Disease relevance of Lgals1

• We found that the expression of galectin-1 and galectin-3 was significantly up-regulated in hepatic stellate cells (HSCs) both in the course of their transdifferentiation into myofibroblasts, a process of "self-activation," and in the fibrosis of liver tissues [1].
• Previous studies have shown that galectin-1 was expressed in fibroblasts of chronic pancreatitis and of desmoplastic reaction associated with pancreatic cancer [2].
• The reduced level of expression of glycoligands for galectin-1 and -3 in foreign-body giant multinucleate cells in contrast with the mononuclear macrophages suggests an inhibitory influence of macrophage fusion on the expression of galectin-reactive molecules [3].
• Intrathecal administration of anti-recombinant human galectin-1 antibody (anti-rhGAL-1 Ab) partially but significantly attenuated the upregulation of substance P receptor (SPR) in the spinal dorsal horn and the mechanical hypersensitivity induced by the peripheral nerve injury [4].
• Lactoside-binding lectins (galectins) with molecular weights of about 14.5 kDa (galectin-1) and 29-35 kDa (galectin-3) bind preferentially to polylactosaminoglycan-containing glycoconjugates and have been found on the surface of tumour cells and implicated in cell-cell and cell-extracellular matrix adhesion and metastasis [5].

Psychiatry related information on Lgals1

• Dex decreased galaptin activity and synthesis when administered daily during the "critical period" of alveolarization (postnatal days 3-13) described by Massaro and coworkers (J Clin Invest 76:1297-1305, 1985) [6].

High impact information on Lgals1

• PCTA-1 encodes a secreted protein of approximately 35 kDa that shares approximately 40% sequence homology with the N-amino terminal region of members of the S-type galactose-binding lectin (galectin) gene family [7].
• The distribution of two endogenous lactose-binding lectins, RL-14.5 and RL-29 (subunit Mrs of 14,500 and 29,000, respectively), was examined by immunoblotting and by immunocytochemistry in embryonic and postnatal rat DRG and spinal cord [8].
• RL-14.5 and RL-29 are present in overlapping, but not coincident, subsets of DRG neurons that project to the superficial dorsal horn of the spinal cord [8].
• Finally, when galectin-1 chloramphenicol acetyltransferase (CAT) promoter constructs were methylated in vitro by SssI methylase at every cytosine residue of the CpG doublets and transfected into mouse fibroblasts, the transcription of the CAT reporter gene was strongly inhibited [9].
• Southern blot analysis with HpaII and MspI endonucleases and sodium bisulfite analysis of genomic DNA from expressing and nonexpressing cell lines and cell hybrids showed a close correlation between gene activity and demethylation of the 5' region of the galectin-1 gene [9].

Chemical compound and disease context of Lgals1

• In contrast, Gal-1 failed to inhibit histamine-induced edema [10].
• Recombinant human galectin-1 (rhGAL-1) and a galectin-1 mutant in which all six cysteine residues were replaced by serine (CSGAL-1) were expressed in and purified from Escherichia coli for further analysis; the purified rhGAL-1 was subjected to oxidation, which induced the same pattern of disulfide linkages as that observed in rhGAL-1/COS1 [11].

Biological context of Lgals1

• A lactose-binding lectin from rat lung (RL-29) and a related lectin from Madin-Darby canine kidney (MDCK) cells have been analyzed with the primary goal of identifying post-translational modifications [12].
• Although galectin-1 and -3 did not induce the apoptosis in the T cells, they inhibited the accumulation of macrophages in the renal glomeruli [13].
• Regulated expression and ultrastructural localization of galectin-1, a proapoptotic beta-galactoside-binding lectin, during spermatogenesis in rat testis [14].
• In this study, galectin-3 was isolated from ovine placental cotyledons round the middle of the gestation period by lactose extraction followed by affinity chromatography on lactosyl-agarose, and separated from galectin-1 by size exclusion chromatography on a Superose 12 column [15].
• Cell-specific transcriptional regulation and reactivation of galectin-1 gene expression are controlled by DNA methylation of the promoter region [9].

Anatomical context of Lgals1

• CONCLUSIONS: Galectin-1 may be involved in adhesion of the photoreceptor and outer plexiform layers by interacting with glycoconjugates with beta-galactoside residues in the interphotoreceptor matrix and synaptic cleft matrix [16].
• Galectin-1 was found in various regions, including the retinal pigment epithelium, outer limiting membrane, and outer plexiform layer in bovine and rat retinas [16].
• High levels of RL-14.5 mRNA are present in primary sensory neurons and motoneurons in the spinal cord and brain stem [17].
• In subconfluent T84 cells, each galectin is distributed to specific domains of lamellipodia, with galectin-4 concentrated in the leading edge and galectin-3 more proximally [18].
• Shortly after irradiation-induced lung injury, when there is active proliferation of type II alveolar epithelial cells and re-epithelialization of alveolar basement membranes by type I cells, the total galectin concentration in the lung increased dramatically [19].

Associations of Lgals1 with chemical compounds

• Primary structure of the soluble lactose binding lectin L-29 from rat and dog and interaction of its non-collagenous proline-, glycine-, tyrosine-rich sequence with bacterial and tissue collagenase [12].
• Gal-1-dependent collagen synthesis was blocked by lactose but not by cellobiose, suggesting that gal-1 acts on PSCs through targeting beta-galactoside-containing glycoconjugates [20].
• Galectin-1 interacts with beta-1 subunit of integrin [21].
• The proliferation of Rat1a cells, but not cell death triggered by ER-DeltaFosB, was completely abolished by butyrolactone I, an inhibitor of cycline-dependent kinases, and was partly suppressed by antisense oligonucleotides against galectin-1, whose expression is induced after estrogen administration [22].
• Recombinant protein expressed in Chinese hamster ovary cells was purified from lysates by lactose and galactose affinity chromatography, proving the galactoside binding capacity of this new galectin [23].

Physical interactions of Lgals1

• Carbohydrates are believed to form a glycocode that mediates sorting out and fasciculation of primary olfactory axons through interactions with carbohydrate-binding proteins such as galectin-1 [24].

Regulatory relationships of Lgals1

• Finally, evidence is also provided by Western blot analysis, showing that Gal-1 inhibits Concanavalin A (Con A) induction of Bcl-2 protein [25].
• In the adult rat, galectin-1 was preferentially expressed by olfactory ensheathing cells in the nerve fibre layer of the ventromedial and lateral surfaces of the olfactory bulb [24].

Other interactions of Lgals1

• RESULTS: The cDNAs of bovine galectin-1, rat galectin-1, and rat galectin-3 were isolated [16].
• We report the expression of multiple members of the lactoseries binding galectin family in the primary olfactory system [26].
• Immunogold staining using the anti-galectin-1 antibody revealed the typical Sertoli cell profile in the seminiferous epithelium, mainly at stages X-II [14].
• Galectin-1 expression was assessed by Western blot analysis and immunocytochemical localization in testes obtained from rats aged from 9 to 60 days [14].
• Infusion of the brain-derived neurotrophic factor into the vicinity of the injured rubrospinal nucleus, which we have previously shown to increase the regenerative capacity of rubrospinal neurons, significantly increased galectin-1 mRNA compared with uninjured control levels [27].

Analytical, diagnostic and therapeutic context of Lgals1

• RNA blot analysis and in situ hybridization reveal a restricted pattern of expression of RL-14.5 mRNA within the rat nervous system [17].
• We found that 7 and 14 days after axotomy, galectin-1 mRNA increased in spinal motoneurons but decreased in rubrospinal neurons [27].
• Expression of galectin-1 was assessed by Western blot analysis, RT-PCR, and immunofluorescent staining [2].
• Immunoelectron microscopy confirmed distribution of galectin-1 in nuclei and cytoplasmic projections of Sertoli cells and on heads and tails of late spermatids and residual bodies [14].
• Direct binding of galectin-1 to beta1 integrin was detected by the immune precipitation of beta1 integrin after chemical cross-linking of 125I-labelled galectin-1 to the cell surface proteins [21].

References