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{{Infobox_gene}}
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'''Angiopoietin-like 3''', also known as '''ANGPTL3''', is a [[protein]] that in humans is encoded by the ''ANGPTL3'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ANGPTL3 angiopoietin-like 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27329| accessdate = }}</ref><ref name="pmid10644446">{{cite journal | vauthors = Conklin D, Gilbertson D, Taft DW, Maurer MF, Whitmore TE, Smith DL, Walker KM, Chen LH, Wattler S, Nehls M, Lewis KB | title = Identification of a mammalian angiopoietin-related protein expressed specifically in liver | journal = Genomics | volume = 62 | issue = 3 | pages = 477–82 |date=December 1999 | pmid = 10644446 | doi = 10.1006/geno.1999.6041 | url =  }}</ref>
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== Function ==
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The protein encoded by this gene is a member of the [[angiopoietin]]-like family of secreted factors. It is expressed predominantly in the liver, and has the characteristic structure of angiopoietins, consisting of a [[signal peptide]], [[N-terminus|N-terminal]] [[coiled-coil]] domain, and the [[C-terminus|C-terminal]] [[fibrinogen]] (FBN)-like domain. The FBN-like domain in angiopoietin-like 3 protein was shown to bind [[Alpha-v beta-3|alpha-5/beta-3 integrins]], and this binding induced endothelial [[cell adhesion]] and [[cell migration|migration]]. This protein may also play a role in the regulation of [[angiogenesis]].<ref name="entrez"/>
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}}
Angptl3 also acts as dual inhibitor of [[lipoprotein lipase]] (LPL) and [[endothelial lipase]] (EL), and increases plasma triglyceride and HDL cholesterol in rodents. ANGPTL3 inhibits endothelial lipase to catalyze HDL-phospholipid and increase HDL-PL levels. Circulating PL-rich HDL particles have high cholesterol efflux abilities.
 
Angptl3 plays a major role in promoting uptake of circulating triglycerides into white adipose tissue in the fed state,<ref name="pmid26305978| 87">{{cite journal | vauthors = Wang Y, McNutt MC, Banfi S, Levin MG, Holland WL, Gusarova V, Gromada J, Cohen JC, Hobbs HH | title = Hepatic ANGPTL3 regulates adipose tissue energy homeostasis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 112 | issue = 37 | pages = 11630–5 | date = Sep 2015 | pmid = 26305978 | doi = 10.1073/pnas.1515374112 | pmc=4577179}}</ref> likely through activation by Angptl8, a feeding-induced hepatokine,<ref name="pmid22809513">{{cite journal | vauthors = Zhang R | title = Lipasin, a novel nutritionally-regulated liver-enriched factor that regulates serum triglyceride levels | journal = Biochemical and Biophysical Research Communications | volume = 424 | issue = 4 | pages = 786–92 | date = Aug 2012 | pmid = 22809513 | doi = 10.1016/j.bbrc.2012.07.038 }}</ref><ref name="pmid22569073">{{cite journal | vauthors = Ren G, Kim JY, Smas CM | title = Identification of RIFL, a novel adipocyte-enriched insulin target gene with a role in lipid metabolism | journal = American Journal of Physiology. Endocrinology and Metabolism | volume = 303 | issue = 3 | pages = E334-51 | date = Aug 2012 | pmid = 22569073 | doi = 10.1152/ajpendo.00084.2012 | pmc=3423120}}</ref> to inhibit postprandial LPL activity in cardiac and skeletal muscles,<ref name="pmid26687026">{{cite journal | vauthors = Fu Z, Abou-Samra AB, Zhang R | title = A lipasin/Angptl8 monoclonal antibody lowers mouse serum triglycerides involving increased postprandial activity of the cardiac lipoprotein lipase | journal = Scientific Reports | volume = 5 | pages = 18502 | date = December 2015 | pmid = 26687026 | doi = 10.1038/srep18502 | url = http://www.nature.com/articles/srep18502 | pmc=4685196}}</ref> as suggested by the ANGPTL3-4-8 model.<ref name="PMID 27053679">{{cite journal | vauthors = Zhang R | title = The ANGPTL3-4-8 model, a molecular mechanism for triglyceride trafficking. | journal = Open Biology | volume = 6 | pages = 150272 | date = April 2016 | pmid = 27053679 | doi = 10.1098/rsob.150272 | url = http://rsob.royalsocietypublishing.org/content/6/4/150272.long | pmc=4852456}}</ref>
 
== Clinical significance ==


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
In human, ANGPTL3 is a determinant factor of HDL level and positively correlates with plasma HDL cholesterol.
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Angiopoietin-like 3
| HGNCid = 491
| Symbol = ANGPTL3
| AltSymbols =; ANGPT5
| OMIM = 604774
| ECnumber = 
| Homologene = 8499
| MGIid = 1353627
| GeneAtlas_image1 = PBB_GE_ANGPTL3_219803_at_tn.png
| Function = {{GNF_GO|id=GO:0004857 |text = enzyme inhibitor activity}} {{GNF_GO|id=GO:0005178 |text = integrin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006641 |text = triacylglycerol metabolic process}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}} {{GNF_GO|id=GO:0030335 |text = positive regulation of cell migration}} {{GNF_GO|id=GO:0045766 |text = positive regulation of angiogenesis}} {{GNF_GO|id=GO:0045834 |text = positive regulation of lipid metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 27329
    | Hs_Ensembl = ENSG00000132855
    | Hs_RefseqProtein = NP_055310
    | Hs_RefseqmRNA = NM_014495
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 62835746
    | Hs_GenLoc_end = 62844418
    | Hs_Uniprot = Q9Y5C1
    | Mm_EntrezGene = 30924
    | Mm_Ensembl = ENSMUSG00000028553
    | Mm_RefseqmRNA = NM_013913
    | Mm_RefseqProtein = NP_038941
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 98522985
    | Mm_GenLoc_end = 98530082
    | Mm_Uniprot = Q3UEF5
  }}
}}
'''Angiopoietin-like 3''', also known as '''ANGPTL3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ANGPTL3 angiopoietin-like 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27329| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
In humans with genetic loss-of-function variants in one copy of ''ANGPTL3'', the serum LDL-C levels are reduced. In those with loss-of-function variants in both copies of ''ANGPTL3'', low LDL-C, low HDL-C, and low triglycerides are seen ("[[familial combined hypolipidemia]]").<ref>{{Cite journal
{{PBB_Summary
| vauthors = Musunuru K, Pirruccello JP, Do R, Peloso GM, Guiducci C, Sougnez C, Garimella KV, Fisher S, Abreu J
| section_title =
| doi = 10.1056/NEJMoa1002926
| summary_text = The protein encoded by this gene is a member of the angiopoietin-like family of secreted factors. It is predominantly expressed in the liver, and has the characteristic structure of angiopoietins, consisting of a signal peptide, N-terminal coiled-coil domain and the C-terminal fibrinogen (FBN)-like domain. The FBN-like domain in angiopoietin-like 3 protein was shown to bind alpha-5/beta-3 integrins, and this binding induced endothelial cell adhesion and migration. This protein may also play a role in the regulation of angiogenesis.<ref name="entrez">{{cite web | title = Entrez Gene: ANGPTL3 angiopoietin-like 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27329| accessdate = }}</ref>
| title = Exome Sequencing,ANGPTL3Mutations, and Familial Combined Hypolipidemia
}}
| journal = New England Journal of Medicine
| volume = 363
| issue = 23
| pages = 2220–2227
| year = 2010
| pmid = 20942659
| pmc =3008575
|display-authors=etal}}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ANGPTL3}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
* {{cite journal | vauthors = Miida T, Seino U, Miyazaki O, Hanyu O, Hirayama S, Saito T, Ishikawa Y, Akamatsu S, Nakano T, Nakajima K, Okazaki M, Okada M | title = Probucol markedly reduces HDL phospholipids and elevated prebeta1-HDL without delayed conversion into alpha-migrating HDL: putative role of angiopoietin-like protein 3 in probucol-induced HDL remodeling | journal = Atherosclerosis | volume = 200 | issue = 2 | pages = 329–35 |date=October 2008 | pmid = 18279878 | doi = 10.1016/j.atherosclerosis.2007.12.031 | url =  }}
* {{cite journal | vauthors = Moon HD, Nakajima K, Kamiyama K, Takanashi K, Sakurabayashi I, Nagamine T | title = Higher frequency of abnormal serum angiopoietin-like protein 3 than abnormal cholesteryl ester transfer protein in Japanese hyperalphalipoproteinemic subjects | journal = Clin. Chim. Acta | volume = 398 | issue = 1–2 | pages = 99–104 |date=December 2008 | pmid = 18804459 | doi = 10.1016/j.cca.2008.08.021 | url =  }}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Li C |title=Genetics and regulation of angiopoietin-like proteins 3 and 4. |journal=Curr. Opin. Lipidol. |volume=17 |issue= 2 |pages= 152-6 |year= 2007 |pmid= 16531751 |doi= 10.1097/01.mol.0000217896.67444.05 }}
*{{cite journal  | author=Li C |title=Genetics and regulation of angiopoietin-like proteins 3 and 4 |journal=Curr. Opin. Lipidol. |volume=17 |issue= 2 |pages= 152–6 |year= 2007 |pmid= 16531751 |doi= 10.1097/01.mol.0000217896.67444.05 }}
*{{cite journal  | author=Conklin D, Gilbertson D, Taft DW, ''et al.'' |title=Identification of a mammalian angiopoietin-related protein expressed specifically in liver. |journal=Genomics |volume=62 |issue= 3 |pages= 477-82 |year= 2000 |pmid= 10644446 |doi= 10.1006/geno.1999.6041 }}
*{{cite journal  | vauthors=Camenisch G, Pisabarro MT, Sherman D |title=ANGPTL3 stimulates endothelial cell adhesion and migration via integrin alpha vbeta 3 and induces blood vessel formation in vivo |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 17281–90 |year= 2002 |pmid= 11877390 |doi= 10.1074/jbc.M109768200 |display-authors=etal}}
*{{cite journal  | author=Camenisch G, Pisabarro MT, Sherman D, ''et al.'' |title=ANGPTL3 stimulates endothelial cell adhesion and migration via integrin alpha vbeta 3 and induces blood vessel formation in vivo. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 17281-90 |year= 2002 |pmid= 11877390 |doi= 10.1074/jbc.M109768200 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Kaplan R, Zhang T, Hernandez M |title=Regulation of the angiopoietin-like protein 3 gene by LXR |journal=J. Lipid Res. |volume=44 |issue= 1 |pages= 136–43 |year= 2003 |pmid= 12518032 |doi=10.1194/jlr.M200367-JLR200 |display-authors=etal}}
*{{cite journal  | author=Kaplan R, Zhang T, Hernandez M, ''et al.'' |title=Regulation of the angiopoietin-like protein 3 gene by LXR. |journal=J. Lipid Res. |volume=44 |issue= 1 |pages= 136-43 |year= 2003 |pmid= 12518032 |doi=  }}
*{{cite journal  | vauthors=Shimamura M, Matsuda M, Kobayashi S |title=Angiopoietin-like protein 3, a hepatic secretory factor, activates lipolysis in adipocytes |journal=Biochem. Biophys. Res. Commun. |volume=301 |issue= 2 |pages= 604–9 |year= 2003 |pmid= 12565906 |doi=10.1016/S0006-291X(02)03058-9 |display-authors=etal}}
*{{cite journal  | author=Shimamura M, Matsuda M, Kobayashi S, ''et al.'' |title=Angiopoietin-like protein 3, a hepatic secretory factor, activates lipolysis in adipocytes. |journal=Biochem. Biophys. Res. Commun. |volume=301 |issue= 2 |pages= 604-9 |year= 2003 |pmid= 12565906 |doi=  }}
*{{cite journal  | vauthors=Zeng L, Dai J, Ying K |title=Identification of a novel human angiopoietin-like gene expressed mainly in heart |journal=J. Hum. Genet. |volume=48 |issue= 3 |pages= 159–62 |year= 2003 |pmid= 12624729 |doi= 10.1007/s100380300025 |display-authors=etal}}
*{{cite journal  | author=Zeng L, Dai J, Ying K, ''et al.'' |title=Identification of a novel human angiopoietin-like gene expressed mainly in heart. |journal=J. Hum. Genet. |volume=48 |issue= 3 |pages= 159-62 |year= 2003 |pmid= 12624729 |doi= 10.1007/s100380300025 }}
*{{cite journal  | vauthors=Ono M, Shimizugawa T, Shimamura M |title=Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 41804–9 |year= 2004 |pmid= 12909640 |doi= 10.1074/jbc.M302861200 |display-authors=etal}}
*{{cite journal  | author=Ono M, Shimizugawa T, Shimamura M, ''et al.'' |title=Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo. |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 41804-9 |year= 2004 |pmid= 12909640 |doi= 10.1074/jbc.M302861200 }}
*{{cite journal  | vauthors=Clark HF, Gurney AL, Abaya E |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 | pmc=403697 |display-authors=etal}}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal  | vauthors=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819–24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504 | pmc=2286551 }}
*{{cite journal  | author=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites. |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819-24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Liu T, Qian WJ, Gritsenko MA |title=Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry |journal=J. Proteome Res. |volume=4 |issue= 6 |pages= 2070–80 |year= 2006 |pmid= 16335952 |doi= 10.1021/pr0502065 | pmc=1850943 |display-authors=etal}}
*{{cite journal  | author=Liu T, Qian WJ, Gritsenko MA, ''et al.'' |title=Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. |journal=J. Proteome Res. |volume=4 |issue= 6 |pages= 2070-80 |year= 2006 |pmid= 16335952 |doi= 10.1021/pr0502065 }}
*{{cite journal  | vauthors=Shimamura M, Matsuda M, Yasumo H |title=Angiopoietin-like protein3 regulates plasma HDL cholesterol through suppression of endothelial lipase |journal=Arterioscler. Thromb. Vasc. Biol. |volume=27 |issue= 2 |pages= 366–72 |year= 2007 |pmid= 17110602 |doi= 10.1161/01.ATV.0000252827.51626.89 |display-authors=etal}}
*{{cite journal  | author=Shimamura M, Matsuda M, Yasumo H, ''et al.'' |title=Angiopoietin-like protein3 regulates plasma HDL cholesterol through suppression of endothelial lipase. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=27 |issue= 2 |pages= 366-72 |year= 2007 |pmid= 17110602 |doi= 10.1161/01.ATV.0000252827.51626.89 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
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Revision as of 18:01, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Angiopoietin-like 3, also known as ANGPTL3, is a protein that in humans is encoded by the ANGPTL3 gene.[1][2]

Function

The protein encoded by this gene is a member of the angiopoietin-like family of secreted factors. It is expressed predominantly in the liver, and has the characteristic structure of angiopoietins, consisting of a signal peptide, N-terminal coiled-coil domain, and the C-terminal fibrinogen (FBN)-like domain. The FBN-like domain in angiopoietin-like 3 protein was shown to bind alpha-5/beta-3 integrins, and this binding induced endothelial cell adhesion and migration. This protein may also play a role in the regulation of angiogenesis.[1]

Angptl3 also acts as dual inhibitor of lipoprotein lipase (LPL) and endothelial lipase (EL), and increases plasma triglyceride and HDL cholesterol in rodents. ANGPTL3 inhibits endothelial lipase to catalyze HDL-phospholipid and increase HDL-PL levels. Circulating PL-rich HDL particles have high cholesterol efflux abilities.

Angptl3 plays a major role in promoting uptake of circulating triglycerides into white adipose tissue in the fed state,[3] likely through activation by Angptl8, a feeding-induced hepatokine,[4][5] to inhibit postprandial LPL activity in cardiac and skeletal muscles,[6] as suggested by the ANGPTL3-4-8 model.[7]

Clinical significance

In human, ANGPTL3 is a determinant factor of HDL level and positively correlates with plasma HDL cholesterol.

In humans with genetic loss-of-function variants in one copy of ANGPTL3, the serum LDL-C levels are reduced. In those with loss-of-function variants in both copies of ANGPTL3, low LDL-C, low HDL-C, and low triglycerides are seen ("familial combined hypolipidemia").[8]

References

  1. ↑ 1.0 1.1 "Entrez Gene: ANGPTL3 angiopoietin-like 3".
  2. ↑ Conklin D, Gilbertson D, Taft DW, Maurer MF, Whitmore TE, Smith DL, Walker KM, Chen LH, Wattler S, Nehls M, Lewis KB (December 1999). "Identification of a mammalian angiopoietin-related protein expressed specifically in liver". Genomics. 62 (3): 477–82. doi:10.1006/geno.1999.6041. PMID 10644446.
  3. ↑ Wang Y, McNutt MC, Banfi S, Levin MG, Holland WL, Gusarova V, Gromada J, Cohen JC, Hobbs HH (Sep 2015). "Hepatic ANGPTL3 regulates adipose tissue energy homeostasis". Proceedings of the National Academy of Sciences of the United States of America. 112 (37): 11630–5. doi:10.1073/pnas.1515374112. PMC 4577179. PMID 26305978.
  4. ↑ Zhang R (Aug 2012). "Lipasin, a novel nutritionally-regulated liver-enriched factor that regulates serum triglyceride levels". Biochemical and Biophysical Research Communications. 424 (4): 786–92. doi:10.1016/j.bbrc.2012.07.038. PMID 22809513.
  5. ↑ Ren G, Kim JY, Smas CM (Aug 2012). "Identification of RIFL, a novel adipocyte-enriched insulin target gene with a role in lipid metabolism". American Journal of Physiology. Endocrinology and Metabolism. 303 (3): E334–51. doi:10.1152/ajpendo.00084.2012. PMC 3423120. PMID 22569073.
  6. ↑ Fu Z, Abou-Samra AB, Zhang R (December 2015). "A lipasin/Angptl8 monoclonal antibody lowers mouse serum triglycerides involving increased postprandial activity of the cardiac lipoprotein lipase". Scientific Reports. 5: 18502. doi:10.1038/srep18502. PMC 4685196. PMID 26687026.
  7. ↑ Zhang R (April 2016). "The ANGPTL3-4-8 model, a molecular mechanism for triglyceride trafficking". Open Biology. 6: 150272. doi:10.1098/rsob.150272. PMC 4852456. PMID 27053679.
  8. ↑ Musunuru K, Pirruccello JP, Do R, Peloso GM, Guiducci C, Sougnez C, Garimella KV, Fisher S, Abreu J, et al. (2010). "Exome Sequencing,ANGPTL3Mutations, and Familial Combined Hypolipidemia". New England Journal of Medicine. 363 (23): 2220–2227. doi:10.1056/NEJMoa1002926. PMC 3008575. PMID 20942659.

External links

Further reading



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