Angiopoietin 1

Angiopoietin 1 is a type of angiopoietin and is encoded by the gene ANGPT1.

ANGPT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4EPU, 4JYO, 4K0V
Identifiers
Aliases	ANGPT1, AGP1, AGPT, ANG1, angiopoietin 1, HAE5, AGPT-1
External IDs	OMIM: 601667; MGI: 108448; HomoloGene: 37447; GeneCards: ANGPT1; OMA:ANGPT1 - orthologs
Gene location (Human) Chr. Chromosome 8 (human) Band 8q23.1 Start 107,249,482 bp End 107,498,055 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15 B3.1|15 16.69 cM Start 42,288,119 bp End 42,540,373 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in lower lobe of lung Achilles tendon optic nerve right lung popliteal artery tibial arteries seminal vesicula urethra stromal cell of endometrium tail of epididymis Top expressed in atrium atrioventricular valve blood genital tubercle intercostal muscle digastric muscle lumbar spinal ganglion molar right lung stroma of bone marrow More reference expression data BioGPS More reference expression data
Gene ontology Molecular function receptor tyrosine kinase binding protein binding signaling receptor binding Cellular component plasma membrane microvillus membrane raft extracellular exosome extracellular region intracellular anatomical structure extracellular space Biological process negative regulation of neuron apoptotic process negative regulation of protein phosphorylation negative regulation of endothelial cell apoptotic process negative regulation of cell adhesion cell differentiation hemopoiesis positive regulation of protein kinase B signaling heparin biosynthetic process positive regulation of receptor internalization regulation of tumor necrosis factor production transmembrane receptor protein tyrosine kinase signaling pathway negative regulation of cytokine production involved in immune response sprouting angiogenesis in utero embryonic development negative regulation of apoptotic process positive regulation of peptidyl-serine phosphorylation MAPK cascade positive regulation of endothelial cell migration multicellular organism development cell-substrate adhesion protein localization to cell surface angiogenesis positive regulation of blood vessel endothelial cell migration positive regulation of ERK1 and ERK2 cascade regulation of macrophage migration inhibitory factor signaling pathway regulation of endothelial cell proliferation positive regulation of phosphatidylinositol 3-kinase signaling positive chemotaxis activation of transmembrane receptor protein tyrosine kinase activity regulation of protein binding regulation of skeletal muscle satellite cell proliferation positive regulation of protein ubiquitination leukocyte migration regulation of I-kappaB kinase/NF-kappaB signaling negative regulation of protein import into nucleus positive regulation of cell adhesion glomerulus vasculature development negative regulation of vascular permeability Tie signaling pathway positive regulation of peptidyl-tyrosine phosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 284 11600 Ensembl ENSG00000154188 ENSMUSG00000022309 UniProt Q15389 O08538 RefSeq (mRNA) NM_001146 NM_001199859 NM_001314051 NM_139290 NM_009640 NM_001286062 RefSeq (protein) NP_001137 NP_001186788 NP_001300980 NP_001272991 NP_033770 Location (UCSC) Chr 8: 107.25 – 107.5 Mb Chr 15: 42.29 – 42.54 Mb PubMed search
Wikidata
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Angiopoietins are proteins with important roles in vascular development and angiogenesis. All angiopoietins bind with similar affinity to an endothelial cell-specific tyrosine-protein kinase receptor. The protein encoded by this gene is a secreted glycoprotein that activates the receptor by inducing its tyrosine phosphorylation. It plays a critical role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. The protein also contributes to blood vessel maturation and stability, and may be involved in early development of the heart. During pregnancy, angiopoietins act complementary to the VEGF system and contribute to endothelial cell survival and the remodeling of vessels. Few studies have examined the role of angiopoietins in human pregnancy complications like preeclampsia and intrauterine growth restriction (IUGR).

A knockout model of ANGPT1 was introduced in mice embryos. Results showed that embryos began to appear abnormal by day 11 and were dead by day 12.5 of pregnancy. The embryos showed prominent defects in endocardial and myocardial development as well as a less complex vascular network.

Interactions

Angiopoietin 1 has been shown to interact with TEK tyrosine kinase.

Placental Malaria

Recently, studies in malaria-endemic areas suggest that placental malaria (PM) may be associated with a dysregulation in angiopoietins. Increased levels of angiopoietin-1 appear to be associated with a decrease in placental weight and placental barrier thickness in women infected with Plasmodium (the causative agent of malaria). In a mouse model of PM, Plasmodium infection of pregnant mice led to decreased angiopoietin-1, increased angiopoietin-2, and an elevated ratio of angiopoietin-2/angiopoietin-1 in the placenta. This suggests that angiopoietin levels could be clinically significant biomarkers to identify mothers infected with PM.

See also

• Angiopoietin

Further reading

• Nakajima D, Okazaki N, Yamakawa H (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Metheny-Barlow LJ, Li LY (2004). "The enigmatic role of angiopoietin-1 in tumor angiogenesis". Cell Res. 13 (5): 309–17. doi:10.1038/sj.cr.7290176. PMID 14672554.
• Makinde T, Murphy RF, Agrawal DK (2007). "Immunomodulatory role of vascular endothelial growth factor and angiopoietin-1 in airway remodeling". Curr. Mol. Med. 6 (8): 831–41. doi:10.2174/156652406779010795. PMID 17168735.
• Nomura N, Miyajima N, Sazuka T (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1". DNA Res. 1 (1): 27–35. doi:10.1093/dnares/1.1.27. PMID 7584026.
• Nomura N, Miyajima N, Sazuka T (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement)". DNA Res. 1 (1): 47–56. doi:10.1093/dnares/1.1.47. PMID 7584028.
• Rüegg C, Pytela R (1995). "Sequence of a human transcript expressed in T-lymphocytes and encoding a fibrinogen-like protein". Gene. 160 (2): 257–62. doi:10.1016/0378-1119(95)00240-7. PMID 7642106.
• Davis S, Aldrich TH, Jones PF (1997). "Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-trap expression cloning". Cell. 87 (7): 1161–9. doi:10.1016/S0092-8674(00)81812-7. PMID 8980223. S2CID 17197564.
• Suri C, Jones PF, Patan S (1997). "Requisite role of angiopoietin-1, a ligand for the TIE2 receptor, during embryonic angiogenesis". Cell. 87 (7): 1171–80. doi:10.1016/S0092-8674(00)81813-9. PMID 8980224. S2CID 15926708.
• Maisonpierre PC, Suri C, Jones PF (1997). "Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis". Science. 277 (5322): 55–60. doi:10.1126/science.277.5322.55. PMID 9204896.
• Ristimäki A, Narko K, Enholm B (1998). "Proinflammatory cytokines regulate expression of the lymphatic endothelial mitogen vascular endothelial growth factor-C". J. Biol. Chem. 273 (14): 8413–8. doi:10.1074/jbc.273.14.8413. PMID 9525952.
• Cheung AH, Stewart RJ, Marsden PA (1998). "Endothelial Tie2/Tek ligands angiopoietin-1 (ANGPT1) and angiopoietin-2 (ANGPT2): regional localization of the human genes to 8q22.3-q23 and 8p23". Genomics. 48 (3): 389–91. doi:10.1006/geno.1997.5207. PMID 9545648.
• Witzenbichler B, Maisonpierre PC, Jones P (1998). "Chemotactic properties of angiopoietin-1 and -2, ligands for the endothelial-specific receptor tyrosine kinase Tie2". J. Biol. Chem. 273 (29): 18514–21. doi:10.1074/jbc.273.29.18514. PMID 9660821.
• Sato A, Iwama A, Takakura N (1998). "Characterization of TEK receptor tyrosine kinase and its ligands, Angiopoietins, in human hematopoietic progenitor cells". Int. Immunol. 10 (8): 1217–27. doi:10.1093/intimm/10.8.1217. PMID 9723709.
• Valenzuela DM, Griffiths JA, Rojas J (1999). "Angiopoietins 3 and 4: diverging gene counterparts in mice and humans". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 1904–9. Bibcode:1999PNAS...96.1904V. doi:10.1073/pnas.96.5.1904. PMC 26709. PMID 10051567.
• Grosios K, Leek JP, Markham AF (1999). "Assignment of ANGPT4, ANGPT1, and ANGPT2 encoding angiopoietins 4, 1 and 2 to human chromosome bands 20p13, 8q22.3→q23 and 8p23.1, respectively, by in situ hybridization and radiation hybrid mapping". Cytogenet. Cell Genet. 84 (1–2): 118–20. doi:10.1159/000015235. PMID 10343124. S2CID 40232421.
• Procopio WN, Pelavin PI, Lee WM, Yielding NM (1999). "Angiopoietin-1 and -2 coiled coil domains mediate distinct homo-oligomerization patterns, but fibrinogen-like domains mediate ligand activity". J. Biol. Chem. 274 (42): 30196–201. doi:10.1074/jbc.274.42.30196. PMID 10514510.
• Huang YQ, Li JJ, Karpatkin S (2000). "Identification of a family of alternatively spliced mRNA species of angiopoietin-1". Blood. 95 (6): 1993–9. doi:10.1182/blood.V95.6.1993. PMID 10706866. S2CID 34946654.
• Kim I, Kim JH, Ryu YS (2000). "Characterization and expression of a novel alternatively spliced human angiopoietin-2". J. Biol. Chem. 275 (24): 18550–6. doi:10.1074/jbc.M910084199. PMID 10766762.
• Dunk C, Shams M, Nijjar S (2000). "Angiopoietin-1 and angiopoietin-2 activate trophoblast Tie-2 to promote growth and migration during placental development". Am. J. Pathol. 156 (6): 2185–99. doi:10.1016/S0002-9440(10)65089-4. PMC 1850068. PMID 10854239.
• Krikun G, Schatz F, Finlay T (2000). "Expression of angiopoietin-2 by human endometrial endothelial cells: regulation by hypoxia and inflammation". Biochem. Biophys. Res. Commun. 275 (1): 159–63. doi:10.1006/bbrc.2000.3277. PMID 10944458.

External links

• Human ANGPT1 genome location and ANGPT1 gene details page in the UCSC Genome Browser.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.