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Identification of a novel secretory leukocyte protease inhibitor-binding protein involved in membrane phospholipid movement.

作者信息

Tseng C C, Tseng C P

机构信息

Divisions of Basic Sciences and of Restorative and Prosthodontic Sciences, New York University College of Dentistry, New York, NY 10010, USA.

出版信息

FEBS Lett. 2000 Jun 23;475(3):232-6. doi: 10.1016/s0014-5793(00)01700-2.

DOI:10.1016/s0014-5793(00)01700-2
PMID:10869562
Abstract

Previous studies have suggested that human salivary secretory leukocyte protease inhibitor (SLPI) inhibits HIV-1 by binding to a host cell surface protein of unknown identity. Using the yeast two-hybrid assay, we identified a gene sequence encoding a novel SLPI-binding protein (SLPI-BP). The 1.5-kb cDNA encodes a 318-amino acid protein with a predicted transmembrane segment near the C-terminus. Sequence analysis revealed that SLPI-BP is the human scramblase protein that is involved in the movement of membrane phospholipids. Co-expression of SLPI and SLPI-BP followed by an S-protein pulldown assay confirmed the specific interaction between these two proteins. Our data represent the first report for the identity of SLPI-BP.

摘要

相似文献

1
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2
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Serine leucocyte proteinase inhibitor-treated monocyte inhibits human CD4(+) lymphocyte proliferation.
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Immunology. 2011 Aug;133(4):434-41. doi: 10.1111/j.1365-2567.2011.03451.x. Epub 2011 May 17.
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PLoS One. 2009;4(3):e5006. doi: 10.1371/journal.pone.0005006. Epub 2009 Mar 31.
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