scholarly journals Proteolysis of serum amyloid A and AA amyloid proteins by cysteine proteases: cathepsin B generates AA amyloid proteins and cathepsin L may prevent their formation

2005 ◽  
Vol 64 (6) ◽  
pp. 808-815 ◽  
Author(s):  
C Rocken
Keyword(s):  
Cathepsin B ◽  
Serum Amyloid A ◽  
Cathepsin L ◽  
Cysteine Proteases ◽  
Serum Amyloid ◽  
Amyloid Proteins ◽  
Amyloid A

scholarly journals Serum Amyloid A Activates the NLRP3 Inflammasome via P2X7 Receptor and a Cathepsin B-Sensitive Pathway

2011 ◽  
Vol 186 (11) ◽  
pp. 6119-6128 ◽  
Author(s):  
Katri Niemi ◽  
Laura Teirilä ◽  
Jani Lappalainen ◽  
Kristiina Rajamäki ◽  
Marc H. Baumann ◽  
...  
Keyword(s):  
Nlrp3 Inflammasome ◽  
Cathepsin B ◽  
P2x7 Receptor ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

Comparison of AA Amyloid Fibril Morphology and Serum Amyloid A Gene Sequence in 5 Animal Species

2020 ◽  
pp. 030098582097049
Author(s):  
Xuguang Lin ◽  
Masahiro Kuragano ◽  
Kenichi Watanabe ◽  
Kiyotaka Tokuraku
Keyword(s):  
Serum Amyloid A ◽  
Animal Species ◽  
Amyloid Fibrils ◽  
Serum Amyloid ◽  
Amyloid Proteins ◽  
Electron Microscopic ◽  
Amyloid A ◽  
Genetic Homology ◽  
Fibril Morphology

Amyloid fibrils are characterized by a linear morphology and a cross-β structure. Polymorphic and multiple fibril morphologies can be found when amyloid fibrils are extracted from amyloid-laden tissue. In this study, we report on the purification and transmission electron microscopic analysis of amyloid fibrils from 5 different animal species (mouse, cow, goat, dog, and camel) with AA amyloidosis. The results show that amyloid fibrils had a linear morphology with a cross-structure and irregular length in vivo. Although the fibrils from these different species showed highly similar conformations, there were significant differences in fibril width and crossover distance. We analyzed the sequences of homologous amyloid proteins and serum amyloid A, an evolutionarily conserved protein and a major amyloid precursor. We found 78.23% homology between the most distant amyloid proteins. The findings suggested similar fibril width and crossover distance in different animal species that displayed high homology of amyloid protein sequences. Dog and camel, as well as goat and cow, showed high genetic homology and similar fibril morphology. These data indicate that the fibrils from different animal species have similar genetic homology and morphology, which may provide a better understanding of the pathogenesis of amyloidosis.

Serum Amyloid A in Healthy Female Bottlenose Dolphins (Tursiops truncatus) During and After Uncomplicated Pregnancy

2017 ◽  
Vol 43 (4) ◽  
pp. 417-420 ◽  
Author(s):  
Sarah N. Miller ◽  
Michelle Davis ◽  
Jorge A. Hernandez ◽  
Judy St. Leger ◽  
Carolyn Cray ◽  
...  
Keyword(s):  
Tursiops Truncatus ◽  
Serum Amyloid A ◽  
Bottlenose Dolphins ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Uncomplicated Pregnancy ◽  
Healthy Female
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