Galectin-1

From Wikipedia, the free encyclopedia

Lectin, galactoside-binding, soluble, 1

PDB rendering based on 1gzw.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1GZW, 1W6M, 1W6N, 1W6O, 1W6P, 1W6Q, 2KM2, 2ZKN, 3OY8, 3OYW, 3T2T

Identifiers

Symbols

LGALS1; GAL1; GBP

External IDs

OMIM: 150570 MGI: 96777 HomoloGene: 7399 ChEMBL: 4915 GeneCards: LGALS1 Gene

Gene Ontology
Molecular function	• glycoprotein binding • signal transducer activity • galactoside binding • lactose binding • protein homodimerization activity • laminin binding
Cellular component	• proteinaceous extracellular matrix • extracellular space • intracellular • nucleus • cytoplasm • cell surface • extracellular matrix
Biological process	• plasma cell differentiation • apoptotic process • signal transduction • negative regulation of cell-substrate adhesion • negative regulation of neuron projection development • T cell costimulation • multicellular organismal response to stress • positive regulation of erythrocyte aggregation • response to drug • regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB cascade • myoblast differentiation • response to axon injury • cellular response to glucose stimulus • cellular response to organic cyclic compound
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 22:
38.07 – 38.08 Mb

Chr 15:
78.93 – 78.93 Mb

PubMed search

Galectin-1 is a protein that in humans is encoded by the LGALS1 gene.^[1]^[2]

Gene and protein

LGALS1 contains four exons. The galectin-1 protein is 135 amino acids in length and highly conserved across species. It can be found in the nucleus, the cytoplasm, the cell surface and in the extracellular space. Galectins in general lack a traditional signal sequence, but are still secreted across the plasma membrane. This non-traditional secretion requires a functional glycan binding site. Galectin 1 contains a single carbohydrate recognition domain through which it can bind glycans both as a monomer and as a homodimer. Dimers are non-covenantly bound and will spontaneously disassociate in low concentration.^[3] Galectin 1 does not bind glycans when oxidized.^[4] Having 6 cysteine residues, the oxidation state has a significant effect on the protein structure. The oxidized form is reported to have alternative functions not involving carbohydrate binding.^[5]

Function

The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. Galectin-1 may act as an autocrine negative growth factor that regulates cell proliferation.^[6]

Role in pregnancy

Galectin-1 is thought to play a role in the immunosuppression required for a successful pregnancy.^[7] Galectin-1 is expressed by the endometrial stromal cells throughout the menstrual cycle, however significantly increases during implantation. Galectin-1 induces the differentiation of Dendritic cells towards a phenotype which dampens T helper 1 cells and T helper 17 cells and dampens inflammation via interleukin-10 and interleukin-27.^[8]

Interactions

LGALS1 has been shown to interact with GEMIN4^[9] HRAS.^[10]

References

↑ Gitt MA, Barondes SH (February 1991). "Genomic sequence and organization of two members of a human lectin gene family". Biochemistry 30 (1): 82–9. doi:10.1021/bi00215a013. PMID 1988031.
↑ Gauthier L, Rossi B, Roux F, Termine E, Schiff C (October 2002). "Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering". Proc Natl Acad Sci U S A 99 (20): 13014–9. doi:10.1073/pnas.202323999. PMC 130578. PMID 12271131.
↑ Cho, M; Cummings, R.D. (1995). "Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. Physical and chemical characterization". JBC 270: 5198–5206. Cite uses deprecated parameters (help)
↑ Outenreath, R.L.; Jones, A.L. (1992). "Influence of an endogenous lectin substrate on cultured dorsal root ganglion cells". J. Neurocytol 21: 788–795. Cite uses deprecated parameters (help)
↑ Kadoya, T; Horie, H. (2005). "Structural and functional studies of galectin-1: a novel axonal regeneration-promoting activity for oxidized galectin-1.". Curr Drug Targets 6 (4): 375–83. Cite uses deprecated parameters (help)
↑ "Entrez Gene: LGALS1 lectin, galactoside-binding, soluble, 1 (galectin 1)".
↑ Munoz-Suano A, Hamilton AB, Betz AG (May 2011). "Gimme shelter: the immune system during pregnancy". Immunol. Rev. 241 (1): 20–38. doi:10.1111/j.1600-065X.2011.01002.x. PMID 21488887.
↑ Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA (September 2009). "Tolerogenic signals delivered by dendritic cells to T cells through a galectin-1-driven immunoregulatory circuit involving interleukin 27 and interleukin 10". Nat. Immunol. 10 (9): 981–91. doi:10.1038/ni.1772. PMID 19668220.
↑ Park JW, Voss PG, Grabski S, Wang JL, Patterson RJ (September 2001). "Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein". Nucleic Acids Res. 29 (17): 3595–602. doi:10.1093/nar/29.17.3595. PMC 55878. PMID 11522829.
↑ Paz A, Haklai R, Elad-Sfadia G, Ballan E, Kloog Y (November 2001). "Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation". Oncogene 20 (51): 7486–93. doi:10.1038/sj.onc.1204950. PMID 11709720.