Claessens An, Van de Vijver Koen, Van Bockstaele Dirk R, Wauters Jan, Berneman Zwi N, Van Marck Eric, Merregaert Joseph
Laboratory of Molecular Biotechnology, Department of Biomedical Sciences, Faculty of Medicine, University of Antwerp, Universiteitsplein 1, B-2610 Wilrijk, and Antwerp University Hospital, Edegem, Belgium.
Cell Biol Int. 2007 Nov;31(11):1323-30. doi: 10.1016/j.cellbi.2007.05.014. Epub 2007 May 26.
The C-type lectin family is a group of animal proteins which can be distinguished from other lectins by the presence of a Ca2+-dependent carbohydrate recognition domain (CRD) in their protein sequence. They are classified into 17 groups according to their domain architecture and have a wide variety of functions. The human chondrolectin gene encodes transmembrane (CHODL, CHODLf) and soluble proteins (CHODLDeltaE, CHODLfDeltaE) belonging to the family of C-type lectins because of the presence of one CRD domain in their N-terminal region. The CHODL splice variants (CHODLf, CHODLDeltaE and CHODLfDeltaE) are differentially expressed in T lymphocytes. The transmembrane-containing isoform CHODLf is localized in the ER-Golgi apparatus. CHODLDeltaE and CHODLfDeltaE are devoid of the transmembrane domain and terminate in QDEL, an ER retention signal. In this paper we have investigated the expression of the CHODLDeltaE/CHODLfDeltaE protein. This variant localizes in the late endoplasmic reticulum. We detected the protein in spleen and tonsils in a small population of lymphocytes. Moreover, the isoform seems to be differentially expressed in thymocytes and lymphocytes suggesting an important biological function during T cell development.
