C-type natriuretic peptide regulates the molecular components of the rainbow trout gill epithelium tight junction complex

Peptides ◽  
2020 ◽  
Vol 124 ◽  
pp. 170211 ◽  
Author(s):  
Dennis Kolosov ◽  
Scott P. Kelly
2018 ◽  
Vol 315 (2) ◽  
pp. R312-R322 ◽  
Author(s):  
Dennis Kolosov ◽  
Scott P. Kelly

Molecular physiology of the tricellular tight junction (tTJ)-associated proteins lipolysis-stimulated lipoprotein receptor ( lsr, = angulin-1) and an immunoglobulin-like domain-containing receptor ( ildr2, ≈angulin-3) was examined in model trout gill epithelia. Transcripts encoding lsr and ildr2 are broadly expressed in trout organs. A reduction in lsr and ildr2 mRNA abundance was observed during and after confluence in flask-cultured gill cells. In contrast, as high-resistance and low-permeability characteristics developed in a model gill epithelium cultured on permeable polyethylene terephthalate membrane inserts, lsr and ildr2 transcript abundance increased. However, as epithelia entered the developmental plateau phase, lsr abundance returned to initial values, while ildr2 transcript abundance remained elevated. When mitochondrion-rich cells were introduced to model preparations, lsr mRNA abundance was unaltered and ildr2 mRNA abundance significantly increased. Transcript abundance of ildr2 was not altered in association with corticosteroid-induced tightening of the gill epithelium, while lsr mRNA abundance decreased. Transcriptional knockdown of the tTJ protein tricelluin (Tric) reduced Tric abundance, increased gill epithelium permeability, and increased lsr without significantly altering ildr2 transcript abundance. Data suggest that angulins contribute to fish gill epithelium barrier properties but that Lsr and Ildr2 seem likely to play different roles. This is because ildr2 typically exhibited increased abundance in association with decreased model permeability, while lsr abundance changed in a manner that suggested a role in Tric recruitment to the tTJ.


2016 ◽  
Vol 53 ◽  
pp. 82-83 ◽  
Author(s):  
Goshi Kato ◽  
Haruya Miyazawa ◽  
Takuya Yamaguchi ◽  
Hidehiro Kondo ◽  
Motohiko Sano ◽  
...  

Heliyon ◽  
2021 ◽  
Vol 7 (9) ◽  
pp. e08018
Author(s):  
Kafilat Adebola Bawa-Allah ◽  
Adebayo Otitoloju ◽  
Christer Hogstrand

2011 ◽  
Vol 214 (9) ◽  
pp. 1473-1487 ◽  
Author(s):  
A. M. Sandbichler ◽  
M. Egg ◽  
T. Schwerte ◽  
B. Pelster

2021 ◽  
Vol 9 (6) ◽  
pp. 1258
Author(s):  
Kerrie Ní Ní Dhufaigh ◽  
Natasha Botwright ◽  
Eugene Dillon ◽  
Ian O’Connor ◽  
Eugene MacCarthy ◽  
...  

Infection with the protozoan ectoparasite Neoparamoeba perurans, the causative agent of AGD, remains a global threat to salmonid farming. This study aimed to analyse the exoproteome of both an attenuated and virulent N. perurans isolate using proteomics and cytotoxicity testing. A disproportionate presence of proteins from the co-cultured microbiota of N. perurans was revealed on searching an amalgamated database of bacterial, N. perurans and Amoebozoa proteins. LC‑MS/MS identified 33 differentially expressed proteins, the majority of which were upregulated in the attenuated exoproteome. Proteins of putative interest found in both exoproteomes were maltoporin, ferrichrome-iron receptor, and putative ferric enterobactin receptor. Protease activity remained significantly elevated in the attenuated exoproteome compared with the virulent exoproteome. Similarly, the attenuated exoproteome had a significantly higher cytotoxic effect on rainbow trout gill cell line (RTgill W1) cells compared with the virulent exoproteome. The presence of a phosphatase and serine protease in the virulent exoproteome may facilitate AGD infection but do not appear to be key players in causing cytotoxicity. Altogether, this study reveals prolonged culture of N. perurans affects the exoproteome composition in favour of nutritional acquisition, and that the current culturing protocol for virulent N. perurans does not facilitate the secretion of virulence factors.


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