scholarly journals Serum amyloid A sequesters diverse phospholipids and their hydrolytic products, hampering fibril formation and proteolysis in a lipid-dependent manner

2018 ◽  
Vol 54 (28) ◽  
pp. 3532-3535 ◽  
Author(s):  
Shobini Jayaraman ◽  
Donald L. Gantz ◽  
Christian Haupt ◽  
Marcus Fändrich ◽  
Olga Gursky
Keyword(s):  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Dependent Manner ◽  
Amyloid A ◽  
Amyloid Fibril Formation

Serum amyloid A can solubilize diverse phospholipids and their hydrolytic products to form lipoprotein nanoparticles, which hampers amyloid fibril formation.

Structural requirements of glycosaminoglycans for facilitating amyloid fibril formation of human serum amyloid A

Amyloid ◽  
2016 ◽  
Vol 23 (2) ◽  
pp. 67-75 ◽  
Author(s):  
Hiroka Takase ◽  
Masafumi Tanaka ◽  
Aki Yamamoto ◽  
Shiori Watanabe ◽  
Sanae Takahashi ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Structural Requirements ◽  
Amyloid A ◽  
Amyloid Fibril Formation

Effect of lipid environment on amyloid fibril formation of human serum amyloid A

2017 ◽  
Vol 202 ◽  
pp. 6-12 ◽  
Author(s):  
Masafumi Tanaka ◽  
Ayaka Nishimura ◽  
Haruka Takeshita ◽  
Hiroka Takase ◽  
Toshiyuki Yamada ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Amyloid Fibril Formation ◽  
Lipid Environment

Acceleration of amyloid fibril formation by carboxyl-terminal truncation of human serum amyloid A

2018 ◽  
Vol 639 ◽  
pp. 9-15 ◽  
Author(s):  
Masafumi Tanaka ◽  
Toru Kawakami ◽  
Nozomi Okino ◽  
Kaoru Sasaki ◽  
Kiwako Nakanishi ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Amyloid Fibril Formation ◽  
Carboxyl Terminal

scholarly journals The potential role of glycosaminoglycans in serum amyloid A fibril formation by in silico approaches

2021 ◽  
pp. 100080
Author(s):  
Martyna Maszota-Zieleniak ◽  
Annemarie Danielsson ◽  
Sergey A. Samsonov
Keyword(s):  
In Silico ◽  
Serum Amyloid A ◽  
Potential Role ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Amyloid A

scholarly journals Serum amyloid A induces endothelial dysfunction in porcine coronary arteries and human coronary artery endothelial cells

2008 ◽  
Vol 295 (6) ◽  
pp. H2399-H2408 ◽  
Author(s):  
Xinwen Wang ◽  
Hong Chai ◽  
Zehao Wang ◽  
Peter H. Lin ◽  
Qizhi Yao ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Coronary Artery ◽  
Endothelial Dysfunction ◽  
Coronary Arteries ◽  
Molecular Mechanisms ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Dependent Manner ◽  
Amyloid A ◽  
Enos Mrna

The objective of this study was to determine the effects and mechanisms of serum amyloid A (SAA) on coronary endothelial function. Porcine coronary arteries and human coronary arterial endothelial cells (HCAECs) were treated with SAA (0, 1, 10, or 25 μg/ml). Vasomotor reactivity was studied using a myograph tension system. SAA significantly reduced endothelium-dependent vasorelaxation of porcine coronary arteries in response to bradykinin in a concentration-dependent manner. SAA significantly decreased endothelial nitric oxide (NO) synthase (eNOS) mRNA and protein levels as well as NO bioavailability, whereas it increased ROS in both artery rings and HCAECs. In addition, the activities of internal antioxidant enzymes catalase and SOD were decreased in SAA-treated HCAECs. Bio-plex immunoassay analysis showed the activation of JNK, ERK2, and IκB-α after SAA treatment. Consequently, the antioxidants seleno-l-methionine and Mn(III) tetrakis-(4-benzoic acid)porphyrin and specific inhibitors for JNK and ERK1/2 effectively blocked the SAA-induced eNOS mRNA decrease and SAA-induced decrease in endothelium-dependent vasorelaxation in porcine coronary arteries. Thus, SAA at clinically relevant concentrations causes endothelial dysfunction in both porcine coronary arteries and HCAECs through molecular mechanisms involving eNOS downregulation, oxidative stress, and activation of JNK and ERK1/2 as well as NF-κB. These findings suggest that SAA may contribute to the progress of coronary artery disease.

Fibril formation from recombinant human serum amyloid A

1994 ◽  
Vol 1226 (3) ◽  
pp. 323-329 ◽  
Author(s):  
Toshiyuki Yamada ◽  
Barbara Kluve-Beckerman ◽  
Juris J. Liepnieks ◽  
Merrill D. Benson
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Amyloid A

scholarly journals Mycobacterium tuberculosis stimulates IL-1β production by macrophages in an ESAT-6 dependent manner with the involvement of serum amyloid A3

2020 ◽  
Author(s):  
Bock-Gie Jung ◽  
Ramakrishna Vankayalapati ◽  
Buka Samten
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Gene Deletion ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Mouse Bone Marrow ◽  
Dependent Manner ◽  
Rna Seq ◽  
Amyloid A ◽  
Highly Expressed Genes ◽  
Mouse Lungs

ABSTRACTTo explore interleukin (IL)-1β production in tuberculosis, we infected mouse bone marrow-derived macrophages (BMDM) with Mycobacterium tuberculosis (Mtb) H37Rv, its early secreted antigenic target protein of 6 kDa (ESAT-6) gene deletion (H37Rv:Δ3875) or complemented strain (H37Rv:Δ3875C) and evaluated IL-1β production. H37Rv induced significantly increased IL-1β production by BMDMs compared to non-infected BMDMs. In contrast, H37Rv:Δ3875 induced significantly less mature IL-1β production despite eliciting comparable levels of pro-IL-1β and IL-8 from BMDMs compared to H37Rv and H37Rv:Δ3875C. Blocking either NLRP3 or K+ efflux diminished H37Rv-induced IL-1β production by BMDMs. Infection of mice intranasally with H37Rv:Δ3875 induced less IL-1β production in the lungs compared with H37Rv.Intranasal delivery of ESAT-6 but not CFP10 induced production of IL-1β in mouse lungs and RNA-Seq analysis identified serum amyloid A (SAA) 3 as one of the highly expressed genes in mouse lungs. Infection of mice with H37Rv but not H37Rv:Δ3875 induced expression of lung SAA3 mRNA and protein, consistent with the effect of intranasal delivery of ESAT-6. Silencing SAA3 reduced Mtb-induced IL-1β production by BMDMs. We conclude that the production of SAA3 is required for Mtb stimulated IL-1β production by macrophages in tuberculosis infection.

scholarly journals Tannic Acid Inhibits α-Synuclein Amyloid Fibril Formation via Binding to the Monomer N-terminal Domain

2021 ◽  
Author(s):  
Jonathan Stoeber ◽  
Jonathan K Williams ◽  
Prabhas V. Moghe ◽  
Jean Baum
Keyword(s):  
Tannic Acid ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Critical Role ◽  
Intrinsically Disordered Protein ◽  
Fibril Formation ◽  
Dependent Manner ◽  
Intrinsically Disordered ◽  
Terminal Domain ◽  
Amyloid Fibril Formation

α-Synuclein (αS) is an intrinsically disordered protein (IDP) that aggregates into amyloid fibrils during the progression of Parkinson's Disease and other synucleinopathies. The N-terminal domain (residues 1-60) is now understood to play a critical role in the initial nucleation of aggregation, as well as a pivotal role in the monomer-fibril interaction underlying amyloid seeding. Here we report on the interaction between αS and the polyphenol tannic acid (TA), where a combination of solution NMR, atomic force microscopy (AFM), and ThT assays have identified that TA targets the αS N-terminal domain to inhibit amyloid fibril formation in a pH dependent manner. This work highlights the importance of targeting the N-terminus of αS to arrest fibril formation, and suggests the importance of including polyphenolic moieties in future amyloid inhibitors.

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