scholarly journals Serum amyloid A1 mediates myotube atrophy via Toll‐like receptors

2019 ◽  
Vol 11 (1) ◽  
pp. 103-119 ◽  
Author(s):  
Alexander Hahn ◽  
Melanie Kny ◽  
Cristina Pablo‐Tortola ◽  
Mihail Todiras ◽  
Michael Willenbrock ◽  
...  
2021 ◽  
pp. 106766
Author(s):  
Y. Linhares Boakari ◽  
A. Esteller-Vico ◽  
S. Loux ◽  
H. El-Sheikh Ali ◽  
C. Barbosa Fernandes ◽  
...  

Biomedicines ◽  
2021 ◽  
Vol 9 (6) ◽  
pp. 599
Author(s):  
Víctor Farré-Alins ◽  
Alejandra Palomino-Antolín ◽  
Paloma Narros-Fernández ◽  
Ana Belen Lopez-Rodriguez ◽  
Céline Decouty-Perez ◽  
...  

Traumatic brain injury (TBI) is one of the leading causes of mortality and disability worldwide without any validated biomarker or set of biomarkers to help the diagnosis and evaluation of the evolution/prognosis of TBI patients. To achieve this aim, a deeper knowledge of the biochemical and pathophysiological processes triggered after the trauma is essential. Here, we identified the serum amyloid A1 protein-Toll-like receptor 4 (SAA1-TLR4) axis as an important link between inflammation and the outcome of TBI patients. Using serum and mRNA from white blood cells (WBC) of TBI patients, we found a positive correlation between serum SAA1 levels and injury severity, as well as with the 6-month outcome of TBI patients. SAA1 levels also correlate with the presence of TLR4 mRNA in WBC. In vitro, we found that SAA1 contributes to inflammation via TLR4 activation that releases inflammatory cytokines, which in turn increases SAA1 levels, establishing a positive proinflammatory loop. In vivo, post-TBI treatment with the TLR4-antagonist TAK242 reduces SAA1 levels, improves neurobehavioral outcome, and prevents blood–brain barrier disruption. Our data support further evaluation of (i) post-TBI treatment in the presence of TLR4 inhibition for limiting TBI-induced damage and (ii) SAA1-TLR4 as a biomarker of injury progression in TBI patients.


2015 ◽  
Vol 185 (10) ◽  
pp. 2641-2652 ◽  
Author(s):  
Sonia Villapol ◽  
Dmitry Kryndushkin ◽  
Maria G. Balarezo ◽  
Ashley M. Campbell ◽  
Juan M. Saavedra ◽  
...  

2021 ◽  
Vol 12 ◽  
Author(s):  
Ann-Kathrin Gaiser ◽  
Shanna Bauer ◽  
Stephanie Ruez ◽  
Karlheinz Holzmann ◽  
Marcus Fändrich ◽  
...  

AA amyloidosis belongs to the group of amyloid diseases which can follow chronic inflammatory conditions of various origin. The disease is characterized by the deposition of insoluble amyloid fibrils formed by serum amyloid A1 (SAA1) leading eventually to organ failure. Macrophages are intimately involved in the fibrillogenesis as well as in the clearance of amyloid fibrils. In vivo, macrophages may occur as classically (M1) or alternatively activated (M2) macrophages. We investigate here how SAA1 might affect the macrophage phenotype and function. Gene microarray analysis revealed upregulation of 64 M1-associated genes by SAA1. M1-like polarization was further confirmed by the expression of the M1-marker MARCO, activation of the NF-κB transcription factor, and secretion of the M1-cytokines TNF-α, IL-6, and MCP-1. Additionally, we demonstrate here that M1-polarized macrophages exhibit enhanced fibrillogenic activity towards SAA1. Based on our data, we propose reconsideration of the currently used cellular amyloidosis models towards an in vitro model employing M1-polarized macrophages. Furthermore, the data suggest macrophage repolarization as potential intervention strategy in AA amyloidosis.


2020 ◽  
Vol 85 ◽  
pp. 27-32
Author(s):  
Cheng Chang ◽  
Yilong Pan ◽  
Hongjiao Du ◽  
Xiao Wang ◽  
Xiaodong Li

1999 ◽  
Vol 274 (52) ◽  
pp. 37154-37160 ◽  
Author(s):  
Yongsheng Ren ◽  
Shrikanth A. G. Reddy ◽  
Warren S.-L. Liao

2011 ◽  
Author(s):  
Michael W. Schaffer ◽  
Joan C. Smith ◽  
Tanusri Ghosh Roy ◽  
Harold L. Moses ◽  
Samuel E. Adunyah ◽  
...  

2012 ◽  
Author(s):  
Hong Lok Lung ◽  
Arthur Kwok Leung Cheung ◽  
Yeung Man Chung ◽  
Edison Tak-Bun Liu ◽  
Daniel Chua ◽  
...  

Amyloid ◽  
1999 ◽  
Vol 6 (3) ◽  
pp. 199-204 ◽  
Author(s):  
Toshiyuki Yamada ◽  
Atsufumi Wada ◽  
Yoshihisa Itoh ◽  
Kouichi Itoh

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