Desacyl-ghrelin and synthetic GH-secretagogues modulate the production of inflammatory cytokines in mouse microglia cells stimulated by β-amyloid fibrils

2009 ◽  
Vol 87 (12) ◽  
pp. 2718-2727 ◽  
Author(s):  
Ilaria Bulgarelli ◽  
Laura Tamiazzo ◽  
Elena Bresciani ◽  
Daniela Rapetti ◽  
Simona Caporali ◽  
...  
Keyword(s):  
Inflammatory Cytokines ◽  
Amyloid Fibrils ◽  
Gh Secretagogues ◽  
Desacyl Ghrelin ◽  
Β Amyloid

scholarly journals Autophagy in microglia degrades extracellular β-amyloid fibrils and regulates the NLRP3 inflammasome

Autophagy ◽  
2014 ◽  
Vol 10 (10) ◽  
pp. 1761-1775 ◽  
Author(s):  
Mi-Hyang Cho ◽  
Kwangmin Cho ◽  
Hoe-Jin Kang ◽  
Eun-Young Jeon ◽  
Hun-Sik Kim ◽  
...  
Keyword(s):  
Nlrp3 Inflammasome ◽  
Amyloid Fibrils ◽  
Β Amyloid

scholarly journals β-Amyloid Fibrils Activate Parallel Mitogen-Activated Protein Kinase Pathways in Microglia and THP1 Monocytes

1998 ◽  
Vol 18 (12) ◽  
pp. 4451-4460 ◽  
Author(s):  
Douglas R. McDonald ◽  
Maria E. Bamberger ◽  
Colin K. Combs ◽  
Gary E. Landreth
Keyword(s):  
Protein Kinase ◽  
Amyloid Fibrils ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Β Amyloid

scholarly journals The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid

2021 ◽  
Vol 118 (3) ◽  
pp. e2014442118
Author(s):  
Nir Salinas ◽  
Einav Tayeb-Fligelman ◽  
Massimo D. Sammito ◽  
Daniel Bloch ◽  
Raz Jelinek ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Membrane Damage ◽  
Fibril Formation ◽  
Regulation Mechanism ◽  
Bacterial Cells ◽  
Amyloid Fibril Formation ◽  
Β Amyloid ◽  
Β Sheets

Antimicrobial activity is being increasingly linked to amyloid fibril formation, suggesting physiological roles for some human amyloids, which have historically been viewed as strictly pathological agents. This work reports on formation of functional cross-α amyloid fibrils of the amphibian antimicrobial peptide uperin 3.5 at atomic resolution, an architecture initially discovered in the bacterial PSMα3 cytotoxin. The fibrils of uperin 3.5 and PSMα3 comprised antiparallel and parallel helical sheets, respectively, recapitulating properties of β-sheets. Uperin 3.5 demonstrated chameleon properties of a secondary structure switch, forming mostly cross-β fibrils in the absence of lipids. Uperin 3.5 helical fibril formation was largely induced by, and formed on, bacterial cells or membrane mimetics, and led to membrane damage and cell death. These findings suggest a regulation mechanism, which includes storage of inactive peptides as well as environmentally induced activation of uperin 3.5, via chameleon cross-α/β amyloid fibrils.

Inhibitory activity of stilbenes on Alzheimer’s β-amyloid fibrils in vitro

2007 ◽  
Vol 15 (2) ◽  
pp. 1160-1167 ◽  
Author(s):  
Céline Rivière ◽  
Tristan Richard ◽  
Lysiane Quentin ◽  
Stéphanie Krisa ◽  
Jean-Michel Mérillon ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Amyloid Fibrils ◽  
Β Amyloid

How Changes in the Sequence of the Peptide CLPFFD-NH2Can Modify the Conjugation and Stability of Gold Nanoparticles and Their Affinity for β-Amyloid Fibrils

2008 ◽  
Vol 19 (6) ◽  
pp. 1154-1163 ◽  
Author(s):  
Ivonne Olmedo ◽  
Eyleen Araya ◽  
Fausto Sanz ◽  
Elias Medina ◽  
Jordi Arbiol ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Amyloid Fibrils ◽  
Β Amyloid

Abstract 539: Soluble Oxidized Apolipoprotein A-I, a Precursor of Amyloid Fibrils, Activates Secretion of Inflammatory Cytokines in Macrophages

2016 ◽  
Vol 36 (suppl_1) ◽  
Author(s):  
Andrzej Witkowski ◽  
Gary K Chan ◽  
Nancy J Li ◽  
Rui Lu ◽  
Shinji Yokoyama ◽  
...  
Keyword(s):  
Inflammatory Response ◽  
Inflammatory Cytokines ◽  
Amyloid Fibrils ◽  
Mouse Bone Marrow ◽  
Amyloid Formation ◽  
Cellular Cholesterol ◽  
Atherosclerosis Progression ◽  
Apolipoprotein A ◽  
Inflammatory Protein ◽  
Release Capacity

Atherosclerosis is often described as an inflammatory disease of the arteries. One mechanism whereby apolipoprotein A-I (apoA-I) exerts its anti-atherosclerotic effect is by mitigating the inflammatory response of cells involved in atherosclerosis progression. However, oxidation transforms apoA-I from an anti-inflammatory to a pro-inflammatory protein. We previously reported that oxidation can also promote apoA-I aggregation and formation of amyloid fibrils. In this study, we investigated the mechanistic interplay between oxidation, amyloid formation and the inflammatory response of macrophages to apoA-I. We hypothesized that amyloid fibrils constituted of oxidized apoA-I activate production of inflammatory cytokines in macrophages. To test this hypothesis, amyloidogenic apoA-I was generated by oxidation with an excess of H 2 O 2 (H 2 O 2 -ApoA-I). Intracellular and secreted levels of IL-1β were determined upon incubation of mouse bone marrow derived macrophages (BMDM) with intact-apoA-I, soluble H 2 O 2 -ApoA-I and pre-formed H 2 O 2 -ApoA-I amyloid fibrils. Cellular cholesterol release from RAW264.7 cells was also measured. Soluble H 2 O 2 -ApoA-I (amyloid precursor) retained the cellular cholesterol release capacity of intact-ApoA-I. In BMDM incubated with soluble H 2 O 2 -ApoA-I however, levels of IL-1β synthesis and secretion were at least 2-fold higher than those induced by intact-ApoA-I. In contrast, incubation with H 2 O 2 -ApoA-I amyloid fibrils did not increase the levels of IL-1β synthesis and secretion, compared to intact-ApoA-I. Thus, soluble and functional oxidized apoA-I activates inflammatory cytokine synthesis and secretion in macrophages. Notably, this pro-inflammatory potential was completely neutralized when oxidized apoA-I was aggregated in amyloids. Therefore in atherosclerotic lesions, amyloid formation could reduce, rather than exacerbate, the inflammatory burden produced by pro-inflammatory soluble oxidized apoA-I species.

Nicotine breaks down preformed Alzheimer’s β-amyloid fibrils in vitro

2002 ◽  
Vol 52 (9) ◽  
pp. 880-886 ◽  
Author(s):  
Kenjiro Ono ◽  
Kazuhiro Hasegawa ◽  
Masahito Yamada ◽  
Hironobu Naiki
Keyword(s):  
Amyloid Fibrils ◽  
Β Amyloid

scholarly journals Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

Cell ◽  
2013 ◽  
Vol 154 (6) ◽  
pp. 1257-1268 ◽  
Author(s):  
Jun-Xia Lu ◽  
Wei Qiang ◽  
Wai-Ming Yau ◽  
Charles D. Schwieters ◽  
Stephen C. Meredith ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Brain Tissue ◽  
Amyloid Fibrils ◽  
Β Amyloid

scholarly journals Structural Polymorphism of Alzheimer’s β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study

2016 ◽  
Vol 138 (31) ◽  
pp. 9840-9852 ◽  
Author(s):  
Matthew R. Elkins ◽  
Tuo Wang ◽  
Mimi Nick ◽  
Hyunil Jo ◽  
Thomas Lemmin ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Fibrils ◽  
Structural Polymorphism ◽  
Nmr Study ◽  
Β Amyloid
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