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Expression and localization of CHODL ΔE /CHODL fΔE , the soluble isoform of chondrolectin
Author(s) -
Claessens An,
Vijver Koen,
Bockstaele Dirk R.,
Wauters Jan,
Berneman Zwi N.,
Marck Eric,
Merregaert Joseph
Publication year - 2007
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2007.05.014
Subject(s) - gene isoform , transmembrane protein , biology , endoplasmic reticulum , transmembrane domain , golgi apparatus , microbiology and biotechnology , alternative splicing , gene , biochemistry , receptor
The C‐type lectin family is a group of animal proteins which can be distinguished from other lectins by the presence of a Ca 2+ ‐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, CHODL f ) and soluble proteins (CHODL ΔE , CHODL fΔE ) 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 ( CHODL f , CHODL ΔE and CHODL fΔE ) are differentially expressed in T lymphocytes. The transmembrane‐containing isoform CHODL f is localized in the ER—Golgi apparatus. CHODL ΔE and CHODL fΔE are devoid of the transmembrane domain and terminate in QDEL, an ER retention signal. In this paper we have investigated the expression of the CHODL ΔE /CHODL fΔE 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.