Galectin-1 is a protein that in humans is encoded by the LGALS1 gene.[5][6]
Gene and protein
editLGALS1 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-covalently bound and will spontaneously disassociate in low concentration.[7] Galectin 1 does not bind glycans when oxidized.[8] 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.[9]
Function
editThe 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.[10] Galectin-1 expression in Hodgkin Lymphoma has also been shown to mediate immunosuppression of CD8+ T-cells.[11]
It has been linked to the inflammatory process in HIV individuals, and some research suggest that Gal-1 could be related to the HIV-1 latency.[12]
Role in pregnancy
editGalectin-1 is thought to play a role in creating immune tolerance in pregnancy.[13] 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.[14] It also plays a role in the formation and expression of HLA-G in the syncytium.[15]
Interactions
editSee also
editReferences
edit- ^ a b c GRCh38: Ensembl release 89: ENSG00000100097 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000068220 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Gitt MA, Barondes SH (January 1991). "Genomic sequence and organization of two members of a human lectin gene family". Biochemistry. 30 (1): 82–89. 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". Proceedings of the National Academy of Sciences of the United States of America. 99 (20): 13014–13019. Bibcode:2002PNAS...9913014G. doi:10.1073/pnas.202323999. PMC 130578. PMID 12271131.
- ^ Cho M, Cummings RD (March 1995). "Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization". The Journal of Biological Chemistry. 270 (10): 5198–5206. doi:10.1074/jbc.270.10.5198. PMID 7890630.
- ^ Outenreath RL, Jones AL (November 1992). "Influence of an endogenous lectin substrate on cultured dorsal root ganglion cells". Journal of Neurocytology. 21 (11): 788–795. doi:10.1007/bf01237904. PMID 1431997. S2CID 20883530.
- ^ Kadoya T, Horie H (June 2005). "Structural and functional studies of galectin-1: a novel axonal regeneration-promoting activity for oxidized galectin-1". Current Drug Targets. 6 (4): 375–383. doi:10.2174/1389450054022007. PMID 16026256.
- ^ "Entrez Gene: LGALS1 lectin, galactoside-binding, soluble, 1 (galectin 1)".
- ^ Gandhi MK, Moll G, Smith C, Dua U, Lambley E, Ramuz O, et al. (August 2007). "Galectin-1 mediated suppression of Epstein-Barr virus specific T-cell immunity in classic Hodgkin lymphoma". Blood. 110 (4): 1326–1329. doi:10.1182/blood-2007-01-066100. PMC 1939905. PMID 17438085.
- ^ Rubione J, Pérez PS, Czernikier A, Duette GA, Pereyra Gerber FP, Salido J, et al. (August 2022). "A Dynamic Interplay of Circulating Extracellular Vesicles and Galectin-1 Reprograms Viral Latency during HIV-1 Infection". mBio. 13 (4): e0061122. doi:10.1128/mbio.00611-22. PMC 9426495. PMID 35943163. S2CID 251407421.
- ^ Munoz-Suano A, Hamilton AB, Betz AG (May 2011). "Gimme shelter: the immune system during pregnancy". Immunological Reviews. 241 (1): 20–38. doi:10.1111/j.1600-065X.2011.01002.x. PMID 21488887. S2CID 46696092.
- ^ Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, et al. (September 2009). "Tolerogenic signals delivered by dendritic cells to T cells through a galectin-1-driven immunoregulatory circuit involving interleukin 27 and interleukin 10". Nature Immunology. 10 (9): 981–991. doi:10.1038/ni.1772. hdl:11336/78711. PMID 19668220. S2CID 24418718.
- ^ Comninos AN, Jayasena CN, Dhillo WS (2014). "The relationship between gut and adipose hormones, and reproduction". Human Reproduction Update. 20 (2): 153–174. doi:10.1093/humupd/dmt033. PMID 24173881.
- ^ 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 Research. 29 (17): 3595–3602. 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): 7486–7493. doi:10.1038/sj.onc.1204950. PMID 11709720.
Further reading
edit- Barondes SH, Cooper DN, Gitt MA, Leffler H (August 1994). "Galectins. Structure and function of a large family of animal lectins". The Journal of Biological Chemistry. 269 (33): 20807–20810. doi:10.1016/S0021-9258(17)31891-4. PMID 8063692.
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