APOA4: Difference between revisions

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{{Infobox_gene}}
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'''Apolipoprotein A-IV''' (also known as apoA-IV, apoAIV, or apoA4) is plasma protein that is the product of the human [[gene]] '''APOA4'''.<ref name="pmid3095836">{{cite journal |vauthors=Karathanasis SK, Oettgen P, Haddad IA, Antonarakis SE | title = Structure, evolution, and polymorphisms of the human apolipoprotein A4 gene (APOA4) | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 83 | issue = 22 | pages = 8457–61 |date=November 1986 | pmid = 3095836 | pmc = 386949 | doi = 10.1073/pnas.83.22.8457| url = | bibcode = 1986PNAS...83.8457K }}</ref><ref name="pmid3036793">{{cite journal |vauthors=Elshourbagy NA, Walker DW, Paik YK, Boguski MS, Freeman M, Gordon JI, Taylor JM | title = Structure and expression of the human apolipoprotein A-IV gene | journal = J. Biol. Chem. | volume = 262 | issue = 17 | pages = 7973–81 |date=June 1987 | pmid = 3036793 | doi = | url = }}</ref>
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== Gene ==
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APOA4 resides on [[chromosome 11]] in close linkage to [[APOA1]] and [[APOC3]]. APOA4 contains 3 [[exon]]s separated by two [[intron]]s, and is [[polymorphism (biology)|polymorphic]], although most of the reported sequence polymorphisms occur in exon 3. The best validated and studied non-synonymous [[Single-nucleotide polymorphism|SNP]]s are a [[glutamine]] → [[histidine]] substitution at [[Codon#RNA codon table|codon]] 360 and a [[threonine]] → [[serine]] substitution at codon 347; a sequence polymorphism has also been identified in the 3'UTR of the third exon.<ref name="entrez"/> Intra-species comparative gene sequence analysis suggests that the APOA4 gene arose from APOA1 by gene duplication approximately 270 [[mya (unit)|MYA]].<ref name="pmid3084795">{{cite journal |vauthors=Luo CC, Li WH, Moore MN, Chan L | title = Structure and evolution of the apolipoprotein multigene family | journal = J. Mol. Biol. | volume = 187 | issue = 3 | pages = 325–340 |date=February 1986 | pmid = 3084795 | doi = 10.1016/0022-2836(86)90436-5| url = }}</ref>
| update_citations = yes
 
}}
== Function ==
 
The primary translation product of the APOA4 gene is a 396-residue preprotein, which undergoes proteolytic processing to yield apo A-IV, a 376-residue mature O-linked glycoprotein. In most mammals, including humans, apo A-IV synthesis is confined to the [[intestine]]; however in mice and rats hepatic synthesis also occurs. Apo A-IV is secreted into circulation on the surface of newly synthesized [[chylomicron]] particles. Intestinal fat absorption dramatically increases the synthesis and secretion of apo A-IV. Although its primary function in human lipid metabolism has not been established, apo A-IV has been found to:
* activate [[lecithin-cholesterol acyltransferase]] and [[cholesterylester transfer protein]] in vitro;
* play a role in the regulation of [[appetite]] and [[satiety]] in rodent models;
* display [[anti-oxidant]] and anti-[[atherosclerosis|atherogenic]] properties in vitro and in rodent models;
* modulate the efficiency of enterocyte and hepatic transcellular [[lipid]] transport in vitro.<ref name="entrez">{{cite web | title = Entrez Gene: APOA4 apolipoprotein A-IV| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=337| accessdate = }}</ref>
 
Human apo A-IV deficiency has not been reported.
 
==Interactions==


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
APOA4 has been shown to [[Protein-protein interaction|interact]] with [[GPLD1]].<ref name=pmid11254757>{{cite journal |last=Deeg |first=M A |authorlink= |author2=Bierman E L |author3=Cheung M C |date=March 2001 |title=GPI-specific phospholipase D associates with an apoA-I- and apoA-IV-containing complex |journal=J. Lipid Res. |volume=42 |issue=3 |pages=442–51 |publisher= |location = United States| issn = 0022-2275| pmid = 11254757 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Apolipoprotein A-IV
| HGNCid = 602
| Symbol = APOA4
| AltSymbols =; MGC142154; MGC142156
  | OMIM = 107690
| ECnumber =
| Homologene = 47927
| MGIid = 88051
| GeneAtlas_image1 = PBB_GE_APOA4_206894_at_tn.png
| Function = {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0016209 |text = antioxidant activity}} {{GNF_GO|id=GO:0030169 |text = low-density lipoprotein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0042627 |text = chylomicron}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006869 |text = lipid transport}} {{GNF_GO|id=GO:0006982 |text = response to lipid hydroperoxide}} {{GNF_GO|id=GO:0008015 |text = circulation}} {{GNF_GO|id=GO:0019430 |text = removal of superoxide radicals}} {{GNF_GO|id=GO:0030300 |text = regulation of cholesterol absorption}} {{GNF_GO|id=GO:0042157 |text = lipoprotein metabolic process}} {{GNF_GO|id=GO:0042744 |text = hydrogen peroxide catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 337
    | Hs_Ensembl = ENSG00000110244
    | Hs_RefseqProtein = NP_000473
    | Hs_RefseqmRNA = NM_000482
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 116196628
    | Hs_GenLoc_end = 116199232
    | Hs_Uniprot = P06727
    | Mm_EntrezGene = 11808
    | Mm_Ensembl = ENSMUSG00000032080
    | Mm_RefseqmRNA = NM_007468
    | Mm_RefseqProtein = NP_031494
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 45992057
    | Mm_GenLoc_end = 45994453
    | Mm_Uniprot = A0AUP0
  }}
}}
'''Apolipoprotein A-IV''', also known as '''APOA4''', is a human [[gene]].


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==Interactive pathway map==
{{PBB_Summary
{{StatinPathway_WP430|highlight=APOA4}}
| section_title =  
| summary_text = Apoliprotein (apo) A-IV gene contains 3 exons separated by two introns. A sequence polymorphism has been identified in the 3'UTR of the third exon.  The primary translation product is a 396-residue preprotein which after proteolytic processing is secreted its primary site of synthesis, the intestine, in association with chylomicron particles.  Although its precise function is not known, apo A-IV is a potent activator of lecithin-cholesterol acyltransferase in vitro.<ref name="entrez">{{cite web | title = Entrez Gene: APOA4 apolipoprotein A-IV| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=337| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{Reflist}}


==Further reading==
==Further reading==
{{refbegin | 2}}
{{Refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=von Eckardstein A, Funke H, Schulte M, ''et al.'' |title=Nonsynonymous polymorphic sites in the apolipoprotein (apo) A-IV gene are associated with changes in the concentration of apo B- and apo A-I-containing lipoproteins in a normal population. |journal=Am. J. Hum. Genet. |volume=50 |issue= 5 |pages= 1115-28 |year= 1992 |pmid= 1349197 |doi=  }}
*{{cite journal  |vauthors=von Eckardstein A, Funke H, Schulte M |title=Nonsynonymous polymorphic sites in the apolipoprotein (apo) A-IV gene are associated with changes in the concentration of apo B- and apo A-I-containing lipoproteins in a normal population. |journal=American Journal of Human Genetics |volume=50 |issue= 5 |pages= 1115–28 |year= 1992 |pmid= 1349197 |doi=  | pmc=1682587  |display-authors=etal}}
*{{cite journal  | author=Kamboh MI, Williams ER, Law JC, ''et al.'' |title=Molecular basis of a unique African variant (A-IV 5) of human apolipoprotein A-IV and its significance in lipid metabolism. |journal=Genet. Epidemiol. |volume=9 |issue= 6 |pages= 379-88 |year= 1993 |pmid= 1487136 |doi= 10.1002/gepi.1370090602 }}
*{{cite journal  |vauthors=Kamboh MI, Williams ER, Law JC |title=Molecular basis of a unique African variant (A-IV 5) of human apolipoprotein A-IV and its significance in lipid metabolism. |journal=Genet. Epidemiol. |volume=9 |issue= 6 |pages= 379–88 |year= 1993 |pmid= 1487136 |doi= 10.1002/gepi.1370090602 |display-authors=etal}}
*{{cite journal  | author=Lohse P, Kindt MR, Rader DJ, Brewer HB |title=Three genetic variants of human plasma apolipoprotein A-IV. apoA-IV-1(Thr347----Ser), apoA-IV-0(Lys167----Glu,Gln360----His), and apoA-IV-3(Glu165----Lys). |journal=J. Biol. Chem. |volume=266 |issue= 21 |pages= 13513-8 |year= 1991 |pmid= 1677358 |doi=  }}
*{{cite journal  |vauthors=Lohse P, Kindt MR, Rader DJ, Brewer HB |title=Three genetic variants of human plasma apolipoprotein A-IV. apoA-IV-1(Thr347----Ser), apoA-IV-0(Lys167----Glu,Gln360----His), and apoA-IV-3(Glu165----Lys). |journal=J. Biol. Chem. |volume=266 |issue= 21 |pages= 13513–8 |year= 1991 |pmid= 1677358 |doi=  }}
*{{cite journal  | author=Tenkanen H, Koskinen P, Metso J, ''et al.'' |title=A novel polymorphism of apolipoprotein A-IV is the result of an asparagine to serine substitution at residue 127. |journal=Biochim. Biophys. Acta |volume=1138 |issue= 1 |pages= 27-33 |year= 1992 |pmid= 1737067 |doi=  }}
*{{cite journal  |vauthors=Tenkanen H, Koskinen P, Metso J |title=A novel polymorphism of apolipoprotein A-IV is the result of an asparagine to serine substitution at residue 127. |journal=Biochim. Biophys. Acta |volume=1138 |issue= 1 |pages= 27–33 |year= 1992 |pmid= 1737067 |doi=  10.1016/0925-4439(92)90147-f|display-authors=etal}}
*{{cite journal  | author=Lohse P, Kindt MR, Rader DJ, Brewer HB |title=Human plasma apolipoproteins A-IV-0 and A-IV-3. Molecular basis for two rare variants of apolipoprotein A-IV-1. |journal=J. Biol. Chem. |volume=265 |issue= 21 |pages= 12734-9 |year= 1990 |pmid= 1973689 |doi=  }}
*{{cite journal  |vauthors=Lohse P, Kindt MR, Rader DJ, Brewer HB |title=Human plasma apolipoproteins A-IV-0 and A-IV-3. Molecular basis for two rare variants of apolipoprotein A-IV-1. |journal=J. Biol. Chem. |volume=265 |issue= 21 |pages= 12734–9 |year= 1990 |pmid= 1973689 |doi=  }}
*{{cite journal  | author=Tenkanen H, Lukka M, Jauhiainen M, ''et al.'' |title=The mutation causing the common apolipoprotein A-IV polymorphism is a glutamine to histidine substitution of amino acid 360. |journal=Arterioscler. Thromb. |volume=11 |issue= 4 |pages= 851-6 |year= 1991 |pmid= 2065039 |doi=  }}
*{{cite journal  |vauthors=Tenkanen H, Lukka M, Jauhiainen M |title=The mutation causing the common apolipoprotein A-IV polymorphism is a glutamine to histidine substitution of amino acid 360. |journal=Arterioscler. Thromb. |volume=11 |issue= 4 |pages= 851–6 |year= 1991 |pmid= 2065039 |doi=  10.1161/01.atv.11.4.851|display-authors=etal}}
*{{cite journal  | author=de Temmerman P, Visvikis S, Boerwinkle E, Siest G |title=Study of the sequence tagged site (STS) in the beginning of human apo A4 gene region. |journal=Nucleic Acids Res. |volume=18 |issue= 18 |pages= 5576 |year= 1990 |pmid= 2216752 |doi=  }}
*{{cite journal  |vauthors=de Temmerman P, Visvikis S, Boerwinkle E, Siest G |title=Study of the sequence tagged site (STS) in the beginning of human apo A4 gene region. |journal=Nucleic Acids Res. |volume=18 |issue= 18 |pages= 5576 |year= 1990 |pmid= 2216752 |doi=10.1093/nar/18.18.5576  | pmc=332267 }}
*{{cite journal  | author=Wei S, Rocchi M, Archidiacono N, ''et al.'' |title=Physical mapping of the human chromosome 11q23 region containing the ataxia-telangiectasia locus. |journal=Cancer Genet. Cytogenet. |volume=46 |issue= 1 |pages= 1-8 |year= 1990 |pmid= 2331673 |doi=  }}
*{{cite journal  |vauthors=Wei S, Rocchi M, Archidiacono N |title=Physical mapping of the human chromosome 11q23 region containing the ataxia-telangiectasia locus. |journal=Cancer Genet. Cytogenet. |volume=46 |issue= 1 |pages= 1–8 |year= 1990 |pmid= 2331673 |doi=10.1016/0165-4608(90)90002-R |display-authors=etal}}
*{{cite journal  | author=Lohse P, Kindt MR, Rader DJ, Brewer HB |title=Genetic polymorphism of human plasma apolipoprotein A-IV is due to nucleotide substitutions in the apolipoprotein A-IV gene. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 10061-4 |year= 1990 |pmid= 2351649 |doi=  }}
*{{cite journal  |vauthors=Lohse P, Kindt MR, Rader DJ, Brewer HB |title=Genetic polymorphism of human plasma apolipoprotein A-IV is due to nucleotide substitutions in the apolipoprotein A-IV gene. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 10061–4 |year= 1990 |pmid= 2351649 |doi=  }}
*{{cite journal  | author=Yang CY, Gu ZW, Chong IS, ''et al.'' |title=The primary structure of human apolipoprotein A-IV. |journal=Biochim. Biophys. Acta |volume=1002 |issue= 2 |pages= 231-7 |year= 1989 |pmid= 2930771 |doi= }}
*{{cite journal  |vauthors=Yang CY, Gu ZW, Chong IS |title=The primary structure of human apolipoprotein A-IV. |journal=Biochim. Biophys. Acta |volume=1002 |issue= 2 |pages= 231–7 |year= 1989 |pmid= 2930771 |doi= 10.1016/0005-2760(89)90292-0 |display-authors=etal}}
*{{cite journal  | author=Elshourbagy NA, Walker DW, Paik YK, ''et al.'' |title=Structure and expression of the human apolipoprotein A-IV gene. |journal=J. Biol. Chem. |volume=262 |issue= 17 |pages= 7973-81 |year= 1987 |pmid= 3036793 |doi=  }}
*{{cite journal  |vauthors=Elshourbagy NA, Walker DW, Boguski MS |title=The nucleotide and derived amino acid sequence of human apolipoprotein A-IV mRNA and the close linkage of its gene to the genes of apolipoproteins A-I and C-III. |journal=J. Biol. Chem. |volume=261 |issue= 5 |pages= 1998–2002 |year= 1986 |pmid= 3080432 |doi=  |display-authors=etal}}
*{{cite journal  | author=Elshourbagy NA, Walker DW, Boguski MS, ''et al.'' |title=The nucleotide and derived amino acid sequence of human apolipoprotein A-IV mRNA and the close linkage of its gene to the genes of apolipoproteins A-I and C-III. |journal=J. Biol. Chem. |volume=261 |issue= 5 |pages= 1998-2002 |year= 1986 |pmid= 3080432 |doi=  }}
*{{cite journal  |vauthors=Bisgaier CL, Sachdev OP, Lee ES |title=Effect of lecithin:cholesterol acyltransferase on distribution of apolipoprotein A-IV among lipoproteins of human plasma. |journal=J. Lipid Res. |volume=28 |issue= 6 |pages= 693–703 |year= 1987 |pmid= 3611972 |doi=  |display-authors=etal}}
*{{cite journal  | author=Karathanasis SK, Oettgen P, Haddad IA, Antonarakis SE |title=Structure, evolution, and polymorphisms of the human apolipoprotein A4 gene (APOA4). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 22 |pages= 8457-61 |year= 1986 |pmid= 3095836 |doi=  }}
*{{cite journal  |vauthors=Karathanasis SK, Yunis I, Zannis VI |title=Structure, evolution, and tissue-specific synthesis of human apolipoprotein AIV. |journal=Biochemistry |volume=25 |issue= 13 |pages= 3962–70 |year= 1986 |pmid= 3755616 |doi=10.1021/bi00361a034 }}
*{{cite journal  | author=Bisgaier CL, Sachdev OP, Lee ES, ''et al.'' |title=Effect of lecithin:cholesterol acyltransferase on distribution of apolipoprotein A-IV among lipoproteins of human plasma. |journal=J. Lipid Res. |volume=28 |issue= 6 |pages= 693-703 |year= 1987 |pmid= 3611972 |doi=  }}
*{{cite journal  | author=Karathanasis SK |title=Apolipoprotein multigene family: tandem organization of human apolipoprotein AI, CIII, and AIV genes |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=82 |issue= 19 |pages= 6374–8 |year= 1985 |pmid= 3931073 |doi=10.1073/pnas.82.19.6374 | pmc=390718  |bibcode=1985PNAS...82.6374K }}
*{{cite journal  | author=Karathanasis SK, Yunis I, Zannis VI |title=Structure, evolution, and tissue-specific synthesis of human apolipoprotein AIV. |journal=Biochemistry |volume=25 |issue= 13 |pages= 3962-70 |year= 1986 |pmid= 3755616 |doi=  }}
*{{cite journal  |vauthors=Gordon JI, Bisgaier CL, Sims HF |title=Biosynthesis of human preapolipoprotein A-IV. |journal=J. Biol. Chem. |volume=259 |issue= 1 |pages= 468–74 |year= 1984 |pmid= 6706947 |doi=  |display-authors=etal}}
*{{cite journal  | author=Karathanasis SK |title=Apolipoprotein multigene family: tandem organization of human apolipoprotein AI, CIII, and AIV genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 19 |pages= 6374-8 |year= 1985 |pmid= 3931073 |doi= }}
*{{cite journal  |vauthors=Menzel HJ, Dieplinger H, Sandholzer C |title=Apolipoprotein A-IV polymorphism in the Hungarian population: gene frequencies, effect on lipid levels, and sequence of two new variants. |journal=Hum. Mutat. |volume=5 |issue= 1 |pages= 58–65 |year= 1995 |pmid= 7728150 |doi= 10.1002/humu.1380050108 |display-authors=etal}}
*{{cite journal  | author=Gordon JI, Bisgaier CL, Sims HF, ''et al.'' |title=Biosynthesis of human preapolipoprotein A-IV. |journal=J. Biol. Chem. |volume=259 |issue= 1 |pages= 468-74 |year= 1984 |pmid= 6706947 |doi=  }}
*{{cite journal  |vauthors=Duverger N, Tremp G, Caillaud JM |title=Protection against atherogenesis in mice mediated by human apolipoprotein A-IV |journal=Science |volume=273 |issue= 5277 |pages= 966–8 |year= 1996 |pmid= 8688083 |doi=10.1126/science.273.5277.966 |display-authors=etal|bibcode=1996Sci...273..966D }}
*{{cite journal  | author=Menzel HJ, Dieplinger H, Sandholzer C, ''et al.'' |title=Apolipoprotein A-IV polymorphism in the Hungarian population: gene frequencies, effect on lipid levels, and sequence of two new variants. |journal=Hum. Mutat. |volume=5 |issue= 1 |pages= 58-65 |year= 1995 |pmid= 7728150 |doi= 10.1002/humu.1380050108 }}
*{{cite journal  |vauthors=Deeb SS, Nevin DN, Iwasaki L, Brunzell JD |title=Two novel apolipoprotein A-IV variants in individuals with familial combined hyperlipidemia and diminished levels of lipoprotein lipase activity. |journal=Hum. Mutat. |volume=8 |issue= 4 |pages= 319–25 |year= 1997 |pmid= 8956036 |doi= 10.1002/(SICI)1098-1004(1996)8:4<319::AID-HUMU4>3.0.CO;2-2 }}
*{{cite journal  | author=Duverger N, Tremp G, Caillaud JM, ''et al.'' |title=Protection against atherogenesis in mice mediated by human apolipoprotein A-IV. |journal=Science |volume=273 |issue= 5277 |pages= 966-8 |year= 1996 |pmid= 8688083 |doi=  }}
}}
*{{cite journal  | author=Deeb SS, Nevin DN, Iwasaki L, Brunzell JD |title=Two novel apolipoprotein A-IV variants in individuals with familial combined hyperlipidemia and diminished levels of lipoprotein lipase activity. |journal=Hum. Mutat. |volume=8 |issue= 4 |pages= 319-25 |year= 1997 |pmid= 8956036 |doi= 10.1002/(SICI)1098-1004(1996)8:4&lt;319::AID-HUMU4&gt;3.0.CO;2-2 }}
{{Refend}}
 
==External links==
* {{MeshName|Apolipoprotein+A-IV}}
* {{UCSC gene info|APOA4}}
 
{{Lipoproteins}}
 
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{{protein-stub}}
{{DEFAULTSORT:Apoa4}}
{{WikiDoc Sources}}
[[Category:Apolipoproteins]]
 
 
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Latest revision as of 11:27, 5 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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Wikidata
View/Edit Human

Apolipoprotein A-IV (also known as apoA-IV, apoAIV, or apoA4) is plasma protein that is the product of the human gene APOA4.[1][2]

Gene

APOA4 resides on chromosome 11 in close linkage to APOA1 and APOC3. APOA4 contains 3 exons separated by two introns, and is polymorphic, although most of the reported sequence polymorphisms occur in exon 3. The best validated and studied non-synonymous SNPs are a glutamine → histidine substitution at codon 360 and a threonine → serine substitution at codon 347; a sequence polymorphism has also been identified in the 3'UTR of the third exon.[3] Intra-species comparative gene sequence analysis suggests that the APOA4 gene arose from APOA1 by gene duplication approximately 270 MYA.[4]

Function

The primary translation product of the APOA4 gene is a 396-residue preprotein, which undergoes proteolytic processing to yield apo A-IV, a 376-residue mature O-linked glycoprotein. In most mammals, including humans, apo A-IV synthesis is confined to the intestine; however in mice and rats hepatic synthesis also occurs. Apo A-IV is secreted into circulation on the surface of newly synthesized chylomicron particles. Intestinal fat absorption dramatically increases the synthesis and secretion of apo A-IV. Although its primary function in human lipid metabolism has not been established, apo A-IV has been found to:

Human apo A-IV deficiency has not been reported.

Interactions

APOA4 has been shown to interact with GPLD1.[5]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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Statin Pathway edit
  1. ↑ The interactive pathway map can be edited at WikiPathways: "Statin_Pathway_WP430".

References

  1. ↑ Karathanasis SK, Oettgen P, Haddad IA, Antonarakis SE (November 1986). "Structure, evolution, and polymorphisms of the human apolipoprotein A4 gene (APOA4)". Proceedings of the National Academy of Sciences of the United States of America. 83 (22): 8457–61. Bibcode:1986PNAS...83.8457K. doi:10.1073/pnas.83.22.8457. PMC 386949. PMID 3095836.
  2. ↑ Elshourbagy NA, Walker DW, Paik YK, Boguski MS, Freeman M, Gordon JI, Taylor JM (June 1987). "Structure and expression of the human apolipoprotein A-IV gene". J. Biol. Chem. 262 (17): 7973–81. PMID 3036793.
  3. ↑ 3.0 3.1 "Entrez Gene: APOA4 apolipoprotein A-IV".
  4. ↑ Luo CC, Li WH, Moore MN, Chan L (February 1986). "Structure and evolution of the apolipoprotein multigene family". J. Mol. Biol. 187 (3): 325–340. doi:10.1016/0022-2836(86)90436-5. PMID 3084795.
  5. ↑ Deeg, M A; Bierman E L; Cheung M C (March 2001). "GPI-specific phospholipase D associates with an apoA-I- and apoA-IV-containing complex". J. Lipid Res. United States. 42 (3): 442–51. ISSN 0022-2275. PMID 11254757.

Further reading

External links


Retrieved from "https://www.wikidoc.org/index.php?title=APOA4&oldid=1527790"