Lp(a)

リポ蛋白(a)

WordNet

1. the 1st letter of the Roman alphabet (同)a
2. the blood group whose red cells carry the A antigen (同)type_A, group A
3. a long-playing phonograph record; designed to be played at 33.3 rpm (同)L-P
4. the 12th letter of the Roman alphabet (同)l
5. a public promotion of some product or service (同)advertisement, advertizement, advertising, advertizing, advert

PrepTutorEJDIC

1. (…と)『同じくらい』,『同様に』 / 《比較》『…ほど』,『…くらい』,…ように / 《様態・程度》『…のように』,…と同じように / 《時》『…のときに』(when);…の間に,…するうちに(while) / 《話》《原因・理由》『…だから』,…なので / 《譲歩》《文》…だけれども(though) / 《先行する名詞の内容を制限して》『…のような』 / 《先行の,または後続の節の内容を受けて》『それは…だが』,…のように / 《役割・資格・機能などを表して》『…として』 / 《seem,appear,consider,pass,regard,treat,know,think of などの動詞の後で補語の働きをする語の前に置いて》…と[して] / 《前置詞・形容詞・分詞などの前に置いてその意味を限定して》…として[の],…とみなして,…と考えて / たとえば(for instance)
2. answer / ampere
3. エルピーレコード(1分間331/3回転のレコード;商標名)
4. lira(イタリアの貨幣単位リラ)
5. 《話》広告(advertisementの略)

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/01/30 08:10:43」(JST)

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LPA
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 1I71, 1JFN, 1KIV, 2FEB, 4BV5, 4BV7, 4BVC, 4BVD, 4BVV, 4BVW, 3KIV, 4KIV
Identifiers
Aliases	LPA, AK38, APOA, LP, Lipoprotein(a)
External IDs	HomoloGene: 87856 GeneCards: LPA
Genetically Related Diseases
coronary artery disease
Gene ontology Molecular function • fibronectin binding • apolipoprotein binding • peptidase activity • endopeptidase inhibitor activity • heparin binding • serine-type endopeptidase activity • serine-type peptidase activity • protein binding • hydrolase activity Cellular component • extracellular region • plasma lipoprotein particle Biological process • lipoprotein metabolic process • lipid transport • blood circulation • proteolysis • lipid metabolic process • transport • negative regulation of endopeptidase activity Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4018	n/a
Ensembl	ENSG00000198670	n/a
UniProt	P08519	n/a
RefSeq (mRNA)	NM_005577	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	Chr 6: 160.53 – 160.66 Mb	n/a
PubMed search		n/a
Wikidata
View/Edit Human

Lipoprotein(a) (also called Lp(a) or LPA) is a lipoprotein subclass. Genetic studies and numerous epidemiologic studies have identified Lp(a) as a risk factor for atherosclerotic diseases such as coronary heart disease and stroke.

Lipoprotein(a) was discovered in 1963 by Kåre Berg and the human gene encoding apolipoprotein(a) was cloned in 1987.

Structure

Lipoprotein(a) [Lp(a)] consists of an LDL-like particle and the specific apolipoprotein(a) [apo(a)], which is covalently bound to the apoB of the LDL like particle. Lp(a) plasma concentrations are highly heritable and mainly controlled by the apolipoprotein(a) gene [LPA] located on chromosome 6q26-27. Apo(a) proteins vary in size due to a size polymorphism [KIV-2 VNTR], which is caused by a variable number of so-called kringle IV repeats in the LPA gene. This size variation at the gene level is expressed on the protein level as well, resulting in apo(a) proteins with 10 to > 50 kringle IV repeats (each of the variable kringle IV consists of 114 amino acids). These variable apo(a) sizes are known as "apo(a) isoforms". There is a general inverse correlation between the size of the apo(a) isoform and the Lp(a) plasma concentration One theory for the size/plasma level correlation involves difference rates of protein synthesis. There appears to be a relationship between the number of kringle repeats and the processing time of the precursor apo (a) protein. That is, the larger the isoform, the more apo(a) precursor protein accumulates intracellularly in the endoplasmic reticulum. Lipoprotein (a) is not fully synthesized until the precursor protein is released from the cell, so the slower rate of production for the larger isoforms limits the plasma concentration.

Apo(a) is expressed by liver cells (hepatocytes), and the assembly of apo(a) and LDL particles seems to take place at the outer hepatocyte surface. The half-life of Lp(a) in the circulation is about 3 to 4 days.

Catabolism and clearance

The mechanism and sites of Lp(a) catabolism are largely unknown. Uptake via the LDL receptor is not a major pathway of Lp(a) metabolism. The kidney has been identified as playing a role in Lp(a) clearance from plasma.

Populations

Lp(a) concentrations vary over one thousandfold between individuals, from <0.2 to > 200 mg/dL. This range of concentrations is observed in all populations studied so far. The mean and median concentrations between different world populations show distinct particularities, the main being the two- to threefold higher Lp(a) plasma concentration of populations of African descent compared to Asian, Oceanic, or European populations. The general inverse correlation between apo(a) isoform size and Lp(a) plasma concentration is observed in all populations. However, mean Lp(a) associated with certain apo(a) isoforms varies between populations.

Function

Lp(a) is assembled at the hepatocyte cell membrane surface, while other scenarios exist with regard to the location of assembly. It mainly exists in plasma. Lp(a) contributes to the process of atherogenesis. Because of its structural similarity to plasminogen and tissue plasminogen activator, competitive inhibition leads to reduced fibrinolysis, and as a result of the stimulation of secretion of plasminogen activator inhibitor 1, Lp(a) leads to thrombogenesis. It may also enhance coagulation by inhibiting the function of tissue factor pathway inhibitor. Lp(a) carries cholesterol and binds atherogenic proinflammatory oxidized phospholipids as a preferential carrier of oxidized phospholipids in human plasma, which attract inflammatory cells to vessel walls and leads to smooth muscle cell proliferation. Moreover, Lp(a) is also hypothesized to be involved in wound healing and tissue repair, interacting with components of the vascular wall and extra cellular matrix. Apo(a), a distinct feature of the Lp(a) particle, binds to immobilized fibronectin and endows Lp(a) with the serine-proteinase-type proteolytic activity.

However, individuals without Lp(a) or with very low Lp(a) levels seem to be healthy. Thus, plasma Lp(a) is not vital, at least under normal environmental conditions. Since apo(a)/Lp(a) derived rather recently in mammalian evolution - only old world monkeys and humans have been shown to harbour Lp(a) - its function might not be vital but just evolutionarily advantageous under certain environmental conditions, e.g. in case of exposure to certain infectious diseases.

Another possibility, suggested by Linus Pauling, is that Lp(a) is a primate adaptation to L-gulonolactone oxidase (GULO) deficiency, found only in certain lines of mammals. GULO is required for converting glucose to ascorbic acid (vitamin C), which is needed to repair arteries; following the loss of GULO, those primates that adopted diets less abundant in vitamin C may have used Lp(a) as an ascorbic-acid surrogate to repair arterial walls.

Pathology

The structure of lipoprotein (a) is similar to plasminogen and tPA (tissue plasminogen activator) and it competes with plasminogen for its binding site, leading to reduced fibrinolysis. Also, because Lp(a) stimulates secretion of PAI-1, it leads to thrombogenesis. Lp(a) also carries cholesterol and thus contributes to atherosclerosis. In addition, Lp(a) transports the more atherogenic proinflammatory oxidized phospholipids, which attract inflammatory cells to vessel walls, and leads to smooth muscle cell proliferation.

Lipoprotein(a) and disease

High Lp(a) in blood is a risk factor for coronary heart disease (CHD), cardiovascular disease (CVD), atherosclerosis, thrombosis, and stroke. The association between Lp(a) levels and stroke is not as strong as that between Lp(a) and cardiovascular disease. Lp-a concentrations may be affected by disease states (for example kidney failure), but are only slightly affected by diet, exercise, and other environmental factors. Most commonly prescribed lipid-reducing drugs have little or no effect on Lp(a) concentration. Results using statin medications have been mixed in most trials, although a meta-analysis published in 2012 suggests that atorvastatin may be of benefit. Niacin VitaminB3 (nicotinic acid) and aspirin are two relatively safe, easily available and inexpensive drugs known to significantly reduce the levels of Lp(a) in some individuals with high Lp(a); they should be used under the supervision of a qualified physician.

High Lp(a) predicts risk of early atherosclerosis independently of other cardiac risk factors, including LDL. In patients with advanced cardiovascular disease, Lp(a)indicates a coagulant risk of plaque thrombosis. Apo(a) contains domains that are very similar to plasminogen (PLG). Lp(a) accumulates in the vessel wall and inhibits binding of PLG to the cell surface, reducing plasmin generation, which increases clotting. This inhibition of PLG by Lp(a) also promotes proliferation of smooth muscle cells. These unique features of Lp(a) suggest Lp(a) causes generation of clots and atherosclerosis.

Vegetarians have higher levels of Lp-a than fish eaters in one homogeneous tribal population of Tanzania raising the possibility that pharmacologic amounts of fish oil supplements may be helpful to lower the levels of Lp-a.

Some studies have shown that regular consumption of moderate amounts of alcohol leads to significant decline in plasma levels of Lp-a while other studies have not.

Diagnostic testing

Numerous studies confirming a strong correlation between elevated Lp(a) and heart disease have led to the consensus that Lp(a) is an important, independent predictor of cardiovascular disease. Animal studies have shown that Lp(a) may directly contribute to atherosclerotic damage by increasing plaque size, inflammation, instability, and smooth muscle cell growth. Genetic data also support the theory that Lp(a) causes cardiovascular disease.

The European Atherosclerosis Society currently recommends that patients with a moderate or high risk of cardiovascular disease have their lipoprotein (a) levels checked. Any patient with one of the following risk factors should be screened;

• premature cardiovascular disease
• familial hypercholesterolaemia
• family history of premature cardiovascular disease
• family history of elevated lipoprotein (a)
• recurrent cardiovascular disease despite statin treatment
• ≥3% 10-year risk of fatal cardiovascular disease according to the European guidelines
• ≥10% 10-year risk of fatal and/or non-fatal cardiovascular disease according to the US guidelines

If the level is elevated, treatment should be initiated with a goal of bringing the level below 50 mg/dL. In addition, the patient's other cardiovascular risk factors (including LDL levels) should be optimally managed. Apart from the total Lp(a) plasma concentration, the apo(a) isoform might be an important risk parameter as well.

Prior studies of the relationship between LP(a) and ethnicity have shown inconsistent results. Lipoprotein (a) levels seem to differ in different populations. For example, in some African populatation, Lp(a) levels are, on average higher, than other groups, so that using a risk threshold of 30 mg/dl would classify up to > 50% of the individuals as higher risk. Some part of this complexity may be related to the different genetic factors involved in determining Lp(a) levels. One recent study showed that in different ethnic groups, different genetic alterations were associated with increased Lp(a) levels.

More recent data suggest that prior studies were under-powered. The Atherosclerosis Risk in Communities (ARIC) followed 3467 African Americans and 9851 whites for 20 years. The researchers found that an elevated Lp(a) conferred the same risk in each group. However, African Americans had roughly three times the level of Lp(a), and Lp(a) also predicted an increased risk of stroke.

Approximate levels of risk are indicated by the results below, although at present there are a variety of different methods by which to measure Lp(a). A standardized international reference material has been developed and is accepted by the WHO Expert Committee on Biological Standardization and the International Federation of Clinical Chemistry and Laboratory Medicine. Although further standardization is still needed, development of a reference material is an importance step towards standardizing results.

Lipoprotein(a) - Lp(a)

Desirable: < 14 mg/dL (< 35 nmol/L)

Borderline risk: 14 - 30 mg/dL (35 - 75 nmol/L)

High risk: 31 - 50 mg/dL (75 - 125 nmol/L)

Very high risk: > 50 mg/dL (> 125 nmol/L)

LP(a) appears with different isoforms (per kringle repeats) of apolipoprotein - 40% of the variation in Lp(a) levels when measured in mg/dl can be attributed to different isoforms. Lighter Lp(a) are also associated with disease. Thus a test with simple quantitative results may not provide a complete assessment of risk.

Treatment

At the current time, the simplest treatment for an elevated lipoprotein(a) is niacin, 1-3 grams daily, in general in an extended-release form. Niacin therapy can reduce lipoprotein(a) levels by 20-30%. A more effectve treatment is the Linus Pauling protocol: 6-18 grams/day ascorbic acid, 6 grams/day L-lysine and 2 grams/day L-proline. This protocol can reduce LP(a) 2-5 fold over a few months. Aspirin may be beneficial, as well, but has only been tested in patients that carry the apolipoprotein(a) gene minor allele variant (rs3798220). A recent meta-analysis suggests that atorvastatin may also lower Lp(a) levels. In severe cases, such as familial hypercholesterolemia, or treatment resistant hypercholesterolemia, lipid apheresis may result in dramatic reductions of lipoprotein(a). The goal of treatment is to reduce levels to below 50 mg/dL.

Other medications that are in various stages of development include thyromimetics, cholesterol-ester-transfer protein (CETP inhibitors), anti-sense oligonucleopeptides, and proprotein convertase subtilisin/kexin type 9 (PCSK-9) inhibitors. L-carnitine may also reduce lipoprotein a levels. TRT (testosterone replacement therapy) also causes Lp(a) to drop.

Gingko biloba may be beneficial, but has not been clinically verified. Coenzyme Q-10 and pine bark extract have been suggested as beneficial, but neither has been proven in clinical trials.

Testosterone is known to reduce lipoprotein(a) levels. Testosterone replacement therapy also appears to be associated with lower lipoprotein(a) levels. One large study suggested that there was a decreased association between lipoprotein(a) levels and risk. Estrogen as a prevention strategy for heart disease is current topic of much research and debate. Risks and benefits may need to be considered for each individual. At present, estrogen is not indicated for treatment of elevated lipoprotein(a). Tamoxifen and raloxifene have not been shown to reduce levels.

The American Academy of Pediatrics now recommends that all children be screened for cholesterol between the ages of 9 and 11. Lipoprotein(a) levels should be considered in particular in children with a family history of early heart disease or high blood cholesterol levels. Unfortunately, there have not been enough studies to determine which therapies might be beneficial.

Interactions

Lipoprotein(a) has been shown to interact with Calnexin, Fibronectin and Fibrinogen beta chain.

See also

• Lipoprotein
• Apolipoprotein
• Very-low-density lipoprotein
• Low-density lipoprotein
• Combined hyperlipidemia

References

Further reading

• Utermann G (1989). "The mysteries of lipoprotein(a)". Science. 246 (4932): 904–10. doi:10.1126/science.2530631. PMID 2530631. 
• Salonen EM, Jauhiainen M, Zardi L, Vaheri A, Ehnholm C (1989). "Lipoprotein(a) binds to fibronectin and has serine proteinase activity capable of cleaving it". EMBO J. 8 (13): 4035–40. PMC 401578. PMID 2531657. 
• Frank SL, Klisak I, Sparkes RS, Mohandas T, Tomlinson JE, McLean JW, Lawn RM, Lusis AJ (1988). "The apolipoprotein(a) gene resides on human chromosome 6q26-27, in close proximity to the homologous gene for plasminogen". Hum. Genet. 79 (4): 352–6. doi:10.1007/BF00282175. PMID 3410459. 
• McLean JW, Tomlinson JE, Kuang WJ, Eaton DL, Chen EY, Fless GM, Scanu AM, Lawn RM (1987). "cDNA sequence of human apolipoprotein(a) is homologous to plasminogen". Nature. 330 (6144): 132–7. doi:10.1038/330132a0. PMID 3670400. 
• Scanu AM, Pfaffinger D, Lee JC, Hinman J (1994). "A single point mutation (Trp72-->Arg) in human apo(a) kringle 4-37 associated with a lysine binding defect in Lp(a)". Biochim. Biophys. Acta. 1227 (1-2): 41–5. doi:10.1016/0925-4439(94)90104-X. PMID 7918682. 
• Grainger DJ, Kemp PR, Liu AC, Lawn RM, Metcalfe JC (1994). "Activation of transforming growth factor-beta is inhibited in transgenic apolipoprotein(a) mice". Nature. 370 (6489): 460–2. doi:10.1038/370460a0. PMID 8047165. 
• Mikol V, LoGrasso PV, Boettcher BR (1996). "Crystal structures of apolipoprotein(a) kringle IV37 free and complexed with 6-aminohexanoic acid and with p-aminomethylbenzoic acid: existence of novel and expected binding modes". J. Mol. Biol. 256 (4): 751–61. doi:10.1006/jmbi.1996.0122. PMID 8642595. 
• Edelstein C, Italia JA, Klezovitch O, Scanu AM (1996). "Functional and metabolic differences between elastase-generated fragments of human lipoprotein[a] and apolipoprotein[a]". J. Lipid Res. 37 (8): 1786–801. PMID 8864963. 
• Edelstein C, Italia JA, Scanu AM (1997). "Polymorphonuclear cells isolated from human peripheral blood cleave lipoprotein(a) and apolipoprotein(a) at multiple interkringle sites via the enzyme elastase. Generation of mini-Lp(a) particles and apo(a) fragments". J. Biol. Chem. 272 (17): 11079–87. doi:10.1074/jbc.272.17.11079. PMID 9111002. 
• Köchl S, Fresser F, Lobentanz E, Baier G, Utermann G (1997). "Novel interaction of apolipoprotein(a) with beta-2 glycoprotein I mediated by the kringle IV domain". Blood. 90 (4): 1482–9. PMID 9269765. 
• Bonen DK, Nassir F, Hausman AM, Davidson NO (1998). "Inhibition of N-linked glycosylation results in retention of intracellular apo[a] in hepatoma cells, although nonglycosylated and immature forms of apolipoprotein[a] are competent to associate with apolipoprotein B-100 in vitro". J. Lipid Res. 39 (8): 1629–40. PMID 9717723. 
• Niemeier A, Willnow T, Dieplinger H, Jacobsen C, Meyer N, Hilpert J, Beisiegel U (1999). "Identification of megalin/gp330 as a receptor for lipoprotein(a) in vitro". Arterioscler. Thromb. Vasc. Biol. 19 (3): 552–61. doi:10.1161/01.ATV.19.3.552. PMID 10073957. 
• Edelstein C, Shapiro SD, Klezovitch O, Scanu AM (1999). "Macrophage metalloelastase, MMP-12, cleaves human apolipoprotein(a) in the linker region between kringles IV-4 and IV-5. Potential relevance to lipoprotein(a) biology". J. Biol. Chem. 274 (15): 10019–23. doi:10.1074/jbc.274.15.10019. PMID 10187779. 
• Ogorelkova M, Gruber A, Utermann G (1999). "Molecular basis of congenital lp(a) deficiency: a frequent apo(a) 'null' mutation in caucasians". Hum. Mol. Genet. 8 (11): 2087–96. doi:10.1093/hmg/8.11.2087. PMID 10484779. 
• Røsby O, Berg K (2000). "LPA gene: interaction between the apolipoprotein(a) size ('kringle IV' repeat) polymorphism and a pentanucleotide repeat polymorphism influences Lp(a) lipoprotein level". J. Intern. Med. 247 (1): 139–52. doi:10.1046/j.1365-2796.2000.00628.x. PMID 10672142. 
• Klose R, Fresser F, Kochl S, Parson W, Kapetanopoulos A, Fruchart-Najib J, Baier G, Utermann G (2000). "Mapping of a minimal apolipoprotein(a) interaction motif conserved in fibrin(ogen) beta - and gamma -chains". J. Biol. Chem. 275 (49): 38206–12. doi:10.1074/jbc.M003640200. PMID 10980194. 
• Ogorelkova M, Kraft HG, Ehnholm C, Utermann G (2001). "Single nucleotide polymorphisms in exons of the apo(a) kringles IV types 6 to 10 domain affect Lp(a) plasma concentrations and have different patterns in Africans and Caucasians". Hum. Mol. Genet. 10 (8): 815–24. doi:10.1093/hmg/10.8.815. PMID 11285247. 
• Garner B, Merry AH, Royle L, Harvey DJ, Rudd PM, Thillet J (2001). "Structural elucidation of the N- and O-glycans of human apolipoprotein(a): role of o-glycans in conferring protease resistance". J. Biol. Chem. 276 (25): 22200–8. doi:10.1074/jbc.M102150200. PMID 11294842. 
• Xue S, Madison EL, Miles LA (2001). "The Kringle V-protease domain is a fibrinogen binding region within Apo(a)". Thromb. Haemost. 86 (5): 1229–37. PMID 11816712. 

External links

• Lipoprotein(a) at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

• 1. リポ蛋白aと心血管疾患 lipoprotein a and cardiovascular disease
• 2. 血栓溶解異常による血栓性および出血性疾患 thrombotic and hemorrhagic disorders due to abnormal fibrinolysis
• 3. リポ蛋白の分類、代謝、およびアテローム性動脈硬化症における役割 lipoprotein classification metabolism and role in atherosclerosis
• 4. 線溶マーカーおよび心血管リスク fibrinolytic markers and cardiovascular risk
• 5. LDLコレステロール代謝の遺伝性疾患 inherited disorders of ldl cholesterol metabolism

English Journal

• Evidence for protective effect of lipoic acid and desvenlafaxine on oxidative stress in a model depression in mice.

• Silva MC1, de Sousa CN1, Gomes PX1, de Oliveira GV1, Araújo FY1, Ximenes NC1, da Silva JC1, Silva Vasconcelos G1, Leal LK2, Macêdo D1, Vasconcelos SM3.
• Progress in neuro-psychopharmacology & biological psychiatry.Prog Neuropsychopharmacol Biol Psychiatry.2016 Jan 4;64:142-8. doi: 10.1016/j.pnpbp.2015.08.002. Epub 2015 Aug 8.
• Oxidative stress is implicated in the neurobiology of depression. Here we investigated oxidative alterations in brain areas of animals submitted to the model of depression induced by corticosterone (CORT) and the effects of the antioxidant compound alpha-lipoic acid (ALA) alone or associated with th
• PMID 26265141

• Interaction of aflatoxin B1 and fumonisin B1 in mice causes immunotoxicity and oxidative stress: Possible protective role using lactic acid bacteria.

• Abbès S1,2, Ben Salah-Abbès J1, Jebali R1, Younes RB1, Oueslati R1.
• Journal of immunotoxicology.J Immunotoxicol.2016 Jan;13(1):46-54. doi: 10.3109/1547691X.2014.997905. Epub 2015 Jan 14.
• Aflatoxins (AF) are important foodborne mycotoxins implicated in human health and have immunocytotoxic effects. The aims of this study were to evaluate a new aflatoxin B1 (AFB1) and fumonisin B1 (FB1)-binding/degrading micro-organism for biological detoxification, to examine its ability to degrade A
• PMID 25585958

• Elevated lipoprotein(a), hypertension and renal insufficiency as predictors of coronary artery disease in patients with genetically confirmed heterozygous familial hypercholesterolemia.

• Chan DC1, Pang J1, Hooper AJ2, Burnett JR3, Bell DA4, Bates TR5, van Bockxmeer FM6, Watts GF7.
• International journal of cardiology.Int J Cardiol.2015 Dec 15;201:633-8. doi: 10.1016/j.ijcard.2015.08.146. Epub 2015 Aug 21.
• BACKGROUND: Familial hypercholesterolemia (FH) is characterized by elevated LDL-cholesterol and increased risk of premature coronary artery disease (CAD). Lipoprotein(a) [Lp(a)] increases CAD in FH, although the independence of this association relative to other CAD risk factors remains unclear. In
• PMID 26340131

Japanese Journal

• A LOCAL PRIORITY BASED COLOR IMAGE SEGMENTATION ALGORITHM

• SHI LEI,YANG FAN,ZHANG WEI
• ICIC express letters. Part B, Applications : an international journal of research and surveys 6(6), 1709-1714, 2015-06
• NAID 40020356037

• COMBINING FINITE-STATE BIT-FLIPPING WITH ADMM-BASED LINEAR PROGRAMMING DECODING FOR LDPC Codes

• WU DAIWEN,GUO JUNJUN
• ICIC express letters. Part B, Applications : an international journal of research and surveys 6(6), 1697-1702, 2015-06
• NAID 40020355997

• 需要7.6%減の1,259千トン,輸入高水準 : 3月分及び26年度分LPガス需給概況

• 旬刊セキツウ (2573), 42-50, 2015-05-10
• NAID 40020444667

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• リポ蛋白（リポプロテイン） - 脂質と血栓の医学

8．リポ蛋白（a）（LP(a)） Lp(a)は、LDLのアポ蛋白であるアポB-100に、アポ蛋白であるアポ(a)が結合して構成されるリポ蛋白。 Lp(a)に含まれるアポ(a)は、線溶系でフィブリン網を溶解するプラスミノゲンと構造的相同性がある。

Related Pictures

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★リンクテーブル★

関連記事	「LP」「A」「L」

「LP」

　　[★]

• 後外側核 posterior lateral nucleus
• 腰椎穿刺 lumbar puncture
• 遅延電位 late potential

　 　

「A」

　　[★]

• アデニン adenine
• アデノシン adenosine
• アラニン alanine

　 　 　

「L」

　　[★]

• リシジン
• リンキング数
• ロイシン
• free ligand concentration