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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/08/19 14:26:29」(JST)

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

Gene and protein[edit source | edit]

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[edit source | edit]

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[edit source | edit]

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[edit source | edit]

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

References[edit source | edit]

^ 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.
^ Outenreath, R.L.; Jones, A.L. (1992). "Influence of an endogenous lectin substrate on cultured dorsal root ganglion cells". J. Neurocytol 21: 788–795.
^ 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.
^ "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.

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English Journal

The Leukocyte Activation Receptor CD69 Controls T Cell Differentiation through Its Interaction with Galectin-1.

de la Fuente H1, Cruz-Adalia A2, Martinez Del Hoyo G3, Cibrián-Vera D2, Bonay P4, Pérez-Hernández D5, Vázquez J5, Navarro P6, Gutierrez-Gallego R7, Ramirez-Huesca M3, Martín P3, Sánchez-Madrid F8.
Molecular and cellular biology.Mol Cell Biol.2014 Jul 1;34(13):2479-87. doi: 10.1128/MCB.00348-14. Epub 2014 Apr 21.
CD69 is involved in immune cell homeostasis, regulating the T cell-mediated immune response through the control of Th17 cell differentiation. However, natural ligands for CD69 have not yet been described. Using recombinant fusion proteins containing the extracellular domain of CD69, we have detected
PMID 24752896

Galectin fingerprinting in naso-sinusal diseases.

Duray A1, De Maesschalck T2, Decaestecker C3, Remmelink M4, Chantrain G2, Neiveyans J1, Horoi M2, Leroy X5, Gabius HJ6, Saussez S1.
Oncology reports.Oncol Rep.2014 Jul;32(1):23-32. doi: 10.3892/or.2014.3213. Epub 2014 May 23.
Galectins, a family of endogenous lectins, are multifunctional effectors that act at various sites and can be used in immunohistochemical localization studies of diseased states. Since they form a potentially cooperative and antagonistic network, we tested the hypothesis that histopathological finge
PMID 24859692

Expression, purification and characterization of galectin-1 in Escherichia coli.

Shu Z1, Li J1, Mu N1, Gao Y1, Huang T1, Zhang Y1, Wang Z1, Li M1, Hao Q1, Li W1, He L2, Zhang C1, Zhang W1, Xue X3, Zhang Y4.
Protein expression and purification.Protein Expr Purif.2014 Jul;99:58-63. doi: 10.1016/j.pep.2014.03.013. Epub 2014 Apr 6.
As a member of beta-galactoside-binding proteins family, Galectin-1 (Gal-1) contains a single carbohydrate recognition domain, by means of which it can bind glycans both as a monomer and as a homodimer. Gal-1 is implicated in modulating cell-cell and cell-matrix interactions and may act as an autocr
PMID 24718258

Japanese Journal

Crosslinking of Cys-Mutated Human Galectin-1 to the Model Glycoprotein Ligands Asialofetuin and Laminin by Using a Photoactivatable Bifunctional Reagent

Tamura Mayumi,Watanabe Tomoe,Igarashi Takanori [他]
Biological & pharmaceutical bulletin 37(5), 877-882, 2014-05
NAID 40020048932

Galectin-3欠損が高脂肪食による肥満症を促進し,脂肪組織および膵島の炎症を増幅する

Pejnovic Nada N.,Pantic Jelena M.,Jovanovic Ivan P. [他]
Diabetes : a journal of the American Diabetes Association 7(1), 14-24, 2013-12
NAID 40019933775

Denaturation of bovine spleen galectin-1 in guanidine hydrochloride and fluoroalcohols : structural characterization and implications for protein folding

Mandal Pritha,Molla Anisur R.,Mandal Dipak K.
The journal of biochemistry 154(6), 531-540, 2013-12
NAID 40019909528

Related Pictures

★リンクテーブル★

リンク元	「ガレクチン1」「ガレクチン-1」
関連記事	「galectin」

「ガレクチン1」

Lectin, galactoside-binding, soluble, 1
	; PDB rendering based on 1gzw.
Available structures
PDB	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
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