Biology:LGALS3BP
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 Generic protein structure example |
Galectin-3-binding protein is a protein that in humans is encoded by the LGALS3BP gene.[1][2][3][4]
Function
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell–cell and cell–matrix interactions. Using fluorescence in–situ hybridization, the full length 90K cDNA has been localized to chromosome 17q25. The native protein binds specifically to a human macrophage-associated lectin known as Mac-2 and also binds to galectin 1.[4]
Clinical significance
LGALS3BP has been found elevated in the serum of patients with cancer and in those infected by the human immunodeficiency virus (HIV). It appears to be implicated in immune response associated with natural killer (NK) and lymphokine-activated killer (LAK) cell cytotoxicity.[4]
Interactions
LGALS3BP has been shown to interact with LGALS3.[3][5][6]
References
- ↑ "The gene (LGALS3BP) encoding the serum protein 90K, associated with cancer and infection by the human immunodeficiency virus, maps at 17q25". Cytogenet Cell Genet 69 (3–4): 223–5. May 1995. doi:10.1159/000133969. PMID 7698018.
- ↑ "The secreted tumor-associated antigen 90K is a potent immune stimulator". J Biol Chem 269 (28): 18401–7. Aug 1994. doi:10.1016/S0021-9258(17)32322-0. PMID 8034587.
- ↑ 3.0 3.1 "Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain". J. Biol. Chem. 268 (19): 14245–9. July 1993. doi:10.1016/S0021-9258(19)85233-X. PMID 8390986.
- ↑ 4.0 4.1 4.2 "Entrez Gene: LGALS3BP lectin, galactoside-binding, soluble, 3 binding protein". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3959.
- ↑ "Mac-2-binding glycoproteins. Putative ligands for a cytosolic beta-galactoside lectin". J. Biol. Chem. 266 (28): 18731–6. October 1991. doi:10.1016/S0021-9258(18)55124-3. PMID 1917996.
- ↑ "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation". Int. J. Cancer 91 (2): 167–72. January 2001. doi:10.1002/1097-0215(200002)9999:9999<::AID-IJC1022>3.3.CO;2-Q. PMID 11146440.
Further reading
- "90K (Mac-2 BP) and galectins in tumor progression and metastasis.". Glycoconj. J. 19 (7–9): 551–6. 2004. doi:10.1023/B:GLYC.0000014085.00706.d4. PMID 14758079.
- "Mac-2-binding glycoproteins. Putative ligands for a cytosolic beta-galactoside lectin.". J. Biol. Chem. 266 (28): 18731–6. 1991. doi:10.1016/S0021-9258(18)55124-3. PMID 1917996.
- "LPS-dependent interaction of Mac-2-binding protein with immobilized CD14.". J. Inflamm. 45 (2): 115–25. 1995. PMID 7583357.
- "Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain.". J. Biol. Chem. 268 (19): 14245–9. 1993. doi:10.1016/S0021-9258(19)85233-X. PMID 8390986.
- "Interactions between galectin-3 and Mac-2-binding protein mediate cell-cell adhesion.". Cancer Res. 56 (19): 4530–4. 1996. PMID 8813152.
- "Expression of the 90K immunostimulator gene is controlled by a promoter with unique features.". J. Biol. Chem. 272 (6): 3674–82. 1997. doi:10.1074/jbc.272.6.3674. PMID 9013622.
- "90K (MAC-2 BP) gene expression in breast cancer and evidence for the production of 90K by peripheral-blood mononuclear cells.". Int. J. Cancer 79 (1): 23–6. 1998. doi:10.1002/(SICI)1097-0215(19980220)79:1<23::AID-IJC5>3.0.CO;2-Y. PMID 9495353.
- "Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin.". EMBO J. 17 (6): 1606–13. 1998. doi:10.1093/emboj/17.6.1606. PMID 9501082.
- "Cyclophilin C-associated protein: a normal secreted glycoprotein that down-modulates endotoxin and proinflammatory responses in vivo.". Proc. Natl. Acad. Sci. U.S.A. 96 (6): 3006–11. 1999. doi:10.1073/pnas.96.6.3006. PMID 10077627. Bibcode: 1999PNAS...96.3006T.
- "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation.". Int. J. Cancer 91 (2): 167–72. 2001. doi:10.1002/1097-0215(200002)9999:9999<::AID-IJC1022>3.3.CO;2-Q. PMID 11146440.
- "Functional studies on recombinant domains of Mac-2-binding protein.". J. Biol. Chem. 277 (18): 15690–6. 2002. doi:10.1074/jbc.M200386200. PMID 11867635.
- "Expression of 90K (Mac-2 BP) correlates with distant metastasis and predicts survival in stage I non-small cell lung cancer patients.". Cancer Res. 62 (9): 2535–9. 2002. PMID 11980646.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932.
- "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.". Nat. Biotechnol. 21 (6): 660–6. 2003. doi:10.1038/nbt827. PMID 12754519.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway.". Nat. Cell Biol. 6 (2): 97–105. 2004. doi:10.1038/ncb1086. PMID 14743216.
- "A proteomic analysis of human bile.". Mol. Cell. Proteomics 3 (7): 715–28. 2005. doi:10.1074/mcp.M400015-MCP200. PMID 15084671.
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