Biology:LRG1
 Generic protein structure example |
Leucine-rich alpha-2-glycoprotein 1 is a protein which in humans is encoded by the gene LRG1.[1]
Function
The leucine-rich repeat (LRR) family of proteins, including LRG1, have been shown to be involved in protein-protein interaction, signal transduction, and cell adhesion and development. LRG1 is expressed during granulocyte differentiation.[1][2]
LRG1 has been shown to be involved in promoting neovascularization (new blood vessel growth) through causing a switch in transforming growth factor beta (TGFbeta) signaling in endothelial cells. LRG1 binds to the accessory receptor endoglin and promotes signaling via the ALK1-Smad1/5/8 pathway.[3]
Application
Levels of the LRG protein are markedly elevated in acute appendicitis and therefore could be used as a diagnostic aid.[4]
LRG1 may be a potential therapeutic target for the treatment of diseases where there is aberrant neovascularization.[3]
Circulating LRG1 levels are increased in many cancer patients and may be a useful biomarker. Inhibition of LRG1 normalises the tumor vasculature, improves the efficacy of cytotoxic and immune therapies,[5] and restricts metastatic spread. [6]
References
- ↑ 1.0 1.1 "Entrez Gene: LRG1 leucine-rich alpha-2-glycoprotein 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=116844.
- ↑ "Molecular characterization and expression analysis of leucine-rich alpha2-glycoprotein, a novel marker of granulocytic differentiation". J. Leukoc. Biol. 72 (3): 478–85. September 2002. doi:10.1189/jlb.72.3.478. PMID 12223515.
- ↑ 3.0 3.1 "LRG1 promotes angiogenesis by modulating endothelial TGF-β signalling". Nature 499 (7458): 306–11. July 2013. doi:10.1038/nature12345. PMID 23868260.
- ↑ Vargas IM (2009-06-23). "A urine test for appendicitis?". HarvardScience Press Release. Harvard College. http://news.harvard.edu/gazette/story/2009/06/a-urine-test-for-appendicitis/.
- ↑ O’Connor, Marie N.; Kallenberg, David M.; Camilli, Carlotta; Pilotti, Camilla; Dritsoula, Athina; Jackstadt, Rene; Bowers, Chantelle E.; Watson, H. Angharad et al. (12 November 2021). "LRG1 destabilizes tumor vessels and restricts immunotherapeutic potency" (in English). Med 2 (11): 1231–1252.e10. doi:10.1016/j.medj.2021.10.002. ISSN 2666-6359. PMID 35590198. https://www.cell.com/med/fulltext/S2666-6340(21)00342-1?.
- ↑ Singhal, Mahak; Gengenbacher, Nicolas; Abdul Pari, Ashik Ahmed; Kamiyama, Miki; Hai, Ling; Kuhn, Bianca J.; Kallenberg, David M.; Kulkarni, Shubhada R. et al. (September 2021). "Temporal multi-omics identifies LRG1 as a vascular niche instructor of metastasis". Science Translational Medicine 13 (609): eabe6805. doi:10.1126/scitranslmed.abe6805. ISSN 1946-6242. PMID 34516824. https://pubmed.ncbi.nlm.nih.gov/34516824/.
Further reading
- "Expression of TGF-betas and TGF-beta type II receptor in cerebrospinal fluid of patients with idiopathic normal pressure hydrocephalus.". Neurosci. Lett. 413 (2): 141–4. 2007. doi:10.1016/j.neulet.2006.11.039. PMID 17194537.
- "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.". J. Proteome Res. 5 (6): 1493–503. 2006. doi:10.1021/pr050492k. PMID 16740002.
- "Serum leucine-rich alpha-2-glycoprotein-1 binds cytochrome c and inhibits antibody detection of this apoptotic marker in enzyme-linked immunosorbent assay.". Apoptosis 11 (7): 1121–9. 2006. doi:10.1007/s10495-006-8159-3. PMID 16699948.
- "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.". J. Proteome Res. 4 (6): 2070–80. 2006. doi:10.1021/pr0502065. PMID 16335952.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.". Oncogene 23 (35): 5901–11. 2004. doi:10.1038/sj.onc.1207782. PMID 15221005.
- "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.". Proteomics 4 (2): 454–65. 2004. doi:10.1002/pmic.200300556. PMID 14760718.
- "The human plasma proteome: a nonredundant list developed by combination of four separate sources.". Mol. Cell. Proteomics 3 (4): 311–26. 2004. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
- "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. Bibcode: 2002PNAS...9916899M.
- "Molecular characterization and expression analysis of leucine-rich alpha2-glycoprotein, a novel marker of granulocytic differentiation.". J. Leukoc. Biol. 72 (3): 478–85. 2002. doi:10.1189/jlb.72.3.478. PMID 12223515.
- "Gene expression profiling of mucosal addressin cell adhesion molecule-1+ high endothelial venule cells (HEV) and identification of a leucine-rich HEV glycoprotein as a HEV marker.". J. Immunol. 168 (3): 1050–9. 2002. doi:10.4049/jimmunol.168.3.1050. PMID 11801638.
- "Periodicity of leucine and tandem repetition of a 24-amino acid segment in the primary structure of leucine-rich alpha 2-glycoprotein of human serum.". Proc. Natl. Acad. Sci. U.S.A. 82 (7): 1906–10. 1985. doi:10.1073/pnas.82.7.1906. PMID 3856868.
- "Identification of candidate biomarkers in ovarian cancer serum by depletion of highly abundant proteins and differential in-gel electrophoresis.". Electrophoresis 31 (4): 599–610. 2010. doi:10.1002/elps.200900441. PMID 20162585.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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