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Publication : Genomic characterization, localization, and functional expression of FGL2, the human gene encoding fibroleukin: a novel human procoagulant.

First Author  Yuwaraj S Year  2001
Journal  Genomics Volume  71
Issue  3 Pages  330-8
PubMed ID  11170750 Mgi Jnum  J:67726
Mgi Id  MGI:1931337 Doi  10.1006/geno.2000.6444
Citation  Yuwaraj S, et al. (2001) Genomic characterization, localization, and functional expression of fgl2, the human gene encoding fibroleukin: a novel human procoagulant. Genomics 71(3):330-8
abstractText  For diseases in which thrombosis plays a pivotal role, such as virus-induced fulminant hepatitis, fetal loss syndrome, and xenograft rejection, the major procoagulant has remained elusive. Here we describe the isolation and functional expression of a distinct human prothrombinase, termed FGL2. The murine fgl2 gene product has been implicated in the pathophysiology of murine fulminant hepatitis. The predicted ORF corresponds to a 439-amino-acid type II integral membrane protein that contains a carboxy-terminal Fibrinogen-related domain. Functional analysis showed that FGL2-encoded protein is indeed a prothrombinase. This enzyme is a serine protease and directly cleaves prothrombin to thrombin. The FGL2 gene is a single-copy gene in the haploid human genome and has two exons separated by a 2195-bp intron expressing two mRNA transcripts of 1.5 and 5.0 kb. The 5'-flanking region contains putative cis-elements including a TATA box, an AP1 site, CEBP sites, Sp1 site, and Ets binding domains. By both radiation hybrid analyses and fluorescence in situ hybridization, human FGL2 was localized to 7q11.23. Copyright 2001 Academic Press.
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