Thematische Bibliographien / ApolipoproteinA-I Milano

Auswahl der wissenschaftlichen Literatur zum Thema „ApolipoproteinA-I Milano“

Autor: Grafiati
Veröffentlicht am 14. März 2023

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  1. Zeitschriftenartikel
  2. Dissertationen

Zeitschriftenartikel zum Thema "ApolipoproteinA-I Milano":

1

Shah, P. K., J. Nilsson, S. Kaul, J. Yano, J. Zhu, A. Hamsten und B. Cercek. „Inhibition of aortic atherosclerosis in apolipoprotein E-deficient mice by recombinant apolipoprotein A-I Milano“. Journal of the American College of Cardiology 31 (Februar 1998): 390. http://dx.doi.org/10.1016/s0735-1097(98)80043-0.

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2

Shah, P. „Inhibition of Aortic Atherosclerosis in Apolipoprotein E-deficient Mice by Recombinant Apolipoprotein A-I Milano“. Journal of the American College of Cardiology 31, Nr. 2 (Februar 1998): 390A. http://dx.doi.org/10.1016/s0735-1097(97)85397-1.

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3

Bhat, Shaila, Mary G. Sorci-Thomas, Laura Calabresi, Michael P. Samuel und Michael J. Thomas. „Conformation of Dimeric Apolipoprotein A-I Milano on Recombinant Lipoprotein Particles“. Biochemistry 49, Nr. 25 (29.06.2010): 5213–24. http://dx.doi.org/10.1021/bi1003734.

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4

Klon, Anthony E., Martin K. Jones, Jere P. Segrest und Stephen C. Harvey. „Molecular Belt Models for the Apolipoprotein A-I Paris and Milano Mutations“. Biophysical Journal 79, Nr. 3 (September 2000): 1679–85. http://dx.doi.org/10.1016/s0006-3495(00)76417-4.

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5

Bielicki, John K., Mark R. McCall, Lori J. Stoltzfus, Amir Ravandi, Arnis Kuksis, Edward M. Rubin und Trudy M. Forte. „Evidence That Apolipoprotein A-I Milano Has Reduced Capacity, Compared With Wild-Type Apolipoprotein A-I, to Recruit Membrane Cholesterol“. Arteriosclerosis, Thrombosis, and Vascular Biology 17, Nr. 9 (September 1997): 1637–43. http://dx.doi.org/10.1161/01.atv.17.9.1637.

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6

Coin, B. D., P. K. Shah, J. Yano, M. D. Molloy, B. Cercek und S. Kaul. „Reversal of impaired endothelium-dependent vasodilatation in apolipoprotein E-deficient mice by recombinant apolipoprotein A-I Milano“. Journal of the American College of Cardiology 31 (1998): 60–61. http://dx.doi.org/10.1016/s0735-1097(98)80909-1.

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7

Bielicki, J. K., T. M. Forte, M. R. McCall, L. J. Stoltzfus, G. Chiesa, C. R. Sirtori, G. Franceschini und E. M. Rubin. „High density lipoprotein particle size restriction in apolipoprotein A-I(Milano) transgenic mice“. Journal of Lipid Research 38, Nr. 11 (November 1997): 2314–21. http://dx.doi.org/10.1016/s0022-2275(20)34945-2.

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8

Coin, B. D., P. K. Shah, J. Yano, M. D. Molloy, B. Cercek und S. Kaul. „Recombinant apolipoprotein A-I Millano protects against lysophosphatidylcholine-induced endothelial dysfunction“. Journal of the American College of Cardiology 31 (1998): 148. http://dx.doi.org/10.1016/s0735-1097(98)81288-6.

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9

Alexander, Eric T., Masafumi Tanaka, Momoe Kono, Hiroyuki Saito, Daniel J. Rader und Michael C. Phillips. „Structural and functional consequences of the Milano mutation (R173C) in human apolipoprotein A-I“. Journal of Lipid Research 50, Nr. 7 (24.03.2009): 1409–19. http://dx.doi.org/10.1194/jlr.m800578-jlr200.

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10

Ameli, S., A. Hultgardh-Nilsson, B. Cercek, P. K. Shah, J. S. Forrester, H. Ageland und J. Nilsson. „Recombinant apolipoprotein A-I Milano reduces intimal thickening after balloon injury in hypercholesterolemic rabbits.“ Circulation 90, Nr. 4 (Oktober 1994): 1935–41. http://dx.doi.org/10.1161/01.cir.90.4.1935.

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Zeitschriftenartikel

Dissertationen zum Thema "ApolipoproteinA-I Milano":

1

Rosini, Giulia. „New insights and tools to study innovative delivery strategies of therapeutic peptides: Apolipoprotein A-I Milano, administered orally via genetically modified rice plants, exerts anti-inflammatory effects in vivo“. Doctoral thesis, Università di Siena, 2022. http://hdl.handle.net/11365/1210413.

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In the proof-of-concept study published by Romano and others in Int.Cardiology 2018, was shown a new approach for treatment of cardiovascular disease (CVDs) because, despite the high therapeutic potential of Apolipoprotein A-I protein, the practical application is hampered by the low efficiency of purification and delivery. A genetically modified rice plants expressing Apolipoprotein A-I variant Milano (AIM) were created. The product was tested in vitro, and in vivo mouse atherosclerotic model treated with genetically modified rice-milk (in the form of protein extract of rice seed proteins) or wild type rice-milk and it was found to be safe and effective. For subsequent aims, initially, in this context, the APO rice flour (RF) product was better characterized to further understand the potential of transgenic rice seeds as an efficient oral production and delivery system for recombinant AIM protein. WT and APO RF were analysed by ELISA and Western Blot (WB) and APO protein was detected in APO rice as expected. To better understand the biodistribution of the AIM protein administered orally in APO3 pre-clinical study and the molecular mechanisms underlying the athero-protective and anti-inflammatory effects, ELISA, WB and immunohistochemistry (IHC) assays were performed on mice liver and/or other organs. AIM in liver and intestine lysates was not detected by ELISA and WB. By increasing the spatial resolution by IHC, positive spots were detected in the liver sections of the treated mice. These investigations were fundamental to lay the foundations for the main purpose, namely the development of a new system of functional AIM product to improve both in quality and quantity of delivered protein to be able to extend the product for future use in humans. In this order, a set of vectors carrying the coding sequence of the AIM and the respective control vectors was constructed, to be tested at a functional level in vitro and subsequently to be used as source of the AIM sequence to engineer the new rice product.
2

Janakiraman, Vignesh Narasimhan. „Expression of wild type and variants of human apolipoprotein A-I in Pichia pastoris“. Thesis, Bordeaux, 2015. http://www.theses.fr/2015BORD0450/document.

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Les lipoprotéines de haute densité (High Density Lipoprotein, HDL) permet deréduction de risque de maladies cardio-vasculaires principalement en raison de leurcapacité à éliminer le cholestérol accumulé des artères (via transport inverse ducholestérol). Les effets protecteurs des HDL sont médiés par l'apolipoprotéine AI(ApoA1), qui est le La protéine la plus importante quantitativement du HDL. L’ApoA1favorise l'efflux de cholestérol vers le foie pour l'excrétion. Une augmentation desniveaux plasmatiques de l’ApoA1 est généralement acceptée d'êtrecardioprotecteur, ce qui en fait un potentiel thérapeutique. Deux variantes naturelle(mutants) de l’ApoA1, Milano et Paris, sont caractérisées par une mutationponctuelle unique a permis l'introduction d'un résidu cystéine. Populations avecApoA1-Milano ont été rapportés d'avoir un système cardiovasculaire, même avec defaibles niveaux de plasma de ApoA1 et HDL. Il est donc d'intérêt pour générerrecombinante de type sauvage et des variantes de ApoA1 humaine pour desapplications thérapeutiques potentielles. Dans cette étude, de type sauvagerhApoA1 a été produit chez P. pastoris et purifié par chromatographie en modemixte en une seule étape. Par la suite, un processus intégré a été le développementde la production et la récupération rapide de type sauvage rhApoA1 chez P. pastorispar chromatographie par lit expansée. En outre, les variantes de l'ApoA1, Milano &Paris, ont été générées par mutagenèse dirigée et ont été exprimés chez P. pastoris.Les motifs d’adsorption de rhApoA1-Milano et rhApoA1-Paris ont été comparés àcelle de type sauvage ApoA1 et les différences ont été discutées
The high-density lipoprotein (HDL) complex helps reduce the risk of cardiovasculardisorders mainly due to its ability to remove accumulated cholesterol from arteriesvia reverse cholesterol transport. These protective effects of HDL are known to bemediated by Apolipoprotein A-I (ApoA1), which is the major protein component ofHDL. ApoA1 is a lipid binding protein and promotes cholesterol efflux fromperipheral tissues to the liver for excretion. An increase in the plasma levels ofApoA1 is generally accepted to be cardioprotective, making it a potentialtherapeutic. Two naturally occuring variants of ApoA1, namely the Milano & Parismutants, are characterised by a single point mutation resulting in the introduction ofa Cysteine residue. Populations with ApoA1-Milano have been reported to have ahealthier cardiovascular system even with low plasma levels of ApoA1/HDL. It ishence of interest to generate recombinant wild type and variants of human ApoA1for potential therapeutic applications. In this study, wild type rhApoA1 was producedin P. pastoris and purified by mixed-mode chromatgraphy in a single step.Subsequently, an integrated process has been development for the production andrapid recovery of wild type rhApoA1 in Pichia pastoris. This has paved way to theestablishment of a scalable integrated process that could be further developed toindustrial levels. In addition, the cysteine variants of ApoA1, Milano & Paris, havebeen generated by site directed mutagenesis and have been successfully expressedin P. pastoris. The binding patterns of rhApoA1-Milano and rhApoA1-Paris have beencompared with that of wild-type ApoA1 and the differences have been discussed

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