scholarly journals Role of the nucleotide-binding domain-like receptor protein 3 inflammasome in acute kidney injury

FEBS Journal ◽  
2015 ◽  
Vol 282 (19) ◽  
pp. 3799-3807 ◽  
Author(s):  
Yanhui Cao ◽  
Dongsheng Fei ◽  
Mingwei Chen ◽  
Miao Sun ◽  
Jun Xu ◽  
...  
Keyword(s):  
Acute Kidney Injury ◽  
Kidney Injury ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Receptor Protein ◽  
Nucleotide Binding Domain

Role of the Nucleotide-Binding Domain-Like Receptor Protein 3 Inflammasome in the Endothelial Dysfunction of Early Sepsis

Inflammation ◽  
2020 ◽  
Vol 43 (4) ◽  
pp. 1561-1571 ◽  
Author(s):  
Minghao Luo ◽  
Jiayu Meng ◽  
Jianghong Yan ◽  
Feifei Shang ◽  
Ting Zhang ◽  
...  
Keyword(s):  
Endothelial Dysfunction ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Receptor Protein ◽  
Nucleotide Binding Domain ◽  
Early Sepsis

scholarly journals The Emerging Role of Inflammasomes as Central Mediators in Inflammatory Bladder Pathology

2017 ◽  
Vol 11 (2) ◽  
pp. 57-72 ◽  
Author(s):  
Brian M. Inouye ◽  
Francis M. Hughes,Jr ◽  
Stephanie J. Sexton ◽  
J. Todd Purves
Keyword(s):  
Outlet Obstruction ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Pyrin Domain ◽  
Voiding Symptoms ◽  
Bladder Pathology ◽  
Tract Infections ◽  
Underlying Inflammation

Irritative voiding symptoms (e.g. increased frequency and urgency) occur in many common pathologic conditions such as urinary tract infections and bladder outlet obstruction, and these conditions are well-established to have underlying inflammation that directly triggers these symptoms. However, it remains unclear as to how such diverse stimuli individually generate a common inflammatory process. Jürg Tschopp provided substantial insight into this conundrum when, working with extracts from THP-1 cells, he reported the existence of the inflammasome. He described it as a structure that senses multiple diverse signals from intracellular/extracellular sources and pathogens and triggers inflammation by the maturation and release of the pro-inflammatory cytokines interleukin-1β and interleukin-18. Recently, many of these sensors were found in the bladder and the nucleotide-binding domain, leucine-rich-containing family, pyrin domain-containing-3, has been shown to be a central mediator of inflammation in several urological diseases. In this review, we introduce the nucleotide-binding domain, leucine-rich-containing family, pyrin domaincontaining-3 inflammasome, highlight its emerging role in several common urologic conditions, and speculate on the potential involvement of other inflammasomes in bladder pathology.

scholarly journals Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities

2011 ◽  
Vol 17 (3) ◽  
pp. 361-373 ◽  
Author(s):  
Łukasz Nowicki ◽  
Paweł Leźnicki ◽  
Ewa Morawiec ◽  
Natalia Litwińczuk ◽  
Krzysztof Liberek
Keyword(s):  
Aspartic Acid ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Nucleotide Binding Domain 1 ◽  
Hsp100 Chaperones

scholarly journals The Spodoptera exigua ABCC2 Acts as a Cry1A Receptor Independently of its Nucleotide Binding Domain II

Toxins ◽  
2019 ◽  
Vol 11 (3) ◽  
pp. 172 ◽  
Author(s):  
Daniel Pinos ◽  
María Martínez-Solís ◽  
Salvador Herrero ◽  
Juan Ferré ◽  
Patricia Hernández-Martínez
Keyword(s):  
Spodoptera Exigua ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Truncated Form ◽  
Extracellular Loops ◽  
Hydrolysis Of ◽  
Functional Receptor ◽  
Abcc2 Transporter

ABC proteins are primary-active transporters that require the binding and hydrolysis of ATP to transport substrates across the membrane. Since the first report of an ABCC2 transporter as receptor of Cry1A toxins, the number of ABC transporters known to be involved in the mode of action of Cry toxins has increased. In Spodoptera exigua, a mutation in the SeABCC2 gene is described as genetically linked to resistance to the Bt-product XentariTM. This mutation affects an intracellular domain involved in ATP binding, but not the extracellular loops. We analyzed whether this mutation affects the role of the SeABCC2 as a functional receptor to Cry1A toxins. The results show that Sf21 cells expressing the truncated form of the transporter were susceptible to Cry1A toxins. Moreover, specific Cry1Ac binding was observed in those cells expressing the truncated SeABCC2. Additionally, no differences in the irreversible Cry1Ac binding component (associated with the toxin insertion into the membrane) were observed when tested in Sf21 cells expressing either the full-length or the truncated form of the SeABCC2 transporter. Therefore, our results point out that the partial lack of the nucleotide binding domain II in the truncated transporter does not affect its functionality as a Cry1A receptor.

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