Home > Publications Database > Medin aggregation causes cerebrovascular dysfunction in aging wild-type mice. > print

001     154362
005     20250717160823.0
024 7 _ |a 10.1073/pnas.2011133117
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024 7 _ |a pmc:PMC7519322
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024 7 _ |a 0027-8424
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024 7 _ |a 1091-6490
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041 _ _ |a English
082 _ _ |a 500
100 1 _ |a Degenhardt, Karoline
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245 _ _ |a Medin aggregation causes cerebrovascular dysfunction in aging wild-type mice.
260 _ _ |a Washington, DC
|c 2020
|b National Acad. of Sciences
336 7 _ |a article
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500 _ _ |a ISSN 1091-6490 not unique: **3 hits**.
520 _ _ |a Medin 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.
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650 _ 7 |a MFG-E8
|2 Other
650 _ 7 |a Medin
|2 Other
650 _ 7 |a aging
|2 Other
650 _ 7 |a amyloid
|2 Other
650 _ 7 |a cerebrovascular dysfunction
|2 Other
650 _ 7 |a Amyloid
|2 NLM Chemicals
650 _ 7 |a Antigens, Surface
|2 NLM Chemicals
650 _ 7 |a MFGE8 protein, human
|2 NLM Chemicals
650 _ 7 |a Mfge8 protein, mouse
|2 NLM Chemicals
650 _ 7 |a Milk Proteins
|2 NLM Chemicals
650 _ 2 |a Aged, 80 and over
|2 MeSH
650 _ 2 |a Aging: metabolism
|2 MeSH
650 _ 2 |a Amyloid: genetics
|2 MeSH
650 _ 2 |a Amyloid: metabolism
|2 MeSH
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Antigens, Surface: genetics
|2 MeSH
650 _ 2 |a Antigens, Surface: metabolism
|2 MeSH
650 _ 2 |a Aorta: metabolism
|2 MeSH
650 _ 2 |a Aorta: pathology
|2 MeSH
650 _ 2 |a Brain Chemistry: physiology
|2 MeSH
650 _ 2 |a Cerebrovascular Circulation: physiology
|2 MeSH
650 _ 2 |a Female
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Male
|2 MeSH
650 _ 2 |a Mice
|2 MeSH
650 _ 2 |a Mice, Inbred C57BL
|2 MeSH
650 _ 2 |a Milk Proteins: genetics
|2 MeSH
650 _ 2 |a Milk Proteins: metabolism
|2 MeSH
650 _ 2 |a Vascular Diseases: metabolism
|2 MeSH
650 _ 2 |a Vascular Diseases: pathology
|2 MeSH
700 1 _ |a Wagner, Jessica
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700 1 _ |a Skodras, Angelos
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700 1 _ |a Candlish, Michael
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700 1 _ |a Koppelmann, Anna Julia
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700 1 _ |a Wild, Katleen
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700 1 _ |a Maxwell, Rusheka
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700 1 _ |a Rotermund, Carola
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700 1 _ |a von Zweydorf, Felix
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700 1 _ |a Gloeckner, Christian Johannes
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700 1 _ |a Davies, Hannah A
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700 1 _ |a Madine, Jillian
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700 1 _ |a Del Turco, Domenico
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700 1 _ |a Feederle, Regina
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700 1 _ |a Lashley, Tammaryn
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700 1 _ |a Deller, Thomas
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700 1 _ |a Kahle, Philipp
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700 1 _ |a Hefendehl, Jasmin K
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700 1 _ |a Jucker, Mathias
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700 1 _ |a Neher, Jonas
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773 _ _ |a 10.1073/pnas.2011133117
|g Vol. 117, no. 38, p. 23925 - 23931
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|n 38
|p 23925 - 23931
|t Proceedings of the National Academy of Sciences of the United States of America
|v 117
|y 2020
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856 4 _ |u https://pub.dzne.de/record/154362/files/DZNE-2021-00215_Restricted.pdf
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