apoprotein(a)

[[]]、ア・蛋白(a)

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apoprotein 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 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. 《話》広告(advertisementの略)

UpToDate Contents

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• 1. リポ蛋白aと心血管疾患 lipoprotein a and cardiovascular disease
• 2. 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
• 3. アミロイド疾患の遺伝的要因 genetic factors in the amyloid diseases
• 4. LDLコレステロール代謝の遺伝性疾患 inherited disorders of ldl cholesterol metabolism
• 5. HDLコレステロール：異常値の臨床的側面 hdl cholesterol clinical aspects of abnormal values

English Journal

• Mitochondrial iron-sulfur protein biogenesis and human disease.

• Stehling O1, Wilbrecht C1, Lill R2.Author information 1Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.2Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch-Str. 10, 35043 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str., 35043 Marburg, Germany. Electronic address: Lill@staff.uni-marburg.de.AbstractWork during the past 14 years has shown that mitochondria are the primary site for the biosynthesis of iron-sulfur (Fe/S) clusters. In fact, it is this process that renders mitochondria essential for viability of virtually all eukaryotes, because they participate in the synthesis of the Fe/S clusters of key nuclear and cytosolic proteins such as DNA polymerases, DNA helicases, and ABCE1 (Rli1), an ATPase involved in protein synthesis. As a consequence, mitochondrial function is crucial for nuclear DNA synthesis and repair, ribosomal protein synthesis, and numerous other extra-mitochondrial pathways including nucleotide metabolism and cellular iron regulation. Within mitochondria, the synthesis of Fe/S clusters and their insertion into apoproteins is assisted by 17 proteins forming the ISC (iron-sulfur cluster) assembly machinery. Biogenesis of mitochondrial Fe/S proteins can be dissected into three main steps: First, a Fe/S cluster is generated de novo on a scaffold protein. Second, the Fe/S cluster is dislocated from the scaffold and transiently bound to transfer proteins. Third, the latter components, together with specific ISC targeting factors insert the Fe/S cluster into client apoproteins. Disturbances of the first two steps impair the maturation of extra-mitochondrial Fe/S proteins and affect cellular and systemic iron homeostasis. In line with the essential function of mitochondria, genetic mutations in a number of ISC genes lead to severe neurological, hematological and metabolic diseases, often with a fatal outcome in early childhood. In this review we briefly summarize our current functional knowledge on the ISC assembly machinery, and we present a comprehensive overview of the various Fe/S protein assembly diseases.
• Biochimie.Biochimie.2014 May;100C:61-77. doi: 10.1016/j.biochi.2014.01.010. Epub 2014 Jan 23.
• Work during the past 14 years has shown that mitochondria are the primary site for the biosynthesis of iron-sulfur (Fe/S) clusters. In fact, it is this process that renders mitochondria essential for viability of virtually all eukaryotes, because they participate in the synthesis of the Fe/S cluster
• PMID 24462711

• Mammalian Fe-S cluster biogenesis and its implication in disease.

• Beilschmidt LK1, Puccio HM2.Author information 1Translational Medicine and Neurogenetics, IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire), Illkirch, France; Inserm, U596, Illkirch, France; CNRS, UMR7104, Illkirch, France; Université de Strasbourg, Strasbourg, France; Collège de France, Chaire de génétique humaine, Illkirch, France.2Translational Medicine and Neurogenetics, IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire), Illkirch, France; Inserm, U596, Illkirch, France; CNRS, UMR7104, Illkirch, France; Université de Strasbourg, Strasbourg, France; Collège de France, Chaire de génétique humaine, Illkirch, France. Electronic address: hpuccio@igbmc.fr.AbstractIron-sulfur (Fe-S) clusters are inorganic cofactors that are ubiquitous and essential. Due to their chemical versatility, Fe-S clusters are implicated in a wide range of protein functions including mitochondrial respiration and DNA repair. Composed of iron and sulfur, they are sensible to oxygen and their biogenesis requires a highly conserved protein machinery that facilitates assembly of the cluster as well as its insertion into apoproteins. Mitochondria are the central cellular compartment for Fe-S cluster biogenesis in eukaryotic cells and the importance of proper function of this biogenesis for life is highlighted by a constantly increasing number of human genetic diseases that are associated with dysfunction of this Fe-S cluster biogenesis pathway. Although these disorders are rare and appear dissimilar, common aspects are found among them. This review will give an overview on what is known on mammalian Fe-S cluster biogenesis today, by putting it into the context of what is known from studies from lower model organisms, and focuses on the associated diseases, by drawing attention to the respective mutations. Finally, it outlines the importance of adequate cellular and murine models to uncover not only each protein function, but to resolve their role and requirement throughout the mammalian organism.
• Biochimie.Biochimie.2014 May;100C:48-60. doi: 10.1016/j.biochi.2014.01.009. Epub 2014 Jan 17.
• Iron-sulfur (Fe-S) clusters are inorganic cofactors that are ubiquitous and essential. Due to their chemical versatility, Fe-S clusters are implicated in a wide range of protein functions including mitochondrial respiration and DNA repair. Composed of iron and sulfur, they are sensible to oxygen and
• PMID 24440636

• Circulating PCSK9 is a strong determinant of plasma triacylglycerols and total cholesterol in homozygous carriers of apolipoprotein ε2.

• Brouwers MC1, van Greevenbroek MM1, Konrad RJ2, Troutt JS2, Schaper NC1, Stehouwer CD1.Author information 1*Department of Internal Medicine, Divisions of General Internal Medicine and Endocrinology, Cardiovascular Research Institute Maastricht, Maastricht University Medical Centre, Maasctricht, The Netherlands.2†Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IA 46285, U.S.A.AbstractHomozygous carriers of the apolipoprotein ε2 allele are at risk of type III hyperlipidaemia, but do not necessarily develop this lipid disorder. In the present study, we have investigated the role of circulating PCSK9 (pro-protein convertase subtilisin kexin type 9), an important regulator of LDL (low-density lipoprotein) receptor expression, in the development of this hyperlipidaemic phenotype. In an observational study, plasma PCSK9 was measured in homozygous carriers of apolipoprotein ε2 (ε2/ε2; n=12), normal controls (n=72) and hypertriglyceridaemic patients with FCHL (familial combined hyperlipidaemia; n=38), who served as a hyperlipidaemic reference group. Cholesterol, triacylglycerols (triglycerides) and apolipoprotein B content in VLDL (very-low-density lipoprotein) and LDL particles was determined by ultracentrifugation in ε2/ε2 and FCHL patients. Median circulating PCSK9 levels did not differ between ε2/ε2 carriers compared with controls and hypertriglyceridaemic FCHL patients (84.5 compared with 82.0 and 84.9 ng/ml; P=0.2 and 0.6 respectively). Circulating PCSK9 was associated with total cholesterol and triacylglycerols levels in ε2/ε2 carriers (P<0.05). These associations were stronger in ε2/ε2 carriers when compared with controls (P values for interaction=0.01 and 0.02 respectively). A direct comparison with FCHL patients demonstrated a similar discrepancy for the association with plasma triacylglycerols and also VLDL-apolipoprotein B, cholesterol and triacylglycerols (P value for interaction=0.01, 0.01, 0.03 and 0.03 respectively). Plasma PCSK9 is associated with type III hyperlipidaemia. Its strong relationship with plasma triacylglycerols and total cholesterol distinguishes ε2/ε2 carriers from controls and another type of dyslipidaemia, which provides valuable information regarding the pathogenesis of this complex dyslipidaemia. Furthermore, these results suggest that patients with type III hyperlipidaemia may benefit from PCSK9-antagonizing therapy.
• Clinical science (London, England : 1979).Clin Sci (Lond).2014 May;126(9):679-84. doi: 10.1042/CS20130556.
• Homozygous carriers of the apolipoprotein ε2 allele are at risk of type III hyperlipidaemia, but do not necessarily develop this lipid disorder. In the present study, we have investigated the role of circulating PCSK9 (pro-protein convertase subtilisin kexin type 9), an important regulator of LDL
• PMID 24308640

Japanese Journal

• 食後血糖改善薬アカルボースの食後脂質代謝におよぼす影響―テストミールAを用いた検討―

• 小林 一貴,竹本 稔,石川 崇広 [他],岡部 恵見子,大西 俊一郎,栗林 伸一
• 糖尿病 58(6), 381-387, 2015
• 糖尿病では，主にトリグリセリド（TG）の上昇を特徴とし，食後高血糖と同様に心血管イベントと関連する食後高脂血症を呈する．我々は食後血糖改善薬アカルボースが，食後脂質代謝におよぼす影響を検討した．食後高血糖を主な病態とする2型糖尿病患者20名にアカルボース300 mg/日を3ヶ月間投与し，その前後でテストミールAによる食事負荷2時間後の各代謝指標等を評価すると，体重，HbA1cおよび食後TGが有意に …
• NAID 130005087450

• ビタミンA誘導体を用いた生物有機化学的研究

• 和田 昭盛
• ビタミン 88(2), 72-81, 2014-02-25
• … To reveal the conformation of chromophores in retinal proteins, various retinal analogs were synthesized, and their interaction with an apoprotein was investigated. … Comparisons of the interactions of several all-trans-8,16-ethanoretinals and all-trans-8,18-ethanoretinal with the apoprotein in phoborhodopsin revealed that the retinal was incorporated into the protein as the 6s-trans conformation. …
• NAID 110009805253

• Repeated Treatment with Furazolidone Induces Multiple Cytochrome P450-Related Activities in Chicken Liver, but Not in Rat Liver

• SASAKI Nobuo,MATUMOTO Tomoyuki,IKENAKA Yoshinori [他],NAKAYAMA Shouta M. M.,ISHIZUKA Mayumi,KAZUSAKA Akio,FUJITA Shoichi
• Journal of Veterinary Medical Science 75(11), 1497-1502, 2013
• … In chickens, treatment with FZ also induced production of microsomal CYP2C6-like apoprotein. …
• NAID 130003362235

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関連記事	「A」「apoproteins」

「A」

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

　 　 　

「apoproteins」

　　[★]

関

See Apolipoproteins／apoproteins

関

Apolipoprotein(s)