Molecular characterization of two novel isoforms and a soluble form of mouse CLEC-2.
CLEC-2 was first identified by sequence similarity to C-type lectin-like molecules with immune functions. Recently, human CLEC-2 has been reported as a receptor for the platelet-aggregating snake venom toxin rhodocytin and the endogenous sialoglycoprotein podoplanin. It has also been reported to facilitate the capture of HIV-1. However, investigation of mouse CLEC-2 (mCLEC-2) has little progressed after its identification. In this study, we identified two novel splicing variants of mCLEC-2 derived from omission of exon 2 and 2/4, respectively. These two variants had different expression profiles and subcellular localization from full-length mCLEC-2. Moreover, we observed that full-length mCLEC-2 could be cleaved probably by proteases sensitive to aprotinin and PMSF into a soluble form that partially existed as a disulfide-linked homodimer. The results presented here represent a further advancement toward the understanding of mCLEC-2.
Xie
Jianhui
J
Gene Research Center, Institutes of Biomedical Science, Box 103, Shanghai 200032, PR China.
Wu
Tao
T
Guo
Liang
L
Ruan
Yuanyuan
Y
Zhou
Lei
L
Zhu
Haiyan
H
Yun
Xiaojing
X
Hong
Yi
Y
Jiang
Jianhai
J
Wen
Yumei
Y
Gu
Jianxin
J
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D007611:Aprotinin / Q000494:pharmacology; D002460:Cell Line; D005091:Exons; D037181:Lectins, C-Type / Q000032:analysis / Q000235:genetics* / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D041681:NIH 3T3 Cells; D010447:Peptide Hydrolases / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D020033:Protein Isoforms / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D014105:Tosyl Compounds / Q000494:pharmacology
C529518:CLEC-2 protein, mouse; D037181:Lectins, C-Type; D011480:Protease Inhibitors; D020033:Protein Isoforms; D014105:Tosyl Compounds; C003614:4-toluenesulfonyl fluoride; D007611:Aprotinin; D010447:Peptide Hydrolases