule that is known to be a ligand for P‐selectin. An anti‐adhesive property of PSGL‐1 has not been previously reported. In this study, we show that PSGL‐1 expression is anti‐adhesive for adherent cells and we have elucidated the underlying mechanism. Overexpression of PSGL‐1 induced cell rounding and floating in HEK293T cells. Similar phenomena were demonstrated in other adherent cell lines with overexpression of PSGL‐1. PSGL‐1 overexpression inhibits access of antibodies to cell surface molecules such as integrins, HLA and CD25. Cells transfected with PSGL‐1 deletion mutants that lack a large part of the extracellular domain and chimeric construct expressing extracellular CD86 and intracellular PSGL‐1 only showed rounded morphology, but there are no floating cells. These results indicated that PSGL‐1 causes steric hindrance due to the extended structure of its extracellular domain that is highly O‐glycosylated, but intracellular domain also has some effect on cell rounding. This study implies that PSGL‐1 has Janus‐faced functions, being both adhesive and anti‐adhesive. J. Cell. Biochem. 114: 1271–1285, 2013. © 2013 Wiley Periodicals, Inc. |
| |
Keywords: | PSGL‐1 ANTI‐ADHESIVE INTEGRIN ECM |
|
|