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000154362 037__ $$aDZNE-2021-00215
000154362 041__ $$aEnglish
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000154362 1001_ $$0P:(DE-2719)2810939$$aDegenhardt, Karoline$$b0$$eFirst author$$udzne
000154362 245__ $$aMedin aggregation causes cerebrovascular dysfunction in aging wild-type mice.
000154362 260__ $$aWashington, DC$$bNational Acad. of Sciences$$c2020
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000154362 520__ $$aMedin is the most common amyloid known in humans, as it can be found in blood vessels of the upper body in virtually everybody over 50 years of age. However, it remains unknown whether deposition of Medin plays a causal role in age-related vascular dysfunction. We now report that aggregates of Medin also develop in the aorta and brain vasculature of wild-type mice in an age-dependent manner. Strikingly, genetic deficiency of the Medin precursor protein, MFG-E8, eliminates not only vascular aggregates but also prevents age-associated decline of cerebrovascular function in mice. Given the prevalence of Medin aggregates in the general population and its role in vascular dysfunction with aging, targeting Medin may become a novel approach to sustain healthy aging.
000154362 536__ $$0G:(DE-HGF)POF4-352$$a352 - Disease Mechanisms (POF4-352)$$cPOF4-352$$fPOF IV$$x0
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000154362 650_7 $$2Other$$aMFG-E8
000154362 650_7 $$2Other$$aMedin
000154362 650_7 $$2Other$$aaging
000154362 650_7 $$2Other$$aamyloid
000154362 650_7 $$2Other$$acerebrovascular dysfunction
000154362 650_7 $$2NLM Chemicals$$aAmyloid
000154362 650_7 $$2NLM Chemicals$$aAntigens, Surface
000154362 650_7 $$2NLM Chemicals$$aMFGE8 protein, human
000154362 650_7 $$2NLM Chemicals$$aMfge8 protein, mouse
000154362 650_7 $$2NLM Chemicals$$aMilk Proteins
000154362 650_2 $$2MeSH$$aAged, 80 and over
000154362 650_2 $$2MeSH$$aAging: metabolism
000154362 650_2 $$2MeSH$$aAmyloid: genetics
000154362 650_2 $$2MeSH$$aAmyloid: metabolism
000154362 650_2 $$2MeSH$$aAnimals
000154362 650_2 $$2MeSH$$aAntigens, Surface: genetics
000154362 650_2 $$2MeSH$$aAntigens, Surface: metabolism
000154362 650_2 $$2MeSH$$aAorta: metabolism
000154362 650_2 $$2MeSH$$aAorta: pathology
000154362 650_2 $$2MeSH$$aBrain Chemistry: physiology
000154362 650_2 $$2MeSH$$aCerebrovascular Circulation: physiology
000154362 650_2 $$2MeSH$$aFemale
000154362 650_2 $$2MeSH$$aHumans
000154362 650_2 $$2MeSH$$aMale
000154362 650_2 $$2MeSH$$aMice
000154362 650_2 $$2MeSH$$aMice, Inbred C57BL
000154362 650_2 $$2MeSH$$aMilk Proteins: genetics
000154362 650_2 $$2MeSH$$aMilk Proteins: metabolism
000154362 650_2 $$2MeSH$$aVascular Diseases: metabolism
000154362 650_2 $$2MeSH$$aVascular Diseases: pathology
000154362 7001_ $$0P:(DE-2719)2812193$$aWagner, Jessica$$b1$$udzne
000154362 7001_ $$0P:(DE-2719)2810430$$aSkodras, Angelos$$b2$$udzne
000154362 7001_ $$aCandlish, Michael$$b3
000154362 7001_ $$0P:(DE-HGF)0$$aKoppelmann, Anna Julia$$b4
000154362 7001_ $$0P:(DE-2719)2811762$$aWild, Katleen$$b5$$udzne
000154362 7001_ $$aMaxwell, Rusheka$$b6
000154362 7001_ $$0P:(DE-2719)2630394$$aRotermund, Carola$$b7$$udzne
000154362 7001_ $$0P:(DE-2719)2811552$$avon Zweydorf, Felix$$b8$$udzne
000154362 7001_ $$0P:(DE-2719)2811291$$aGloeckner, Christian Johannes$$b9$$udzne
000154362 7001_ $$aDavies, Hannah A$$b10
000154362 7001_ $$0P:(DE-HGF)0$$aMadine, Jillian$$b11
000154362 7001_ $$aDel Turco, Domenico$$b12
000154362 7001_ $$0P:(DE-2719)2812867$$aFeederle, Regina$$b13$$udzne
000154362 7001_ $$0P:(DE-HGF)0$$aLashley, Tammaryn$$b14
000154362 7001_ $$aDeller, Thomas$$b15
000154362 7001_ $$0P:(DE-2719)2810803$$aKahle, Philipp$$b16$$udzne
000154362 7001_ $$0P:(DE-HGF)0$$aHefendehl, Jasmin K$$b17
000154362 7001_ $$0P:(DE-2719)2000010$$aJucker, Mathias$$b18$$udzne
000154362 7001_ $$0P:(DE-2719)2811021$$aNeher, Jonas$$b19$$eLast author$$udzne
000154362 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.2011133117$$gVol. 117, no. 38, p. 23925 - 23931$$n38$$p23925 - 23931$$tProceedings of the National Academy of Sciences of the United States of America$$v117$$x1091-6490$$y2020
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