Galectin-7

Gene map locus 19q13.2

GENE FUNCTION
Cao et al. (2003) reported the role of the carbohydrate-binding protein, galectin-7, in reepithelialization of corneal wounds. They found that expression of galectin-7 was markedly upregulated in corneal epithelium after injury and that exogenous galectin-7 stimulated reepithelialization of corneal wounds. The stimulatory effect of galectin-7 on corneal epithelial wound closure was specifically inhibited by beta-lactose, a competing sugar, but unaffected by sucrose, an irrelevant disaccharide.

GenBank: NM_002307

Protein: EAW56818

Reference:
http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600615

Galectin-4

Gene map locus 19q13.2

Huflejt et al. (1997) found that LGALS4 is expressed as a 38-kD protein in the human colon adenocarcinoma T84 cell line.In confluent T84 cells, LGALS4 is mainly cytosolic and is concentrated at the basal membrane. In subconfluent T84 cells, it is found in attachment sites of newly seeded cells and is concentrated at the leading edge of lamellipodia. Based on the localization of LGALS4 and the ability of immobilized recombinant rat Lgals4 to enhance adhesion of T84 cells, Huflejt et al. (1997) suggested that LGALS4 plays a role in cell adhesion.

GenBank: NM_006149

Protein : EAW56820

Reference:
http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602518

Galectin-3

Gene map locus 14q21-q22

Gene function
Galectin-3 is expressed in various tissues and organs, but is significantly absent in normal hepatocytes. However, evaluation of patient liver biopsies for galectin-3 expression revealed that hepatocellular carcinoma (HCC) frequently expressed significant levels of this lectin; 76% were immunohistochemically positive. Further investigations showed that galectin-3 expression in HCC is independent of whether the patient had prior hepatitis B virus infection (Hsu et al., 1999). Hsu et al. (1999) suggested that deregulated expression of galectin-3 can result in tumor transformation and invasiveness, or confer propensity for tumor cell survival.
In the thyroid, expression of galectin-3 protein had been described in differentiated follicular cancer, suggesting that the immunohistochemical study of galectin-3 may be a potential marker of malignancy in thyroid neoplasms. Martins et al. (2002) analyzed galectin-3 protein and mRNA expression in thyroid tissues from 87 patients with histomorphologic diagnosis of multinodular goiter (MNG), follicular adenoma, follicular carcinoma, papillary carcinoma, and 5 normal tissues.
Yoshimura et al. (2003) found increased expression of the LGALS3 gene in human nonsmall cell lung cancer, and suggested that it may play a role in the process of metastasis in this malignancy but not in small cell lung cancer. They considered that LGALS3 may be a phenotypic marker that excludes small cell lung cancer and a novel target molecule in therapy of nonsmall cell lung cancer.
Ohshima et al. (2003) found that galectin-3 mRNA and protein are expressed throughout synovial tissue in rheumatoid arthritis (RA; 180300) and that both galectin-3 and its binding protein are found at sites of joint destruction. In addition, levels of galectin-3 in serum and synovial fluid as well as levels of its binding protein in synovial fluid were significantly elevated in RA compared to osteoarthritis and healthy controls (p less than 0.001).
Henderson et al. (2006) found that galectin-3 was upregulated in established human fibrotic liver disease. In experimental hepatic fibrosis in rats, galectin-3 upregulation was associated with induction and resolution of fibrosis.

GenBank: NM_002306

Protein: EAW80660.

Reference:
http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=153619

Galectin-2

Gal-2 is encoded by the LSGALS1 gene and LGALS2在 chromosome 22q13.1 上

Gene fuction
Ozaki et al. (2004) demonstrated that galectin-2 binds to lymphotoxin-alpha (LTA; 153440).

GenBank: NM_006498

Protein: EAW60167.

Reference:

http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=150571

Galectin-1

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:

http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=150570