High impact information on Fgl1

• The fibrinogen-like globe within tenascin-C or -R enables both proteins to bind to CALEB [1].
• In contrast, the differential effects of these ligands on endothelial Tie2 phosphorylation is mediated by their fibrinogen-like domains [2].
• Angiopoietin-1 and -2 coiled coil domains mediate distinct homo-oligomerization patterns, but fibrinogen-like domains mediate ligand activity [2].
• Association of mouse fibrinogen-like protein with murine hepatitis virus-induced prothrombinase activity [3].
• Sequence of a human transcript expressed in T-lymphocytes and encoding a fibrinogen-like protein [4].

Biological context of Fgl1

• Ficolins are a group of proteins mainly consisting of collagen-like and fibrinogen-like domains and are thought to play a role in innate immunity via their carbohydrate-binding activities [5].

Anatomical context of Fgl1

• The FIBLP (fibrinogen-like protein) gene is a T-lymphocyte-specific gene that is expressed in mouse cytotoxic T lymphocytes but not in helper T lymphocytes or B lymphocytes [6].
• Analysis of mRNA transcripts for mouse fibrinogen like protein (musfiblp), the MHV-3 specific prothrombinase, in macrophages which were incubated with MP prior to exposure to MHV-3 demonstrated significantly increased mRNA levels as compared to macrophages not incubated with MP prior to MHV-3 exposure [7].

Associations of Fgl1 with chemical compounds

• Tyrosine kinase inhibition precluded this increase and abrogated expression of the virus-induced procoagulant mouse fibrinogen-like protein (musfiblp) gene [8].

Other interactions of Fgl1

• The sequence identified this clone as representing part of a gene, musfiblp, that encodes a fibrinogen-like protein [3].

References