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Human LGALS1 Protein expressed in Escherichia coli (E. coli) - ABIN2002512
Nishi, Abe, Iwaki, Yoshida, Itoh, Shoji, Kamitori, Hirabayashi, Nakamura: Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1. in Glycobiology 2008
Show all 4 Pubmed References
Results show that Galectin-1 teams up with Galectin-3 (zeige LGALS3 Proteine) to induce inflammatory/pro-degradative gene signature in human chondrocytes affecting the progression of osteoarthritis. Also, Galectin-3 (zeige LGALS3 Proteine) was found to induce a pro-degradative-inflammatory gene signature in human chondrocytes, teaming up with Galectin-1 in the pathogenesis of osteoarthritis.
We also found a subset of prostate cancer patient-derived xenografts and prostate cancer patient samples with mild HO-1 (zeige HMOX1 Proteine) and low Gal-1 expression levels. These results highlight a novel function of a human-used drug as a means of boosting the antitumor response
Gal-1, Gal-3 (zeige LGALS3 Proteine) and Gal-9 (zeige LGALS9 Proteine) galectin expression was higher in the myenteric plexus ganglia of chagasic patients
Results have shown that Gal-1 in the farnesyl-bound form acquires the ability to form self-clusters, and the galactoside-binding pocket of Gal-1 in the FTS (zeige AKTIP Proteine)-bound form plays an important role in self-cluster formation.
Our findings support the introduction of galectin-1 as a reliable diagnostic marker for thyroid carcinomas. Its involvement in cell proliferation, migration, invasion and tumor growth also intimate functional involvement of galectin-1 in the progression of thyroid carcinoma, suggesting its potential as a therapeutic target
This study showed that obese children had significantly higher galectin-1 levels in proportion to fat mass in obese cases than those in healthy children, which may be interpreted as a compensatory increase in an attempt to improve glucose metabolism.
We further demonstrated using the NMR-based hydrogen-deuterium exchange (HDX) that lactose binding increases the exchange rates of residues located on the opposite side of the ligand-binding pocket for hGal1 and hGal8(NTD), indicative of allostery. Additionally, lactose binding induces significant stabilisation of hGal8(CTD) across the entire domain
our findings indicate that galectin-1 plays a pivotal role in the regulation of key processes in cancer cells, such as migration, invasion, and chemoresistance, by modulating FAK (zeige PTK2 Proteine) and ERK (zeige EPHB2 Proteine) signaling and survivin (zeige BIRC5 Proteine) level.
Gal-3 (zeige LGALS3 Proteine) staining in the nucleus could be a new positive prognosticator for ovarian cancer.
Gal-1 may offer an additional therapeutic target linking anti-angiogenesis and immune checkpoint blockade.
Gal-1 may serve as an adhesion molecule (zeige NCAM1 Proteine) to interact with both cells and laminins
Gal-1 is expressed in a wide range of porcine tissues, including striated (zeige NSDHL Proteine) muscle, liver, lung, brain, kidney, spleen, and intestine
LGALS1 was found widely expressed in all tissues and transient transfection indicated that galectin-1 locates both in cytoplasm and nucleus.
Data suggest that galectin-1 and VEGFR-2 (zeige KDR Proteine) are expressed at mid-luteal stages in luteal cells of corpus luteum; galectin-1 binds directly to asparagine-linked glycans (N-glycans) on VEGFR-2 (zeige KDR Proteine) in luteal cells.
The relative abundance of PIBF (zeige PIBF1 Proteine), LGALS1, LGALS3 (zeige LGALS2 Proteine), LGALS3BP (zeige LGALS3BP Proteine), and LGALS9 (zeige LGALS9 Proteine) mRNA would display a differential expression pattern in the endometrium.
The binding affinity and specificity of galectin-1 for eight different beta-galactosyl terminal disaccharides was studied using molecular-dynamics simulations.
This work identified Gal1, an endogenous immune regulatory lectin, as an integral component of the secretory granule machinery and unveil the unexpected function of this lectin in regulating CTL killing activity.
The results of this study showed that development of spinal axons as well as the locomotor abilities observed in adult mice are independent of Gal-1.
GAL-1 also enhanced the generation of neural crest cells from explanted neural tubes
this present study indicated that Gal-1 secreted from MSCs upregulated expression of Gal-1 and stimulated formation of tolerance immunophenotype on DCs, where the underlying mechanism was the regulation of the MAPK (zeige MAPK1 Proteine) signaling pathway in DCs, thereby inhibiting the function of DCs
markedly increased brain Gal-1 and S-nitrosylated Gal-1 both in scrapie-infected rodents and human prion (zeige PRNP Proteine) diseases.
Gal-1 can limit eosinophil recruitment to allergic airways and suppresses airway inflammation by inhibiting cell migration and promoting eosinophil apoptosis.
Gal1 protein is essential for efficient liver regeneration following partial hepatectomy through the regulation of liver inflammation, hepatic cell proliferation, and the control of lipid storage in the regenerating liver.
findings show that galectin-1 (Gal-1), an immunoregulatory lectin widely expressed in mucosal tissues, contributes to Y. enterocolitica pathogenicity by undermining protective antibacterial responses.
Gal-1 functions as an important regulator in RNV and offers a promising strategy for the treatment of RNV diseases, such as proliferative diabetic retinopathy and retinopathy of prematurity.
These findings demonstrate that galectin-1 is required for i.v. tolerance induction, likely via induction of tolerogenic DCs leading to enhanced development of Tr1 (zeige TXNRD1 Proteine) cells, Treg cells, and downregulation of proinflammatory responses.
Equine bone marrow mesenchymal stromal cells constitutively express high levels of galectin-1 mRNA relative to other articular cell types, suggesting a possible mechanism for their intra-articular immunomodulatory properties.
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. This gene product may act as an autocrine negative growth factor that regulates cell proliferation.
14 kDa laminin-binding protein
, 14 kDa lectin
, S-Lac lectin 1
, beta-galactoside-binding lectin L-14-I
, beta-galactoside-binding protein 14kDa
, galectin 1
, lactose-binding lectin 1
, putative MAPK-activating protein PM12
, lectin galactoside-binding soluble 1
, beta-galactoside-binding lectin
, RL 14.5
, lectin, galactose binding, soluble 1
, lectin, galactoside-binding, soluble, 1 (galectin 1)
, 14K beta-galactoside-binding lectin
, galectin CG-1B
, lectin, galactoside-binding, soluble, 1
, beta-galactoside binding protein
, Beta-galactoside-binding lectin L-14-I
, Lactose-binding lectin 1
, Lectin galactoside-binding soluble 1