1. Academic Validation
  2. Characterization of a novel C-type lectin-like gene, LSECtin: demonstration of carbohydrate binding and expression in sinusoidal endothelial cells of liver and lymph node

Characterization of a novel C-type lectin-like gene, LSECtin: demonstration of carbohydrate binding and expression in sinusoidal endothelial cells of liver and lymph node

  • J Biol Chem. 2004 Apr 30;279(18):18748-58. doi: 10.1074/jbc.M311227200.
Wanli Liu 1 Li Tang Ge Zhang Handong Wei Yufang Cui Lihai Guo Zikuan Gou Xiaoxiao Chen Daifeng Jiang Yunping Zhu Gefei Kang Fuchu He
Affiliations

Affiliation

  • 1 Department of Genomics and Proteomics, Beijing Institute of Radiation Medicine, Chinese Human Genome Center at Beijing, 27 Taiping Road, Beijing 100850, People's Republic of China.
Abstract

A new C-type lectin-like gene encodes 293 Amino acids and maps to chromosome 19p13.3 adjacent to the previously described C-type lectin genes, CD23, dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN), and DC-SIGN-related protein (DC-SIGNR). The four genes form a tight cluster in an insert size of 105 kb and have analogous genomic structures. The new C-type lectin-like molecule, designated liver and lymph node sinusoidal endothelial cell C-type lectin (LSECtin), is a type II integral membrane protein of approximately 40 kDa in size with a single C-type lectin-like domain at the COOH terminus, closest in homology to DC-SIGNR, DC-SIGN, and CD23. LSECtin mRNA was only expressed in liver and lymph node among 15 human tissues tested, intriguingly neither expressed on hematopoietic cell lines nor on monocyte-derived dendritic cells (DCs). Moreover, LSECtin is expressed predominantly by sinusoidal endothelial cells of human liver and lymph node and co-expressed with DC-SIGNR. LSECtin binds to mannose, GlcNAc, and fucose in a Ca(2+)-dependent manner but not to galactose. Our results indicate that LSECtin is a novel member of a family of proteins comprising CD23, DC-SIGN, and DC-SIGNR and might function in vivo as a lectin receptor.

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