作者: Sivashankary Yuwaraj , JinWen Ding , Mingfeng Liu , Philip A. Marsden , Gary A. Levy
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摘要: Abstract 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 isolation functional expression of distinct human prothrombinase, termed FGL2. The murine fgl2 gene product been implicated pathophysiology hepatitis. predicted ORF corresponds to 439-amino-acid type II integral membrane protein that contains carboxy-terminal Fibrinogen-related domain. Functional analysis showed FGL2-encoded is indeed prothrombinase. This enzyme serine protease directly cleaves prothrombin thrombin. FGL2 single-copy haploid genome two exons separated by 2195-bp intron expressing mRNA transcripts 1.5 5.0 kb. 5′-flanking region putative cis-elements including TATA box, an AP1 site, CEBP sites, Sp1 Ets binding domains. By both radiation hybrid analyses fluorescence situ hybridization, was localized 7q11.23.