Disease relevance of Lgals1

• Together with data on the heparin-binding lectin, revealing reduced expression to be associated with a positive lymph-node status in the breast cancer group, these results can be interpreted to reflect cell-type-dependent requirements of galectin ligand presentation during the metastatic cascade [1].
• Histopathological analysis of lymph-node-negative and -positive breast and colorectal carcinomas (n = 180 including 60 metastatic lesions) indicated a correlation of either increased galectin-1 binding and reduced galectin-3 expression or reduced binding of both galectins with the occurrence of lymph node lesions [1].
• Thus, the coordinate expression of galectin-1 and laminin in the embryonic nerve fibre layer suggests that these molecules support the adhesion and fasciculation of axons en route to their glomerular targets [2].
• Transcriptional regulation by butyrate of mouse galectin-1 gene in embryonal carcinoma cells [3].
• These results indicate that galectin-1 expression may be associated with the differentiation of KM12 cells and that several glycoproteins shown to be important in colon carcinoma adhesion and metastasis are capable of functioning as its endogenous ligands [4].

Psychiatry related information on Lgals1

• The results showed that the administration of oxidized galectin-1 improved the motor activity, delayed the onset of symptoms, and prolonged the survival of the galectin-1-treated mice [5].

High impact information on Lgals1

• Pre-treatment of wild-type T cells with lactose to compete for galectin binding produced a phenocopy of Mgat5-/- TCR clustering [6].
• Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis [7].
• Moreover, GAL-1-expressing fibroblasts and recombinant GAL-1 revealed a specific dose-dependent inhibitory effect in vitro in antigen-dependent interleukin 2 production to an A(q)-restricted, collagen type 2-specific T cell hybridoma clone [7].
• Thus, a correlation between the apoptotic properties of GAL-1 in vitro and its immunomodulatory properties in vivo supports its therapeutic potential in the treatment of T helper cell type 1-mediated autoimmune disorders [7].
• Galectin-1 suppresses experimental colitis in mice [8].

Chemical compound and disease context of Lgals1

• The endogenous beta-D-galactoside-binding lectins of UV-2237-IP3 fibrosarcoma cells consist of two polypeptides with molecular weights of 14,500 (L-14.5) and 34,000 (L-34) [9].
• Lectins purified by affinity chromatography on immobilized asialofetuin from extracts of mouse K-1735P melanoma cells appeared as two polypeptides [L-14.5 (Mr 14,500) and L-34 (Mr 34,000)] in one-dimensional polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate [10].
• A parallel association between differentiation and induction of galectin-1, and inhibition of galectin-3 by retinoic acid in mouse embryonal carcinoma F9 cells [11].
• Plasma levels of galectin-1 were higher in tumor-bearing severe combined immunodeficiency (SCID) mice breathing 10% O2 compared with mice breathing room air [12].
• In addition, galectin-1 caused a decreased expression of PKC associated with increased resistance to glutamate toxicity [13].

Biological context of Lgals1

• The structural gene for beta-galactoside-binding protein (Lgals-1), a cell growth regulatory molecule and cystostatic factor, is assigned to the E-region of mouse chromosome 15 and to the region q12-q13.1 of human chromosome 22 [14].
• Galectin-1beta, a natural monomeric form of galectin-1 lacking its six amino-terminal residues promotes axonal regeneration but not cell death [15].
• The L14 lectin is a 14 x 10(3) M(r) carbohydrate binding protein belonging to the family of S-type lectins [16].
• Expression of the L14 lectin during mouse embryogenesis suggests multiple roles during pre- and post-implantation development [17].
• Dimeric galectin-1 induces surface exposure of phosphatidylserine and phagocytic recognition of leukocytes without inducing apoptosis [18].

Anatomical context of Lgals1

• In the case of the galectin 1 gene (Lgals1), localised differential expression in the Sertoli cells can be traced back to neonatal and embryonic stages, making this the earliest known molecular marker of functional heterogeneity in mammalian testis cords [19].
• However, we show that galectin 5, a third member of this gene family, is also present in the blastocyst at the time of implantation [20].
• Galectin-1 was present in all tissue compartments of the uterus except the luminal and glandular epithelium [21].
• Differential cellular expression of galectin family mRNAs in the epithelial cells of the mouse digestive tract [22].
• This study revealed the cellular expression of galectin subtypes throughout the mouse digestive tract by in situ hybridization [22].

Associations of Lgals1 with chemical compounds

• The surrogate light chain/GAL1 association is a direct protein-protein interaction (K(a) = 2 x 10(6) M(-1)), and the NH(2) extra loop of lambda-like is the major binding element [23].
• A cDNA encoding L14, the lactose-binding, soluble lectin of relative molecular mass 14 x 10(3), has been isolated in a differential screen designed to identify genes that are regulated during the differentiation of murine embryonic stem cells in vitro [17].
• Galectin-1, a bivalent galactose-binding vertebrate lectin, is expressed in the developing rodent olfactory system [24].
• Affinity-purified human galectin-1 was found to bind to purified polylactosamine-containing glycoproteins and to detergent-solubilized cellular proteins electroblotted onto nitrocellulose membranes [4].
• Finally, galectin-1 is shown to negatively regulate B cell proliferation and tyrosine phosphorylation upon BCR stimulation [25].

Physical interactions of Lgals1

• Galectin-3 is a 30 kDa beta-galactoside binding protein that belongs to the galectin family of animal lectins [26].
• Galectin-1 is a beta-galactoside-binding protein with potent anti-inflammatory and immunoregulatory effects [27].

Regulatory relationships of Lgals1

• Between E16.5 and birth galectin-1 began to be expressed by olfactory nerve ensheathing cells in the lamina propria of the neuroepithelium and nerve fibre layer [2].
• These results suggest that the 5' proximal Sp1 site at -57 is crucial for the butyrate-induced expression of the gal-1, and the direct binding of SP1 to this Sp1 site may be involved in this induction [3].

Other interactions of Lgals1

• In the course of studying mouse colon mRNA for galectin-4, we detected a related mRNA that encodes a new galectin that also has two CRDs in a single peptide chain [28].
• Embryonic implantation in galectin 1/galectin 3 double mutant mice [20].
• Role of galectin-1 in the developing mouse olfactory system [24].
• Gal1(-/-) mice have a significantly reduced proportion of IB4-binding DRG neurons, an increased proportion of NF200-immunoreactive DRG neurons, increased depth of central terminals of IB4-binding and CGRP-immunoreactive axons in the dorsal horn, and a reduced number of Fos-positive second order neurons following thermal (cold or hot) stimulation [29].
• While there is no difference in the total number of axons in the dorsal root of Gal1(-/-) mice, there are an increased number of myelinated axons, suggesting that in the absence of Gal1, neurons that are normally destined to become IB4-binding instead become NF200-expressing [29].

Analytical, diagnostic and therapeutic context of Lgals1

• In the present study, cellular expression of galectin subtypes in the urinary system of adult mice was examined by in situ hybridization and immunohistochemistry [30].
• Endogenous neuronal galectin-1 expression has recently been demonstrated to increase after axotomy [31].
• Treatment of these cells with sodium butyrate, an established differentiation-inducing agent for colon carcinoma cells, resulted in the induction of galectin-1, which was detected by immunoblotting as well as by affinity chromatography [4].
• Butyrate-induced galectin-1 was detected on the cell surface by immunoprecipitation from radioiodinated cell surface proteins as well as by indirect immunofluorescence labeling [4].
• The role of galectin-1, -3 and -8 in tumor astrocyte migration was quantitatively determined in vitro by means of computer-assisted phase-contrast videomicroscopy [32].

References