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Apolipoprotein

February 15, 2024

Apolipoproteins are proteins that bind lipids (oil-soluble substances such as fats, cholesterol and fat soluble vitamins) to form lipoproteins. They transport lipids in blood, cerebrospinal fluid and lymph.

Apolipoprotein
Apolipoprotein e3 (Apoe3)
Identifiers
SymbolApolipoprotein
PfamPF01442
InterProIPR000074
SCOP21oef / SCOPe / SUPFAM
OPM superfamily172
OPM protein3r2p
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The lipid components of lipoproteins are insoluble in water. However, because of their detergent-like (amphipathic) properties, apolipoproteins and other amphipathic molecules (such as phospholipids) can surround the lipids, creating a lipoprotein particle that is itself water-soluble, and can thus be carried through body fluids (i.e., blood, lymph).

In addition to stabilizing lipoprotein structure and solubilizing the lipid component, apolipoproteins interact with lipoprotein receptors and lipid transport proteins, thereby participating in lipoprotein uptake and clearance. They also serve as enzyme cofactors for specific enzymes involved in the metabolism of lipoproteins.[1]

Apolipoproteins are also exploited by hepatitis C virus (HCV) to enable virus entry, assembly, and transmission. They play a role in viral pathogenesis and viral evasion from neutralizing antibodies.[2]

Functions edit

In lipid transport, apolipoproteins function as structural components of lipoprotein particles, ligands for cell-surface receptors and lipid transport proteins, and cofactors for enzymes (e.g. apolipoprotein C-II for lipoprotein lipase and apolipoprotein A-I (apoA1) for lecithin-cholesterol acyltransferase).[citation needed]

Different lipoproteins contain different classes of apolipoproteins, which influence their function.

Apolipoprotein A-I (apoA1) is the major structural protein component of high-density lipoproteins (HDL), although it is present in other lipoproteins in smaller amounts.[3] Apolipoprotein A-IV (apoA4) is present in chylomicrons, very-low-density lipoproteins (VLDL), and HDL. It is thought to act primarily in reverse cholesterol transport[4] and intestinal lipid absorption via chylomicron assembly and secretion. ApoA-IV synthesized in hypothalamus is suggested to be a satiating factor which regulate the food intake of the rodent.[5][1]

Apolipoprotein B plays a particularly important role in lipoprotein transport being the primary organizing protein of many lipoproteins.[1]

Apolipoprotein C-III (apoC3) plays an important role in lipid metabolism specific in regulating the metabolism of triglyceride-rich lipoproteins (TRLs).[6]

Apolipoprotein D (apoD) is a soluble carrier protein of lipophilic molecules in neurons and glial cells within the central and peripheral nervous system and apoD can also modulate the stability and oxidation status of these molecules.[7]

Apolipoprotein E (apoE) plays an important role in the transport and uptake of cholesterol by way of its high affinity interaction with lipoprotein receptors, including the low-density lipoprotein (LDL) receptor. ApoE is the major lipoprotein in the central nervous system. Recent findings with apoA1 and apoE suggest that the tertiary structures of these two members of the human exchangeable apolipoprotein gene family are related.[8] The three-dimensional structure of the LDL receptor-binding domain of apoE indicates that the protein forms an unusually elongated four-helix bundle that may be stabilised by a tightly packed hydrophobic core that includes leucine zipper-type interactions and by numerous salt bridges on the mostly charged surface. Basic amino acids important for LDL receptor binding are clustered into a surface patch on one long helix.[9]

Apolipoprotein F (apoF) is one of the minor apolipoprotein in blood plasma and it is a lipid transfer inhibit protein to inhibit cholesteryl ester transfer protein-mediated transfers of cholesteryl esters and triglycerides.[10][11]

Apolipoprotein M (apoM) participates in the lipid metabolism and exhibit anti‑atherosclerotic functions and it is presented in high-density lipoprotein (HDL), low-density lipoprotein (LDL) and very low-density lipoprotein (VLDL).[12]

Classes edit

There are multiple classes of apolipoproteins and several sub-classes:

Exchangeable apolipoproteins (apoA, apoC, and apoE) have the same genomic structure and are members of a multi-gene family that probably evolved from a common ancestral gene. Apo-AI and ApoA4 are part of the APOA1/C3/A4/A5 gene cluster on chromosome 11.[14]

Hundreds of genetic polymorphisms of the apolipoproteins have been described, and many of them alter their structure and function.

Evolution edit

The cluster of exchangeable apoliproteins is well conserved in vertebrates.[15] The family diversified by duplication, with the ancestral gene most similar to ApoC1.[16]

Beyond vertebrates, proteins similar to the exchangeable ApoA/C/E and the nonexchangable Apo-B are found in a wide range of animals and choanoflagellates. This suggests that the ancestral animal already has both kinds of apolipoproteins. In arthropods in particular, diacylglycerol-carrying apolipoproteins are known as apolipophorins, with the ApoA/C/E-like one known as apolipophorin III and the Apo-B like one known as apolipophorin I/II.[16]

Synthesis and regulation edit

Apolipoprotein synthesis in the intestine is regulated principally by the fat content of the diet.

Apolipoprotein synthesis in the liver is controlled by a host of factors, including dietary composition, hormones (insulin, glucagon, thyroxin, estrogens, androgens), alcohol intake, and various drugs (statins, niacin, and fibric acids). ApoB is an integral apoprotein whereas the others are peripheral apoproteins.

Apolipoprotein synthesis such as ApoA4 in hypothalamus involves in the integration of signals for regulation of food intake[5] which is regulated by vagal nerve and cholecystokinin.[17]

Disease edit

Apolipoprotein has been suggested to be implicated in several types of diseases and dysfunction.

ApoC1 level increases in neuropathic pain and fibromyalgia patients which suggest it plays an important role in occurrence of these conditions.[18]

ApoC3 is a risk factor of cardiovascular disease. Accumulation of plasma TRLs caused by elevated apoC-III leading to hypertriglyceridaemia.[19]

ApoD level increases in nervous system with a large number of neurologic disorders inclusive of Alzheimer's disease, schizophrenia, and stroke.[7]

ApoE has been implicated in dementia and Alzheimer's disease.[20]

Apo(a) is a component of lipoprotein(a) (Lp(a)) and elevated plasma Lp(a) level is a heritable, independent, and possibly causal risk factor for Atherosclerotic Cardiovascular Disease (ASCVD).[21] The cholesterol-rich apoB-containing lipoproteins also participate in the pathogenesis of ASCVD.

References edit

  1. ^ a b Either roman numerals or arabic numbers may be used for gene family members. For example, apoA5 is also known as apo A-V.
  2. ^ Isoforms from the same gene by alternative splicing.
  1. ^ a b c Ramasamy I (December 2014). "Recent advances in physiological lipoprotein metabolism". Clinical Chemistry and Laboratory Medicine. 52 (12): 1695–727. doi:10.1515/cclm-2013-0358. PMID 23940067. S2CID 6925754.
  2. ^ Wrensch F, Crouchet E, Ligat G, Zeisel MB, Keck ZY, Foung SK, et al. (2018). "Hepatitis C Virus (HCV)-Apolipoprotein Interactions and Immune Evasion and Their Impact on HCV Vaccine Design". Frontiers in Immunology. 9: 1436. doi:10.3389/fimmu.2018.01436. PMC 6021501. PMID 29977246.
  3. ^ von Zychlinski A, Williams M, McCormick S, Kleffmann T (June 2014). "Absolute quantification of apolipoproteins and associated proteins on human plasma lipoproteins". Journal of Proteomics. 106: 181–90. doi:10.1016/j.jprot.2014.04.030. PMID 24780726.
  4. ^ Steinmetz A, Barbaras R, Ghalim N, Clavey V, Fruchart JC, Ailhaud G (May 1990). "Human apolipoprotein A-IV binds to apolipoprotein A-I/A-II receptor sites and promotes cholesterol efflux from adipose cells". The Journal of Biological Chemistry. 265 (14): 7859–63. doi:10.1016/S0021-9258(19)39010-6. PMID 2159462.
  5. ^ a b Liu M, Doi T, Shen L, Woods SC, Seeley RJ, Zheng S, et al. (May 2001). "Intestinal satiety protein apolipoprotein AIV is synthesized and regulated in rat hypothalamus". American Journal of Physiology. Regulatory, Integrative and Comparative Physiology. 280 (5): R1382-7. doi:10.1152/ajpregu.2001.280.5.R1382. PMID 11294757.
  6. ^ Ooi EM, Barrett PH, Chan DC, Watts GF (May 2008). "Apolipoprotein C-III: understanding an emerging cardiovascular risk factor". Clinical Science. 114 (10): 611–24. doi:10.1042/CS20070308. PMID 18399797.
  7. ^ a b Dassati S, Waldner A, Schweigreiter R (July 2014). "Apolipoprotein D takes center stage in the stress response of the aging and degenerative brain". Neurobiology of Aging. 35 (7): 1632–42. doi:10.1016/j.neurobiolaging.2014.01.148. PMC 3988949. PMID 24612673.
  8. ^ Saito H, Lund-Katz S, Phillips MC (July 2004). "Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins". Progress in Lipid Research. 43 (4): 350–80. doi:10.1016/j.plipres.2004.05.002. PMID 15234552.
  9. ^ Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA (June 1991). "Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E". Science. 252 (5014): 1817–22. Bibcode:1991Sci...252.1817W. doi:10.1126/science.2063194. PMID 2063194.
  10. ^ Wang X, Driscoll DM, Morton RE (January 1999). "Molecular cloning and expression of lipid transfer inhibitor protein reveals its identity with apolipoprotein F". The Journal of Biological Chemistry. 274 (3): 1814–20. doi:10.1074/jbc.274.3.1814. PMID 9880564.
  11. ^ Koren E, McConathy WJ, Alaupovic P (October 1982). "Isolation and characterization of simple and complex lipoproteins containing apolipoprotein F from human plasma". Biochemistry. 21 (21): 5347–51. doi:10.1021/bi00264a035. PMID 6816269.
  12. ^ Huang LZ, Gao JL, Pu C, Zhang PH, Wang LZ, Feng G, Zhang Y (August 2015). "Apolipoprotein M: Research progress, regulation and metabolic functions (Review)". Molecular Medicine Reports. 12 (2): 1617–24. doi:10.3892/mmr.2015.3658. PMID 25901639.
  13. ^ Ağar C, de Groot PG, Levels JH, Marquart JA, Meijers JC (January 2009). "Beta2-glycoprotein I is incorrectly named apolipoprotein H". Journal of Thrombosis and Haemostasis. 7 (1): 235–6. doi:10.1111/j.1538-7836.2008.03223.x. PMID 19017258. S2CID 43329586.
  14. ^ Fullerton SM, Buchanan AV, Sonpar VA, Taylor SL, Smith JD, Carlson CS, et al. (June 2004). "The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster". Human Genetics. 115 (1): 36–56. doi:10.1007/s00439-004-1106-x. PMID 15108119. S2CID 24857340.
  15. ^ Babin PJ, Thisse C, Durliat M, Andre M, Akimenko MA, Thisse B (August 1997). "Both apolipoprotein E and A-I genes are present in a nonmammalian vertebrate and are highly expressed during embryonic development". Proceedings of the National Academy of Sciences of the United States of America. 94 (16): 8622–7. Bibcode:1997PNAS...94.8622B. doi:10.1073/pnas.94.16.8622. PMC 23048. PMID 9238027.
  16. ^ a b Huebbe P, Rimbach G (August 2017). "Evolution of human apolipoprotein E (APOE) isoforms: Gene structure, protein function and interaction with dietary factors". Ageing Research Reviews. 37: 146–161. doi:10.1016/j.arr.2017.06.002. PMID 28647612. S2CID 3758905.
  17. ^ Lo CC, Langhans W, Georgievsky M, Arnold M, Caldwell JL, Cheng S, et al. (December 2012). "Apolipoprotein AIV requires cholecystokinin and vagal nerves to suppress food intake". Endocrinology. 153 (12): 5857–65. doi:10.1210/en.2012-1427. PMC 3512075. PMID 23027805.
  18. ^ Lind, Anne-Li; Just, David; Mikus, Maria; Fredolini, Claudia; Ioannou, Marina; Gerdle, Björn; Ghafouri, Bijar; Bäckryd, Emmanuel; Tanum, Lars (2019-10-15). "CSF levels of apolipoprotein C1 and autotaxin found to associate with neuropathic pain and fibromyalgia". Journal of Pain Research. 12: 2875–2889. doi:10.2147/jpr.s215348. PMC 6800548. PMID 31686904.
  19. ^ Chan DC, Chen MM, Ooi EM, Watts GF (May 2008). "An ABC of apolipoprotein C-III: a clinically useful new cardiovascular risk factor?". International Journal of Clinical Practice. 62 (5): 799–809. doi:10.1111/j.1742-1241.2007.01678.x. PMID 18201179. S2CID 34553066.
  20. ^ Chang TY, Yamauchi Y, Hasan MT, Chang C (December 2017). "Cellular cholesterol homeostasis and Alzheimer's disease". Journal of Lipid Research. 58 (12): 2239–2254. doi:10.1194/jlr.R075630. PMC 5711498. PMID 28298292.
  21. ^ Wu MF, Xu KZ, Guo YG, Yu J, Wu Y, Lin LM (October 2019). "Lipoprotein(a) and Atherosclerotic Cardiovascular Disease: Current Understanding and Future Perspectives". Cardiovascular Drugs and Therapy. 33 (6): 739–748. doi:10.1007/s10557-019-06906-9. PMID 31655942. S2CID 204886420.

External links edit

  • HuGENet Review
  • Apolipoprotein AI Mutations and Information
  • Apolipoproteins. Apo A1, B, C2. Apolipoproteins information
This article incorporates text from the public domain Pfam and InterPro: IPR000074

February 15, 2024
apolipoprotein, proteins, that, bind, lipids, soluble, substances, such, fats, cholesterol, soluble, vitamins, form, lipoproteins, they, transport, lipids, blood, cerebrospinal, fluid, lymph, apoe3, identifierssymbolpfampf01442interproipr000074scop21oef, scope. Apolipoproteins are proteins that bind lipids oil soluble substances such as fats cholesterol and fat soluble vitamins to form lipoproteins They transport lipids in blood cerebrospinal fluid and lymph ApolipoproteinApolipoprotein e3 Apoe3 IdentifiersSymbolApolipoproteinPfamPF01442InterProIPR000074SCOP21oef SCOPe SUPFAMOPM superfamily172OPM protein3r2pAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryThe lipid components of lipoproteins are insoluble in water However because of their detergent like amphipathic properties apolipoproteins and other amphipathic molecules such as phospholipids can surround the lipids creating a lipoprotein particle that is itself water soluble and can thus be carried through body fluids i e blood lymph In addition to stabilizing lipoprotein structure and solubilizing the lipid component apolipoproteins interact with lipoprotein receptors and lipid transport proteins thereby participating in lipoprotein uptake and clearance They also serve as enzyme cofactors for specific enzymes involved in the metabolism of lipoproteins 1 Apolipoproteins are also exploited by hepatitis C virus HCV to enable virus entry assembly and transmission They play a role in viral pathogenesis and viral evasion from neutralizing antibodies 2 Contents 1 Functions 2 Classes 2 1 Evolution 3 Synthesis and regulation 4 Disease 5 References 6 External linksFunctions editIn lipid transport apolipoproteins function as structural components of lipoprotein particles ligands for cell surface receptors and lipid transport proteins and cofactors for enzymes e g apolipoprotein C II for lipoprotein lipase and apolipoprotein A I apoA1 for lecithin cholesterol acyltransferase citation needed Different lipoproteins contain different classes of apolipoproteins which influence their function Apolipoprotein A I apoA1 is the major structural protein component of high density lipoproteins HDL although it is present in other lipoproteins in smaller amounts 3 Apolipoprotein A IV apoA4 is present in chylomicrons very low density lipoproteins VLDL and HDL It is thought to act primarily in reverse cholesterol transport 4 and intestinal lipid absorption via chylomicron assembly and secretion ApoA IV synthesized in hypothalamus is suggested to be a satiating factor which regulate the food intake of the rodent 5 1 Apolipoprotein B plays a particularly important role in lipoprotein transport being the primary organizing protein of many lipoproteins 1 Apolipoprotein C III apoC3 plays an important role in lipid metabolism specific in regulating the metabolism of triglyceride rich lipoproteins TRLs 6 Apolipoprotein D apoD is a soluble carrier protein of lipophilic molecules in neurons and glial cells within the central and peripheral nervous system and apoD can also modulate the stability and oxidation status of these molecules 7 Apolipoprotein E apoE plays an important role in the transport and uptake of cholesterol by way of its high affinity interaction with lipoprotein receptors including the low density lipoprotein LDL receptor ApoE is the major lipoprotein in the central nervous system Recent findings with apoA1 and apoE suggest that the tertiary structures of these two members of the human exchangeable apolipoprotein gene family are related 8 The three dimensional structure of the LDL receptor binding domain of apoE indicates that the protein forms an unusually elongated four helix bundle that may be stabilised by a tightly packed hydrophobic core that includes leucine zipper type interactions and by numerous salt bridges on the mostly charged surface Basic amino acids important for LDL receptor binding are clustered into a surface patch on one long helix 9 Apolipoprotein F apoF is one of the minor apolipoprotein in blood plasma and it is a lipid transfer inhibit protein to inhibit cholesteryl ester transfer protein mediated transfers of cholesteryl esters and triglycerides 10 11 Apolipoprotein M apoM participates in the lipid metabolism and exhibit anti atherosclerotic functions and it is presented in high density lipoprotein HDL low density lipoprotein LDL and very low density lipoprotein VLDL 12 Classes editThere are multiple classes of apolipoproteins and several sub classes Apolipoprotein A Apo AI Apo A2 Apo A4 and Apo A5 a Apolipoprotein B Apo B48 and Apo B 100 b Apolipoprotein C ApoC I apo ApoC II apo ApoC III and ApoC IV a Apolipoprotein D Apolipoprotein E Apolipoprotein F Apolipoprotein H a misnomer 13 Apolipoprotein L Apolipoprotein M Apolipoprotein a Exchangeable apolipoproteins apoA apoC and apoE have the same genomic structure and are members of a multi gene family that probably evolved from a common ancestral gene Apo AI and ApoA4 are part of the APOA1 C3 A4 A5 gene cluster on chromosome 11 14 Hundreds of genetic polymorphisms of the apolipoproteins have been described and many of them alter their structure and function Evolution edit The cluster of exchangeable apoliproteins is well conserved in vertebrates 15 The family diversified by duplication with the ancestral gene most similar to ApoC1 16 Beyond vertebrates proteins similar to the exchangeable ApoA C E and the nonexchangable Apo B are found in a wide range of animals and choanoflagellates This suggests that the ancestral animal already has both kinds of apolipoproteins In arthropods in particular diacylglycerol carrying apolipoproteins are known as apolipophorins with the ApoA C E like one known as apolipophorin III and the Apo B like one known as apolipophorin I II 16 Synthesis and regulation editApolipoprotein synthesis in the intestine is regulated principally by the fat content of the diet Apolipoprotein synthesis in the liver is controlled by a host of factors including dietary composition hormones insulin glucagon thyroxin estrogens androgens alcohol intake and various drugs statins niacin and fibric acids ApoB is an integral apoprotein whereas the others are peripheral apoproteins Apolipoprotein synthesis such as ApoA4 in hypothalamus involves in the integration of signals for regulation of food intake 5 which is regulated by vagal nerve and cholecystokinin 17 Disease editApolipoprotein has been suggested to be implicated in several types of diseases and dysfunction ApoC1 level increases in neuropathic pain and fibromyalgia patients which suggest it plays an important role in occurrence of these conditions 18 ApoC3 is a risk factor of cardiovascular disease Accumulation of plasma TRLs caused by elevated apoC III leading to hypertriglyceridaemia 19 ApoD level increases in nervous system with a large number of neurologic disorders inclusive of Alzheimer s disease schizophrenia and stroke 7 ApoE has been implicated in dementia and Alzheimer s disease 20 Apo a is a component of lipoprotein a Lp a and elevated plasma Lp a level is a heritable independent and possibly causal risk factor for Atherosclerotic Cardiovascular Disease ASCVD 21 The cholesterol rich apoB containing lipoproteins also participate in the pathogenesis of ASCVD References edit a b Either roman numerals or arabic numbers may be used for gene family members For example apoA5 is also known as apo A V Isoforms from the same gene by alternative splicing a b c Ramasamy I December 2014 Recent advances in physiological lipoprotein metabolism Clinical Chemistry and Laboratory Medicine 52 12 1695 727 doi 10 1515 cclm 2013 0358 PMID 23940067 S2CID 6925754 Wrensch F Crouchet E Ligat G Zeisel MB Keck ZY Foung SK et al 2018 Hepatitis C Virus HCV Apolipoprotein Interactions and Immune Evasion and Their Impact on HCV Vaccine Design Frontiers in Immunology 9 1436 doi 10 3389 fimmu 2018 01436 PMC 6021501 PMID 29977246 von Zychlinski A Williams M McCormick S Kleffmann T June 2014 Absolute quantification of apolipoproteins and associated proteins on human plasma lipoproteins Journal of Proteomics 106 181 90 doi 10 1016 j jprot 2014 04 030 PMID 24780726 Steinmetz A Barbaras R Ghalim N Clavey V Fruchart JC Ailhaud G May 1990 Human apolipoprotein A IV binds to apolipoprotein A I A II receptor sites and promotes cholesterol efflux from adipose cells The Journal of Biological Chemistry 265 14 7859 63 doi 10 1016 S0021 9258 19 39010 6 PMID 2159462 a b Liu M Doi T Shen L Woods SC Seeley RJ Zheng S et al May 2001 Intestinal satiety protein apolipoprotein AIV is synthesized and regulated in rat hypothalamus American Journal of Physiology Regulatory Integrative and Comparative Physiology 280 5 R1382 7 doi 10 1152 ajpregu 2001 280 5 R1382 PMID 11294757 Ooi EM Barrett PH Chan DC Watts GF May 2008 Apolipoprotein C III understanding an emerging cardiovascular risk factor Clinical Science 114 10 611 24 doi 10 1042 CS20070308 PMID 18399797 a b Dassati S Waldner A Schweigreiter R July 2014 Apolipoprotein D takes center stage in the stress response of the aging and degenerative brain Neurobiology of Aging 35 7 1632 42 doi 10 1016 j neurobiolaging 2014 01 148 PMC 3988949 PMID 24612673 Saito H Lund Katz S Phillips MC July 2004 Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins Progress in Lipid Research 43 4 350 80 doi 10 1016 j plipres 2004 05 002 PMID 15234552 Wilson C Wardell MR Weisgraber KH Mahley RW Agard DA June 1991 Three dimensional structure of the LDL receptor binding domain of human apolipoprotein E Science 252 5014 1817 22 Bibcode 1991Sci 252 1817W doi 10 1126 science 2063194 PMID 2063194 Wang X Driscoll DM Morton RE January 1999 Molecular cloning and expression of lipid transfer inhibitor protein reveals its identity with apolipoprotein F The Journal of Biological Chemistry 274 3 1814 20 doi 10 1074 jbc 274 3 1814 PMID 9880564 Koren E McConathy WJ Alaupovic P October 1982 Isolation and characterization of simple and complex lipoproteins containing apolipoprotein F from human plasma Biochemistry 21 21 5347 51 doi 10 1021 bi00264a035 PMID 6816269 Huang LZ Gao JL Pu C Zhang PH Wang LZ Feng G Zhang Y August 2015 Apolipoprotein M Research progress regulation and metabolic functions Review Molecular Medicine Reports 12 2 1617 24 doi 10 3892 mmr 2015 3658 PMID 25901639 Agar C de Groot PG Levels JH Marquart JA Meijers JC January 2009 Beta2 glycoprotein I is incorrectly named apolipoprotein H Journal of Thrombosis and Haemostasis 7 1 235 6 doi 10 1111 j 1538 7836 2008 03223 x PMID 19017258 S2CID 43329586 Fullerton SM Buchanan AV Sonpar VA Taylor SL Smith JD Carlson CS et al June 2004 The effects of scale variation in the APOA1 C3 A4 A5 gene cluster Human Genetics 115 1 36 56 doi 10 1007 s00439 004 1106 x PMID 15108119 S2CID 24857340 Babin PJ Thisse C Durliat M Andre M Akimenko MA Thisse B August 1997 Both apolipoprotein E and A I genes are present in a nonmammalian vertebrate and are highly expressed during embryonic development Proceedings of the National Academy of Sciences of the United States of America 94 16 8622 7 Bibcode 1997PNAS 94 8622B doi 10 1073 pnas 94 16 8622 PMC 23048 PMID 9238027 a b Huebbe P Rimbach G August 2017 Evolution of human apolipoprotein E APOE isoforms Gene structure protein function and interaction with dietary factors Ageing Research Reviews 37 146 161 doi 10 1016 j arr 2017 06 002 PMID 28647612 S2CID 3758905 Lo CC Langhans W Georgievsky M Arnold M Caldwell JL Cheng S et al December 2012 Apolipoprotein AIV requires cholecystokinin and vagal nerves to suppress food intake Endocrinology 153 12 5857 65 doi 10 1210 en 2012 1427 PMC 3512075 PMID 23027805 Lind Anne Li Just David Mikus Maria Fredolini Claudia Ioannou Marina Gerdle Bjorn Ghafouri Bijar Backryd Emmanuel Tanum Lars 2019 10 15 CSF levels of apolipoprotein C1 and autotaxin found to associate with neuropathic pain and fibromyalgia Journal of Pain Research 12 2875 2889 doi 10 2147 jpr s215348 PMC 6800548 PMID 31686904 Chan DC Chen MM Ooi EM Watts GF May 2008 An ABC of apolipoprotein C III a clinically useful new cardiovascular risk factor International Journal of Clinical Practice 62 5 799 809 doi 10 1111 j 1742 1241 2007 01678 x PMID 18201179 S2CID 34553066 Chang TY Yamauchi Y Hasan MT Chang C December 2017 Cellular cholesterol homeostasis and Alzheimer s disease Journal of Lipid Research 58 12 2239 2254 doi 10 1194 jlr R075630 PMC 5711498 PMID 28298292 Wu MF Xu KZ Guo YG Yu J Wu Y Lin LM October 2019 Lipoprotein a and Atherosclerotic Cardiovascular Disease Current Understanding and Future Perspectives Cardiovascular Drugs and Therapy 33 6 739 748 doi 10 1007 s10557 019 06906 9 PMID 31655942 S2CID 204886420 External links editHuGENet Review Apolipoprotein AI Mutations and Information Apolipoproteins Apo A1 B C2 Apolipoproteins information This article incorporates text from the public domain Pfam and InterPro IPR000074 Retrieved from https en wikipedia org w index php title Apolipoprotein amp oldid 1189311682, wikipedia, wiki, book, books, library,

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