Galectin-1

{{Short description|Protein-coding gene in the species Homo sapiens}}

Galectin-1 is a protein that in humans is encoded by the LGALS1 gene.{{cite journal | vauthors = Gitt MA, Barondes SH | title = Genomic sequence and organization of two members of a human lectin gene family | journal = Biochemistry | volume = 30 | issue = 1 | pages = 82–89 | date = January 1991 | pmid = 1988031 | doi = 10.1021/bi00215a013 }}{{cite journal | vauthors = Gauthier L, Rossi B, Roux F, Termine E, Schiff C | title = 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 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 20 | pages = 13014–13019 | date = October 2002 | pmid = 12271131 | pmc = 130578 | doi = 10.1073/pnas.202323999 | bibcode = 2002PNAS...9913014G | doi-access = free }}

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-covalently bound and will spontaneously disassociate in low concentration.{{cite journal | vauthors = Cho M, Cummings RD | title = Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization | journal = The Journal of Biological Chemistry | volume = 270 | issue = 10 | pages = 5198–5206 | date = March 1995 | pmid = 7890630 | doi = 10.1074/jbc.270.10.5198 | doi-access = free }} Galectin 1 does not bind glycans when oxidized.{{cite journal | vauthors = Outenreath RL, Jones AL | title = Influence of an endogenous lectin substrate on cultured dorsal root ganglion cells | journal = Journal of Neurocytology | volume = 21 | issue = 11 | pages = 788–795 | date = November 1992 | pmid = 1431997 | doi = 10.1007/bf01237904 | s2cid = 20883530 }} 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.{{cite journal | vauthors = Kadoya T, Horie H | title = Structural and functional studies of galectin-1: a novel axonal regeneration-promoting activity for oxidized galectin-1 | journal = Current Drug Targets | volume = 6 | issue = 4 | pages = 375–383 | date = June 2005 | pmid = 16026256 | doi = 10.2174/1389450054022007 }}

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.{{cite web | title = Entrez Gene: LGALS1 lectin, galactoside-binding, soluble, 1 (galectin 1)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3956}} Galectin-1 expression in Hodgkin Lymphoma has also been shown to mediate immunosuppression of CD8+ T-cells.{{cite journal | vauthors = Gandhi MK, Moll G, Smith C, Dua U, Lambley E, Ramuz O, Gill D, Marlton P, Seymour JF, Khanna R | display-authors = 6 | title = Galectin-1 mediated suppression of Epstein-Barr virus specific T-cell immunity in classic Hodgkin lymphoma | journal = Blood | volume = 110 | issue = 4 | pages = 1326–1329 | date = August 2007 | pmid = 17438085 | pmc = 1939905 | doi = 10.1182/blood-2007-01-066100 }}

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.{{cite journal | vauthors = Rubione J, Pérez PS, Czernikier A, Duette GA, Pereyra Gerber FP, Salido J, Fabiano MP, Ghiglione Y, Turk G, Laufer N, Cagnoni AJ, Pérez Sáez JM, Merlo JP, Pascuale C, Stupirski JC, Sued O, Varas-Godoy M, Lewin SR, Mariño KV, Rabinovich GA, Ostrowski M | display-authors = 6 | title = A Dynamic Interplay of Circulating Extracellular Vesicles and Galectin-1 Reprograms Viral Latency during HIV-1 Infection | journal = mBio | volume = 13| issue = 4| pages = e0061122 | date = August 2022 | pmid = 35943163 | doi = 10.1128/mbio.00611-22 | pmc = 9426495 | s2cid = 251407421 }}

Role in pregnancy

Galectin-1 is thought to play a role in creating immune tolerance in pregnancy.{{cite journal | vauthors = Munoz-Suano A, Hamilton AB, Betz AG | title = Gimme shelter: the immune system during pregnancy | journal = Immunological Reviews | volume = 241 | issue = 1 | pages = 20–38 | date = May 2011 | pmid = 21488887 | doi = 10.1111/j.1600-065X.2011.01002.x | s2cid = 46696092 }} 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.{{cite journal | vauthors = Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA | display-authors = 6 | title = Tolerogenic signals delivered by dendritic cells to T cells through a galectin-1-driven immunoregulatory circuit involving interleukin 27 and interleukin 10 | journal = Nature Immunology | volume = 10 | issue = 9 | pages = 981–991 | date = September 2009 | pmid = 19668220 | doi = 10.1038/ni.1772 | s2cid = 24418718 | hdl = 11336/78711 | hdl-access = free }} It also plays a role in the formation and expression of HLA-G in the syncytium.{{cite journal | vauthors = Comninos AN, Jayasena CN, Dhillo WS | title = The relationship between gut and adipose hormones, and reproduction | journal = Human Reproduction Update | volume = 20 | issue = 2 | pages = 153–174 | year = 2014 | pmid = 24173881 | doi = 10.1093/humupd/dmt033 | doi-access = free }}

Interactions

LGALS1 has been shown to interact with GEMIN4{{cite journal | vauthors = Park JW, Voss PG, Grabski S, Wang JL, Patterson RJ | title = Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein | journal = Nucleic Acids Research | volume = 29 | issue = 17 | pages = 3595–3602 | date = September 2001 | pmid = 11522829 | pmc = 55878 | doi = 10.1093/nar/29.17.3595 }} HRAS.{{cite journal | vauthors = Paz A, Haklai R, Elad-Sfadia G, Ballan E, Kloog Y | title = Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation | journal = Oncogene | volume = 20 | issue = 51 | pages = 7486–7493 | date = November 2001 | pmid = 11709720 | doi = 10.1038/sj.onc.1204950 | doi-access = free }}

Galectin-1

Gene and protein

Function

Role in pregnancy

Interactions

See also

References

Further reading