同: apolipoprotein

同: apolipoprotein

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/03/20 16:56:05」(JST)

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Apolipoproteins are proteins that bind lipids (oil-soluble substances such as fat and cholesterol) to form lipoproteins. They transport the lipids through the lymphatic and circulatory systems.

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 the lipoprotein particle that is itself water-soluble, and can thus be carried through water-based circulation (i.e., blood, lymph).

Apolipoproteins also serve as enzyme cofactors, receptor ligands, and lipid transfer carriers that regulate the metabolism of lipoproteins and their uptake in tissues.

Functions[edit]

In lipid transport, apolipoproteins function as structural components of lipoprotein particles, cofactors for enzymes and ligands for cell-surface receptors. In particular, apoA1 is the major protein component of high-density lipoproteins; apoA4 is thought to act primarily in intestinal lipid absorption. Further, apoE is a blood plasma protein that mediates the transport and uptake of cholesterol and lipid by way of its high affinity interaction with different cellular receptors, including the low-density lipoprotein (LDL) receptor. Recent findings with apoA1 and apoE suggest that the tertiary structures of these two members of the human exchangeable apolipoprotein gene family are related.^[1] 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.^[2]

They are enzyme coenzymes (C-II for lipoprotein lipase and A-I for lecithin-cholesterol acyltransferase)
Lipid transport proteins
Ligands for interaction with lipoprotein receptors in tissues ( apoB100 and apoE for LDL-receptors, apoA-I for HDL receptors)

Classes[edit]

There are two major types of apolipoproteins. Apolipoproteins B form low-density lipoprotein ("bad cholesterol") particles. These proteins have mostly beta-sheet structure and associate with lipid droplets irreversibly. Other apolipoproteins form high-density lipoprotein ("good cholesterol") particles. These proteins consist of alpha-helices and associate with lipid droplets reversibly. During binding to the lipid particles these proteins change their three-dimensional structure.

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

A (apo A-I, apo A-II, apo A-IV, and apo A-V)
B (apo B48 and apo B100)
C (apo C-I, apo C-II, apo C-III, and apo C-IV)
D
E
H

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. ApoA1 and ApoA4 are part of the APOA1/C3/A4/A5 gene cluster on chromosome 11.^[3]

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

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). Apo B is an integral apoprotein whereas the others are peripheral apoproteins.

References[edit]

^ Saito H, Lund-Katz S, Phillips MC (July 2004). "Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins". Prog. Lipid Res. 43 (4): 350–80. doi:10.1016/j.plipres.2004.05.002. PMID 15234552.
^ Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA; Wardell; Weisgraber; Mahley; Agard (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.
^ Fullerton SM, Buchanan AV, Sonpar VA, Taylor SL, Smith JD, Carlson CS, Salomaa V, StengÃ¥rd JH, Boerwinkle E, Clark AG, Nickerson DA, Weiss KM (June 2004). "The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster". Hum. Genet. 115 (1): 36–56. doi:10.1007/s00439-004-1106-x. PMID 15108119.

External links[edit]

HuGENet Review
Apolipoprotein AI Mutations and Information

This article incorporates text from the public domain Pfam and InterPro IPR000074

UpToDate Contents

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English Journal

The evolution of apolipoprotein B and its mRNA editing complex. Does the lack of editing contribute to hypertriglyceridemia?

Damsteegt EL1, Davie A2, Lokman PM3.
Gene.Gene.2018 Jan 30;641:46-54. doi: 10.1016/j.gene.2017.10.024. Epub 2017 Oct 12.
PMID 29031774

Serum lipid, lipoprotein and apolipoprotein profiles in workers exposed to low arsenic levels: Lipid profiles and occupational arsenic exposure.

Ledda C1, Iavicoli I2, Bracci M3, Avola R4, Senia P5, Santarelli L3, Pomara C6, Rapisarda V5.
Toxicology letters.Toxicol Lett.2018 Jan 5;282:49-56. doi: 10.1016/j.toxlet.2017.10.014. Epub 2017 Oct 18.
PMID 29054558

Mitochondria-targeted esculetin inhibits PAI-1 levels by modulating STAT3 activation and miR-19b via SIRT3: Role in acute coronary artery syndrome.

Katta S1, Karnewar S1,2, Panuganti D1, Jerald MK3, Sastry BKS4, Kotamraju S1,2.
Journal of cellular physiology.J Cell Physiol.2018 Jan;233(1):214-225. doi: 10.1002/jcp.25865. Epub 2017 May 3.
PMID 28213977

Japanese Journal

Intercorrelations of lipoprotein subfractions and their covariation with lifestyle factors in healthy men

Parlesak Alexandr,Eckoldt Joachim,Winkler Karl,Bode Christian J,Schäfer Christian
Journal of Clinical Biochemistry and Nutrition 54(3), 174-180, 2014
… In the current study, we measured the correlations among physical activity, nutrient intake, smoking, body-mass index (BMI), and age with the concentration of triglycerides, cholesterol, phospholipids, and apolipoproteins (ApoA1, ApoA2 and ApoB) in subfractions of LDL and HDL in 265 healthy working men. …
NAID 130004466750

Relationship of Body Mass Index with High-Density Lipoprotein Cholesterol in Well-Trained Collegiate Male Athletes

ODA Kazuto,MASUDA Reika,IIDE Kazuhide,MIYAMOTO Noriko,MIYAHARA Keiko,KOJIMA Namie,MATSUO Kayoko,YOSHIMURA Yoshitaka,MIZUNO Shuichi,IMAMURA Hiroyuki
総合健診 40(4), 464-467, 2013
… Also, the High Group showed significantly lower apolipoproteins (apo) A-I than the Low Group. …
NAID 130004562616

Relationships between the Visceral Fat Area on CT and Coronary Risk Factor Markers

Shiina Yutaka,Homma Yasuhiko
Internal Medicine 52(16), 1775-1780, 2013
… Measuring the levels of apolipoproteins in addition to lipoproteins during health screening is therefore useful for evaluating of atherogenicity. …
NAID 130003365762

Related Pictures

Apolipoproteins B; Apo-B Apolipoprotein B to Apolipoprotein A1 Ratio as a Risk Factor for Cardiovascular Disease | Lipoprotein Metabolism And Disorders - ppt video online download Apolipoproteins - LabCE.com, Laboratory Continuing Education Literature References on Apolipoproteins

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関連記事	「apolipoprotein」

「apolipoprotein」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Apolipoprotein
	; apolipoprotein e3 (apoe3)
Identifiers
Symbol	Apolipoprotein
Pfam	PF01442
InterPro	IPR000074
SCOP	1oef
SUPERFAMILY	1oef
OPM superfamily	193
OPM protein	3r2p
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

　　[★]

アポリポタンパク質、アポリポ蛋白質、アポリポタンパク、アポリポ蛋白、アポリポプロテイン

関: apo

[pmid15234552-1] Saito H, Lund-Katz S, Phillips MC (July 2004). "Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins". Prog. Lipid Res. 43 (4): 350–80. doi:10.1016/j.plipres.2004.05.002. PMID 15234552.

[pmid2063194-2] Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA; Wardell; Weisgraber; Mahley; Agard (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.

[pmid15108119-3] Fullerton SM, Buchanan AV, Sonpar VA, Taylor SL, Smith JD, Carlson CS, Salomaa V, StengÃ¥rd JH, Boerwinkle E, Clark AG, Nickerson DA, Weiss KM (June 2004). "The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster". Hum. Genet. 115 (1): 36–56. doi:10.1007/s00439-004-1106-x. PMID 15108119.

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apolipoproteins