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| Home > Publications Database > Integrative proteomics identifies a conserved Aβ amyloid responsome, novel plaque proteins, and pathology modifiers in Alzheimer's disease. > print |
| Home > Publications Database > Integrative proteomics identifies a conserved Aβ amyloid responsome, novel plaque proteins, and pathology modifiers in Alzheimer's disease. > print |
| 001 | 271706 | ||
| 005 | 20250127091627.0 | ||
| 024 | 7 | _ | |a pmc:PMC11384960 |2 pmc |
| 024 | 7 | _ | |a 10.1016/j.xcrm.2024.101669 |2 doi |
| 024 | 7 | _ | |a pmid:39127040 |2 pmid |
| 024 | 7 | _ | |a altmetric:166141083 |2 altmetric |
| 037 | _ | _ | |a DZNE-2024-01058 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 610 |
| 100 | 1 | _ | |a Levites, Yona |b 0 |
| 245 | _ | _ | |a Integrative proteomics identifies a conserved Aβ amyloid responsome, novel plaque proteins, and pathology modifiers in Alzheimer's disease. |
| 260 | _ | _ | |a Maryland Heights, MO |c 2024 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1725271159_32477 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Alzheimer's disease (AD) is a complex neurodegenerative disorder that develops over decades. AD brain proteomics reveals vast alterations in protein levels and numerous altered biologic pathways. Here, we compare AD brain proteome and network changes with the brain proteomes of amyloid β (Aβ)-depositing mice to identify conserved and divergent protein networks with the conserved networks identifying an Aβ amyloid responsome. Proteins in the most conserved network (M42) accumulate in plaques, cerebrovascular amyloid (CAA), and/or dystrophic neuronal processes, and overexpression of two M42 proteins, midkine (Mdk) and pleiotrophin (PTN), increases the accumulation of Aβ in plaques and CAA. M42 proteins bind amyloid fibrils in vitro, and MDK and PTN co-accumulate with cardiac transthyretin amyloid. M42 proteins appear intimately linked to amyloid deposition and can regulate amyloid deposition, suggesting that they are pathology modifiers and thus putative therapeutic targets. We posit that amyloid-scaffolded accumulation of numerous M42+ proteins is a central mechanism mediating downstream pathophysiology in AD. |
| 536 | _ | _ | |a 353 - Clinical and Health Care Research (POF4-353) |0 G:(DE-HGF)POF4-353 |c POF4-353 |f POF IV |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, , Journals: pub.dzne.de |
| 650 | _ | 7 | |a Alzheimer’s disease |2 Other |
| 650 | _ | 7 | |a Midkine |2 Other |
| 650 | _ | 7 | |a Pleiotrophin |2 Other |
| 650 | _ | 7 | |a aggregation |2 Other |
| 650 | _ | 7 | |a amyloid |2 Other |
| 650 | _ | 7 | |a animal models |2 Other |
| 650 | _ | 7 | |a plaques |2 Other |
| 650 | _ | 7 | |a proteomics |2 Other |
| 650 | _ | 7 | |a Amyloid beta-Peptides |2 NLM Chemicals |
| 650 | _ | 7 | |a Proteome |2 NLM Chemicals |
| 650 | _ | 7 | |a pleiotrophin |0 134034-50-7 |2 NLM Chemicals |
| 650 | _ | 7 | |a Carrier Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Cytokines |2 NLM Chemicals |
| 650 | _ | 2 | |a Alzheimer Disease: metabolism |2 MeSH |
| 650 | _ | 2 | |a Alzheimer Disease: pathology |2 MeSH |
| 650 | _ | 2 | |a Alzheimer Disease: genetics |2 MeSH |
| 650 | _ | 2 | |a Proteomics: methods |2 MeSH |
| 650 | _ | 2 | |a Animals |2 MeSH |
| 650 | _ | 2 | |a Amyloid beta-Peptides: metabolism |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Plaque, Amyloid: metabolism |2 MeSH |
| 650 | _ | 2 | |a Plaque, Amyloid: pathology |2 MeSH |
| 650 | _ | 2 | |a Mice |2 MeSH |
| 650 | _ | 2 | |a Brain: metabolism |2 MeSH |
| 650 | _ | 2 | |a Brain: pathology |2 MeSH |
| 650 | _ | 2 | |a Proteome: metabolism |2 MeSH |
| 650 | _ | 2 | |a Mice, Transgenic |2 MeSH |
| 650 | _ | 2 | |a Carrier Proteins: metabolism |2 MeSH |
| 650 | _ | 2 | |a Carrier Proteins: genetics |2 MeSH |
| 650 | _ | 2 | |a Cytokines: metabolism |2 MeSH |
| 650 | _ | 2 | |a Male |2 MeSH |
| 700 | 1 | _ | |a Dammer, Eric B |b 1 |
| 700 | 1 | _ | |a Ran, Yong |b 2 |
| 700 | 1 | _ | |a Tsering, Wangchen |b 3 |
| 700 | 1 | _ | |a Duong, Duc |b 4 |
| 700 | 1 | _ | |a Abreha, Measho |b 5 |
| 700 | 1 | _ | |a Gadhavi, Joshna |b 6 |
| 700 | 1 | _ | |a Lolo, Kiara |b 7 |
| 700 | 1 | _ | |a Trejo-Lopez, Jorge |b 8 |
| 700 | 1 | _ | |a Phillips, Jennifer |b 9 |
| 700 | 1 | _ | |a Iturbe, Andrea |b 10 |
| 700 | 1 | _ | |a Erquizi, Aya |b 11 |
| 700 | 1 | _ | |a Moore, Brenda D |b 12 |
| 700 | 1 | _ | |a Ryu, Danny |b 13 |
| 700 | 1 | _ | |a Natu, Aditya |b 14 |
| 700 | 1 | _ | |a Dillon, Kristy |b 15 |
| 700 | 1 | _ | |a Torrellas, Jose |b 16 |
| 700 | 1 | _ | |a Moran, Corey |b 17 |
| 700 | 1 | _ | |a Ladd, Thomas |b 18 |
| 700 | 1 | _ | |a Afroz, Farhana |b 19 |
| 700 | 1 | _ | |a Islam, Tariful |b 20 |
| 700 | 1 | _ | |a Jagirdar, Jaishree |b 21 |
| 700 | 1 | _ | |a Funk, Cory C |b 22 |
| 700 | 1 | _ | |a Robinson, Max |b 23 |
| 700 | 1 | _ | |a Rangaraju, Srikant |b 24 |
| 700 | 1 | _ | |a Borchelt, David R |b 25 |
| 700 | 1 | _ | |a Ertekin-Taner, Nilüfer |b 26 |
| 700 | 1 | _ | |a Kelly, Jeffrey W |b 27 |
| 700 | 1 | _ | |a Heppner, Frank L |0 P:(DE-2719)2812386 |b 28 |u dzne |
| 700 | 1 | _ | |a Johnson, Erik C B |b 29 |
| 700 | 1 | _ | |a McFarland, Karen |b 30 |
| 700 | 1 | _ | |a Levey, Allan I |b 31 |
| 700 | 1 | _ | |a Prokop, Stefan |b 32 |
| 700 | 1 | _ | |a Seyfried, Nicholas T |b 33 |
| 700 | 1 | _ | |a Golde, Todd E |b 34 |
| 773 | _ | _ | |a 10.1016/j.xcrm.2024.101669 |g Vol. 5, no. 8, p. 101669 - |0 PERI:(DE-600)3019420-9 |n 8 |p 101669 |t Cell reports / Medicine |v 5 |y 2024 |x 2666-3791 |
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