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{{SK}} CERP; cholesterol efflux regulatory protein
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'''ATP-binding cassette transporter ABCA1 (member 1 of human transporter sub-family ABCA'''is a human protein and [[gene]]. This transporter is a major regulator of cellular [[cholesterol]] and [[phospholipid]] [[homeostasis]].


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==Overview==
{{PBB_Summary
{{See also|ATP-binding cassette transporter}}
| section_title =  
'''ATP-binding cassette transporter ABCA1 (member 1 of human transporter sub-family ABCA'''), also known as the cholesterol efflux regulatory protein (CERP) is a [[protein]] which in humans is encoded by the ''ABCA1'' [[gene]].<ref name="pmid8088782">{{cite journal | author = Luciani MF, Denizot F, Savary S, Mattei MG, Chimini G | title = Cloning of two novel ABC transporters mapping on human chromosome 9 | journal = Genomics | volume = 21 | issue = 1 | pages = 150–9 | year = 1994 | month = May | pmid = 8088782 | doi = 10.1006/geno.1994.1237 | url = }}</ref> This transporter is a major regulator of cellular [[cholesterol]] and [[phospholipid]] [[homeostasis]]. The membrane-associated protein encoded by this gene is a member of the superfamily of [[ATP-binding cassette transporter|ATP-binding cassette (ABC) transporters]].  ABC proteins transport various molecules across extra- and intracellular membranes.  ABC genes are divided into seven distinct subfamilies (ABCA, MDR/TAP, MRP, ALD, OABP, GCN20, White).  This protein is a member of the ABCA subfamily.  Members of the ABCA subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes.  With cholesterol as its substrate, this protein functions as a cholesterol [[efflux]] pump in the cellular lipid removal pathway.  Mutations in this gene have been associated with [[Tangier's disease]] and familial [[high-density lipoprotein]] deficiency.<ref>{{cite web | title = Entrez Gene: ABCA1 ATP-binding cassette, sub-family A (ABC1), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=19| accessdate =}}</ref>
| summary_text = The membrane-associated protein encoded by this gene is a member of the superfamily of [[ATP-binding cassette transporter|ATP-binding cassette (ABC) transporters]].  ABC proteins transport various molecules across extra- and intracellular membranes.  ABC genes are divided into seven distinct subfamilies (ABCA, MDR/TAP, MRP, ALD, OABP, GCN20, White).  This protein is a member of the ABCA subfamily.  Members of the ABCA subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes.  With cholesterol as its substrate, this protein functions as a cholesterol [[efflux]] pump in the cellular lipid removal pathway.  Mutations in this gene have been associated with [[Tangier's disease]] and familial [[high-density lipoprotein]] deficiency.<ref>{{cite web | title = Entrez Gene: ABCA1 ATP-binding cassette, sub-family A (ABC1), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=19| accessdate = }}</ref>
 
}}
==Tangier Disease==
ABCA1 was discovered as the mutation causing [[Tangier Disease]] by several groups in 1998.  Gerd Schmitz's group in Germany<ref name="pmid10431237">{{cite journal | author = Bodzioch M, Orsó E, Klucken J, Langmann T, Böttcher A, Diederich W, Drobnik W, Barlage S, Büchler C, Porsch-Ozcürümez M, Kaminski WE, Hahmann HW, Oette K, Rothe G, Aslanidis C, Lackner KJ, Schmitz G | title = The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease | journal = Nature Genetics | volume = 22 | issue = 4 | pages = 347–51 | year = 1999 | month = August | pmid = 10431237 | doi = 10.1038/11914 | url =  }}</ref> and Michael Hayden's group in British Columbia<ref name="pmid10431236">{{cite journal | author = Brooks-Wilson A, Marcil M, Clee SM, Zhang LH, Roomp K, van Dam M, Yu L, Brewer C, Collins JA, Molhuizen HO, Loubser O, Ouelette BF, Fichter K, Ashbourne-Excoffon KJ, Sensen CW, Scherer S, Mott S, Denis M, Martindale D, Frohlich J, Morgan K, Koop B, Pimstone S, Kastelein JJ, Genest J, Hayden MR | title = Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency | journal = Nature Genetics | volume = 22 | issue = 4 | pages = 336–45 | year = 1999 | month = August | pmid = 10431236 | doi = 10.1038/11905 | url =  }}</ref> were using standard genetics techniques and DNA from family pedigrees to locate the mutation.  Richard Lawn's group at CV Therapeutics in Palo Alto, CA used cDNA microarrays, which were relatively new at the time, to assess gene expression profiles from cell lines created from normal and effected individuals.<ref name="pmid10525055">{{cite journal | author = Lawn RM, Wade DP, Garvin MR, Wang X, Schwartz K, Porter JG, Seilhamer JJ, Vaughan AM, Oram JF | title = The Tangier disease gene product ABC1 controls the cellular apolipoprotein-mediated lipid removal pathway | journal = The Journal of Clinical Investigation | volume = 104 | issue = 8 | pages = R25–31 | year = 1999 | month = October | pmid = 10525055 | pmc = 481052 | doi = 10.1172/JCI8119 | url =  }}</ref>  They showed cell lines from patients with Tangier's disease showed differential regulation of the ABCA1 gene.  Subsequent sequencing of the gene identified the mutations.  This group received an award from the American Heart Association for their discovery.<ref name="urlAmerican Heart Association ">{{cite web | url = http://www.prnewswire.com/cgi-bin/stories.pl?ACCT=104&STORY=/www/story/01-03-2000/0001106348&EDATE= | title = American Heart Association Selects CV Therapeutics' Discovery of Role Of 'Good' Cholesterol-Regulating Gene as Top Ten 1999 Research Advances In Heart Disease | author = | authorlink = | coauthors = | date = 2000-01-03 | format = | work = | publisher = PR Newswire Association | pages = | language = | archiveurl = | archivedate = | quote = | accessdate = 2009-05-08}}</ref>
 
==Function==
The membrane-associated protein encoded by this gene is a member of the superfamily of [[ATP-binding cassette transporter|ATP-binding cassette (ABC) transporters]].  ABC proteins transport various molecules across extra- and intracellular membranes.  ABC genes are divided into seven distinct subfamilies (ABCA, MDR/TAP, MRP, ALD, OABP, GCN20, White).  This protein is a member of the ABCA subfamily.  Members of the ABCA subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes.  With cholesterol as its substrate, this protein functions as a cholesterol [[efflux (microbiology)|efflux]] pump in the cellular lipid removal pathway.<ref>{{cite web | title = Entrez Gene: ABCA1 ATP-binding cassette, sub-family A (ABC1), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=19| accessdate = }}</ref><ref name="pmid11264984">{{cite journal | author = Schmitz G, Langmann T | title = Structure, function and regulation of the ABC1 gene product | journal = Curr. Opin. Lipidol. | volume = 12 | issue = 2 | pages = 129–40 | year = 2001 | month = April | pmid = 11264984 | doi = 10.1097/00041433-200104000-00006| url = }}</ref>
 
==Physiological role==
ABCA1 mediates the efflux of [[cholesterol]] and [[phospholipid]]s to lipid-poor [[apolipoprotein]]s (apo-A1 and apoE), which then form nascent [[high-density lipoprotein]]s (HDL). It also mediates the transport of lipids between Golgi and [[cell membrane]]. Since this protein is needed throughout the body it is [[Biosynthesis|expressed]] ubiquitously as a 220-[[Dalton (unit)|kDa]] protein. It is present in higher quantities in tissues that shuttle or are involved in the turnover of lipids such as the liver, the small intestine and adipose tissue.<ref>E. M. Wagner, F. Basso, C. S. Kim, M. J. A. Amar, "ABC lipid transporters", in AccessScience@McGraw-Hill</ref>
 
Factors that act upon the ABCA1 transporter's expression or its [[posttranslational modification]] are also molecules that are involved in its subsequent function like [[fatty acid]]s, cholesterol and also [[cytokine]]s and [[cyclic adenosine monophosphate]].<ref name="pmid16505586">{{cite journal | author = Yokoyama S | title = ABCA1 and biogenesis of HDL | journal = J. Atheroscler. Thromb. | volume = 13 | issue = 1 | pages = 1–15 | year = 2006 | month = February | pmid = 16505586 | doi = 10.5551/jat.13.1| url = http://www.jstage.jst.go.jp/article/jat/13/1/13_1/_article }}</ref>
 
Overexpression of ABCA1 has been reported to induce resistance to the anti-inflammatory, dietary [[polyphenolic antioxidant]] [[Curcumin]]<ref>{{cite journal | author = Bachmeier BE, Iancu CM, Killian PH, Kronski E, Mirisola V, Angelini G, Jochum M, Nerlich AG,Pfeffer U.| year = 2009 | title = Overexpression of the ATP binding cassette gene ABCA1 determines resistance to Curcumin in M14 melanoma cells | journal = Mol Cancer| volume = 8 | pages = 129–141 | pmid = 20030852 | doi=10.1186/1476-4598-8-129 | pmc=2804606}}</ref>
Downregulation of ABCA1 in senescent macrophages disrupts the cell's ability to remove cholesterol from it's cytosoplasm, leading the cells to promote the pathologic angiogenesis that "plays a central role in common age-associated diseases such as atherosclerosis, cancer, and macular degeneration" <ref>{{cite journal | author = Sene A, Khan AA,, et al| year = 2013 | title = Impaired Cholesterol Efflux in Senescent Macrophages Promotes Age-Related Macular Degeneration | journal = Cell Metabolism| volume = 17 | pages = 549–561 }}</ref>
 
==Clinical significance==
Mutations in this gene have been associated with [[Tangier disease]] and familial [[high-density lipoprotein]] deficiency. ABCA1 has been shown to be reduced in [[Tangier disease]] which features physiological deficiencies of HDL.<ref name="pmid10812922">{{cite journal | author = Ordovas JM | title = ABC1: the gene for Tangier disease and beyond | journal = Nutr. Rev. | volume = 58 | issue = 3 Pt 1 | pages = 76–9 | year = 2000 | month = March | pmid = 10812922 | doi = 10.1111/j.1753-4887.2000.tb01843.x| url =  }}</ref><ref name="pmid10882340">{{cite journal | author = Oram JF, Vaughan AM | title = ABCA1-mediated transport of cellular cholesterol and phospholipids to HDL apolipoproteins | journal = Curr. Opin. Lipidol. | volume = 11 | issue = 3 | pages = 253–60 | year = 2000 | month = June | pmid = 10882340 | doi = 10.1097/00041433-200006000-00005| url =  }}</ref>
 
==Interactions==
ABCA1 has been shown to [[Protein-protein interaction|interact]] with [[Apolipoprotein A1]],<ref name=pmid12084722>{{cite journal |last=Fitzgerald |first=Michael L |authorlink= |coauthors=Morris Andrea L, Rhee Jeongmi S, Andersson Lorna P, Mendez Armando J, Freeman Mason W |year=2002|month=September  |title=Naturally occurring mutations in the largest extracellular loops of ABCA1 can disrupt its direct interaction with apolipoprotein A-I |journal=J. Biol. Chem. |volume=277 |issue=36 |pages=33178–87 |publisher= |location = United States| issn = 0021-9258| pmid = 12084722 |doi = 10.1074/jbc.M204996200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[FADD]],<ref name=pmid12235128>{{cite journal |last=Buechler |first=Christa |authorlink= |coauthors=Bared Salim Maa, Aslanidis Charalampos, Ritter Mirko, Drobnik Wolfgang, Schmitz Gerd |year=2002|month=November  |title=Molecular and functional interaction of the ATP-binding cassette transporter A1 with Fas-associated death domain protein |journal=J. Biol. Chem. |volume=277 |issue=44 |pages=41307–10 |publisher= |location = United States| issn = 0021-9258| pmid = 12235128 |doi = 10.1074/jbc.C200436200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[XPC (gene)|XPC]]<ref name=pmid12505994>{{cite journal |last=Shimizu |first=Yuichiro |authorlink= |coauthors=Iwai Shigenori, Hanaoka Fumio, Sugasawa Kaoru |year=2003|month=January  |title=Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase |journal=EMBO J. |volume=22 |issue=1 |pages=164–73 |publisher= |location = England| issn = 0261-4189| pmid = 12505994 |doi = 10.1093/emboj/cdg016 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=140069 }}</ref> and [[SNTB2]].<ref name=pmid12054535>{{cite journal |last=Buechler |first=Christa |authorlink= |coauthors=Boettcher Alfred, Bared Salim Maa, Probst Mario C O, Schmitz Gerd |year=2002|month=May. |title=The carboxyterminus of the ATP-binding cassette transporter A1 interacts with a beta2-syntrophin/utrophin complex |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue=2 |pages=759–65 |publisher= |location = United States| issn = 0006-291X| pmid = 12054535 |doi = 10.1016/S0006-291X(02)00303-0 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{Reflist|2}}
==Further reading==
 
{{refbegin | 2}}
[[Category:ABC transporters]]
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Oram JF |title=ATP-binding cassette transporter A1 and cholesterol trafficking. |journal=Curr. Opin. Lipidol. |volume=13 |issue= 4 |pages= 373-81 |year= 2003 |pmid= 12151852 |doi=  }}
*{{cite journal  | author=Hong SH, Rhyne J, Zeller K, Miller M |title=ABCA1(Alabama): a novel variant associated with HDL deficiency and premature coronary artery disease. |journal=Atherosclerosis |volume=164 |issue= 2 |pages= 245-50 |year= 2003 |pmid= 12204794 |doi=  }}
*{{cite journal  | author=Kozak M |title=Emerging links between initiation of translation and human diseases. |journal=Mamm. Genome |volume=13 |issue= 8 |pages= 401-10 |year= 2003 |pmid= 12226704 |doi= 10.1007/s00335-002-4002-5 }}
*{{cite journal  | author=Joyce C, Freeman L, Brewer HB, Santamarina-Fojo S |title=Study of ABCA1 function in transgenic mice. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=23 |issue= 6 |pages= 965-71 |year= 2004 |pmid= 12615681 |doi= 10.1161/01.ATV.0000055194.85073.FF }}
*{{cite journal  | author=Singaraja RR, Brunham LR, Visscher H, ''et al.'' |title=Efflux and atherosclerosis: the clinical and biochemical impact of variations in the ABCA1 gene. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=23 |issue= 8 |pages= 1322-32 |year= 2004 |pmid= 12763760 |doi= 10.1161/01.ATV.0000078520.89539.77 }}
*{{cite journal  | author=Nofer JR, Remaley AT |title=Tangier disease: still more questions than answers. |journal=Cell. Mol. Life Sci. |volume=62 |issue= 19-20 |pages= 2150-60 |year= 2005 |pmid= 16235041 |doi= 10.1007/s00018-005-5125-0 }}
*{{cite journal  | author=Yokoyama S |title=ABCA1 and biogenesis of HDL. |journal=J. Atheroscler. Thromb. |volume=13 |issue= 1 |pages= 1-15 |year= 2006 |pmid= 16505586 |doi=  }}
*{{cite journal  | author=Schmitz G, Schambeck CM |title=Molecular defects in the ABCA1 pathway affect platelet function. |journal=Pathophysiol. Haemost. Thromb. |volume=35 |issue= 1-2 |pages= 166-74 |year= 2006 |pmid= 16855366 |doi= 10.1159/000093563 }}
}}
{{refend}}


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Revision as of 02:01, 31 July 2013

Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]

Synonyms and keywords: CERP; cholesterol efflux regulatory protein

ATP-binding cassette, sub-family A (ABC1), member 1
Identifiers
Symbols ABCA1 ; ABC-1; ABC1; CERP; FLJ14958; HDLDT1; TGD
External IDs Template:OMIM5 Template:MGI HomoloGene: 21130
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Overview

See also: ATP-binding cassette transporter

ATP-binding cassette transporter ABCA1 (member 1 of human transporter sub-family ABCA), also known as the cholesterol efflux regulatory protein (CERP) is a protein which in humans is encoded by the ABCA1 gene.[1] This transporter is a major regulator of cellular cholesterol and phospholipid homeostasis. The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intracellular membranes. ABC genes are divided into seven distinct subfamilies (ABCA, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ABCA subfamily. Members of the ABCA subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes. With cholesterol as its substrate, this protein functions as a cholesterol efflux pump in the cellular lipid removal pathway. Mutations in this gene have been associated with Tangier's disease and familial high-density lipoprotein deficiency.[2]

Tangier Disease

ABCA1 was discovered as the mutation causing Tangier Disease by several groups in 1998. Gerd Schmitz's group in Germany[3] and Michael Hayden's group in British Columbia[4] were using standard genetics techniques and DNA from family pedigrees to locate the mutation. Richard Lawn's group at CV Therapeutics in Palo Alto, CA used cDNA microarrays, which were relatively new at the time, to assess gene expression profiles from cell lines created from normal and effected individuals.[5] They showed cell lines from patients with Tangier's disease showed differential regulation of the ABCA1 gene. Subsequent sequencing of the gene identified the mutations. This group received an award from the American Heart Association for their discovery.[6]

Function

The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intracellular membranes. ABC genes are divided into seven distinct subfamilies (ABCA, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ABCA subfamily. Members of the ABCA subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes. With cholesterol as its substrate, this protein functions as a cholesterol efflux pump in the cellular lipid removal pathway.[7][8]

Physiological role

ABCA1 mediates the efflux of cholesterol and phospholipids to lipid-poor apolipoproteins (apo-A1 and apoE), which then form nascent high-density lipoproteins (HDL). It also mediates the transport of lipids between Golgi and cell membrane. Since this protein is needed throughout the body it is expressed ubiquitously as a 220-kDa protein. It is present in higher quantities in tissues that shuttle or are involved in the turnover of lipids such as the liver, the small intestine and adipose tissue.[9]

Factors that act upon the ABCA1 transporter's expression or its posttranslational modification are also molecules that are involved in its subsequent function like fatty acids, cholesterol and also cytokines and cyclic adenosine monophosphate.[10]

Overexpression of ABCA1 has been reported to induce resistance to the anti-inflammatory, dietary polyphenolic antioxidant Curcumin[11] Downregulation of ABCA1 in senescent macrophages disrupts the cell's ability to remove cholesterol from it's cytosoplasm, leading the cells to promote the pathologic angiogenesis that "plays a central role in common age-associated diseases such as atherosclerosis, cancer, and macular degeneration" [12]

Clinical significance

Mutations in this gene have been associated with Tangier disease and familial high-density lipoprotein deficiency. ABCA1 has been shown to be reduced in Tangier disease which features physiological deficiencies of HDL.[13][14]

Interactions

ABCA1 has been shown to interact with Apolipoprotein A1,[15] FADD,[16] XPC[17] and SNTB2.[18]

References

  1. ↑ Luciani MF, Denizot F, Savary S, Mattei MG, Chimini G (1994). "Cloning of two novel ABC transporters mapping on human chromosome 9". Genomics. 21 (1): 150–9. doi:10.1006/geno.1994.1237. PMID 8088782. Unknown parameter |month= ignored (help)
  2. ↑ "Entrez Gene: ABCA1 ATP-binding cassette, sub-family A (ABC1), member 1".
  3. ↑ Bodzioch M, Orsó E, Klucken J, Langmann T, Böttcher A, Diederich W, Drobnik W, Barlage S, Büchler C, Porsch-Ozcürümez M, Kaminski WE, Hahmann HW, Oette K, Rothe G, Aslanidis C, Lackner KJ, Schmitz G (1999). "The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease". Nature Genetics. 22 (4): 347–51. doi:10.1038/11914. PMID 10431237. Unknown parameter |month= ignored (help)
  4. ↑ Brooks-Wilson A, Marcil M, Clee SM, Zhang LH, Roomp K, van Dam M, Yu L, Brewer C, Collins JA, Molhuizen HO, Loubser O, Ouelette BF, Fichter K, Ashbourne-Excoffon KJ, Sensen CW, Scherer S, Mott S, Denis M, Martindale D, Frohlich J, Morgan K, Koop B, Pimstone S, Kastelein JJ, Genest J, Hayden MR (1999). "Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency". Nature Genetics. 22 (4): 336–45. doi:10.1038/11905. PMID 10431236. Unknown parameter |month= ignored (help)
  5. ↑ Lawn RM, Wade DP, Garvin MR, Wang X, Schwartz K, Porter JG, Seilhamer JJ, Vaughan AM, Oram JF (1999). "The Tangier disease gene product ABC1 controls the cellular apolipoprotein-mediated lipid removal pathway". The Journal of Clinical Investigation. 104 (8): R25–31. doi:10.1172/JCI8119. PMC 481052. PMID 10525055. Unknown parameter |month= ignored (help)
  6. ↑ "American Heart Association Selects CV Therapeutics' Discovery of Role Of 'Good' Cholesterol-Regulating Gene as Top Ten 1999 Research Advances In Heart Disease". PR Newswire Association. 2000-01-03. Retrieved 2009-05-08.
  7. ↑ "Entrez Gene: ABCA1 ATP-binding cassette, sub-family A (ABC1), member 1".
  8. ↑ Schmitz G, Langmann T (2001). "Structure, function and regulation of the ABC1 gene product". Curr. Opin. Lipidol. 12 (2): 129–40. doi:10.1097/00041433-200104000-00006. PMID 11264984. Unknown parameter |month= ignored (help)
  9. ↑ E. M. Wagner, F. Basso, C. S. Kim, M. J. A. Amar, "ABC lipid transporters", in AccessScience@McGraw-Hill
  10. ↑ Yokoyama S (2006). "ABCA1 and biogenesis of HDL". J. Atheroscler. Thromb. 13 (1): 1–15. doi:10.5551/jat.13.1. PMID 16505586. Unknown parameter |month= ignored (help)
  11. ↑ Bachmeier BE, Iancu CM, Killian PH, Kronski E, Mirisola V, Angelini G, Jochum M, Nerlich AG,Pfeffer U. (2009). "Overexpression of the ATP binding cassette gene ABCA1 determines resistance to Curcumin in M14 melanoma cells". Mol Cancer. 8: 129–141. doi:10.1186/1476-4598-8-129. PMC 2804606. PMID 20030852.
  12. ↑ Sene A, Khan AA,; et al. (2013). "Impaired Cholesterol Efflux in Senescent Macrophages Promotes Age-Related Macular Degeneration". Cell Metabolism. 17: 549–561.
  13. ↑ Ordovas JM (2000). "ABC1: the gene for Tangier disease and beyond". Nutr. Rev. 58 (3 Pt 1): 76–9. doi:10.1111/j.1753-4887.2000.tb01843.x. PMID 10812922. Unknown parameter |month= ignored (help)
  14. ↑ Oram JF, Vaughan AM (2000). "ABCA1-mediated transport of cellular cholesterol and phospholipids to HDL apolipoproteins". Curr. Opin. Lipidol. 11 (3): 253–60. doi:10.1097/00041433-200006000-00005. PMID 10882340. Unknown parameter |month= ignored (help)
  15. ↑ Fitzgerald, Michael L (2002). "Naturally occurring mutations in the largest extracellular loops of ABCA1 can disrupt its direct interaction with apolipoprotein A-I". J. Biol. Chem. United States. 277 (36): 33178–87. doi:10.1074/jbc.M204996200. ISSN 0021-9258. PMID 12084722. Unknown parameter |month= ignored (help); Unknown parameter |coauthors= ignored (help)
  16. ↑ Buechler, Christa (2002). "Molecular and functional interaction of the ATP-binding cassette transporter A1 with Fas-associated death domain protein". J. Biol. Chem. United States. 277 (44): 41307–10. doi:10.1074/jbc.C200436200. ISSN 0021-9258. PMID 12235128. Unknown parameter |month= ignored (help); Unknown parameter |coauthors= ignored (help)
  17. ↑ Shimizu, Yuichiro (2003). "Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase". EMBO J. England. 22 (1): 164–73. doi:10.1093/emboj/cdg016. ISSN 0261-4189. PMC 140069. PMID 12505994. Unknown parameter |month= ignored (help); Unknown parameter |coauthors= ignored (help)
  18. ↑ Buechler, Christa (2002). "The carboxyterminus of the ATP-binding cassette transporter A1 interacts with a beta2-syntrophin/utrophin complex". Biochem. Biophys. Res. Commun. United States. 293 (2): 759–65. doi:10.1016/S0006-291X(02)00303-0. ISSN 0006-291X. PMID 12054535. Unknown parameter |month= ignored (help); Unknown parameter |coauthors= ignored (help)

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