Gal-1 is encoded by the LSGALS1 gene 在chromosome 22q12的位置上
Gene fuction
Baldini et al. (1993) stated that the mouse beta-galactoside-binding protein is an autocrine regulator of cell proliferation with a role in the maintenance of G0 and in the control of G2 traverse.
Gene fuctionBaldini et al. (1993) stated that the mouse beta-galactoside-binding protein is an autocrine regulator of cell proliferation with a role in the maintenance of G0 and in the control of G2 traverse.
Nipah virus (NiV) is an emerging pathogen that causes severe, often fatal, febrile encephalitis. Levroney et al. (2005) examined the effect of GAL1 on cell fusion mediated by the heavily glycosylated fusion (F) and attachment (G) proteins of NiV. Immunoblot analysis showed that both proteins bound GAL1. NiV envelope-mediated cell-cell fusion was blocked by dimeric GAL1, but not by a monomeric GAL1 mutant, in a paramyxovirus-specific manner. GAL1 binding occurred at specific virus N-glycans and caused aberrant oligomerization of NiV-F and NiV-G, suggesting a mechanism for fusion inhibition. Levroney et al. (2005) proposed that GAL1-mediated production of IL6 (147620) may assist in augmenting the innate immune response against NiV.
A number of distinct interactions influence binding of human immunodeficiency virus (HIV)-1 (see 609423) to the host cell surface. Ouellet et al. (2005) challenged cells and lymphoid tissue explants with HIV-1 and found that recombinant GAL1, but not GAL3 (LGALS3; 153619), increased virus production in a dose-dependent manner by facilitating and accelerating attachment of HIV-1 to the cell surface, even in the presence of various HIV-1 absorption and binding blockers (e.g., anti-CD4 (186940)). Inhibition of HIV-1 fusion using the T-20 peptide (enfuvirtide) was not affected by the presence of GAL1. Because GAL1 is highly expressed in HIV-1 reservoir organs, such as thymus and lymph nodes, and is secreted by activated CD8 (see 186910)-positive T cells, which are present in high levels in HIV-1-infected patients, Ouellet et al. (2005) proposed that GAL1 may be a significant factor that augments the efficiency of the HIV-1 infection process.
Using a yeast 2-hybrid assay, Thijssen et al. (2006) found that GAL1 is the receptor for anginex, an antiangiogenic drug. GAL1 was overexpressed in endothelial cells of different human tumors, and its knockdown in cultured human endothelial cells inhibited cell proliferation and migration.
GenBank: NM_002305
Protein: EAW60178
Reference:
沒有留言:
張貼留言