scholarly journals COX2 in a euryhaline teleost, Fundulus heteroclitus: primary sequence, distribution, localization, and potential function in gills during salinity acclimation

2006 ◽  
Vol 209 (9) ◽  
pp. 1696-1708 ◽  
Author(s):  
K. P. Choe
Keyword(s):  
Potential Function ◽  
Fundulus Heteroclitus ◽  
Primary Sequence ◽  
Salinity Acclimation ◽  
Sequence Distribution ◽  
Euryhaline Teleost

A novel 14-3-3 gene is osmoregulated in gill epithelium of the euryhaline teleost Fundulus heteroclitus

2001 ◽  
Vol 204 (17) ◽  
pp. 2975-2985 ◽  
Author(s):  
Dietmar Kültz ◽  
Devulapalli Chakravarty ◽  
Tadepalli Adilakshmi
Keyword(s):  
Signal Transduction ◽  
Amino Acid ◽  
Fundulus Heteroclitus ◽  
Sea Water ◽  
Amino Acid Residues ◽  
Gill Epithelium ◽  
Protein Levels ◽  
Euryhaline Teleost ◽  
Binding Groove ◽  
High Level

SUMMARY We have cloned and analyzed the full-length coding sequence and 3′ untranslated region (UTR) of a unique 14-3-3 gene of the euryhaline teleost Fundulus heteroclitus, which we named 14-3-3.a. Phylogenetic analysis of the deduced amino acid sequence revealed that the 14-3-3.a gene product is most similar to vertebrate 14-3-3ζ and β, yet it displays considerable divergence to known classes of vertebrate 14-3-3 isoforms. The N and C termini of 14-3-3.a are the most unique regions, whereas the amino acid residues forming the amphipathic ligand-binding groove are highly conserved. F. heteroclitus 14-3-3.a mRNA expression is high in gill epithelium, moderate in intestine and brain, and low in gonads, white muscle and heart. Because 14-3-3 proteins are important molecular scaffolds and cofactors for phosphoproteins and signaling complexes, the high level of 14-3-3.a expression in gill epithelium of the euryhaline teleost F. heteroclitus suggests that it is crucial for signal transduction in gill epithelial cells. We provide evidence that 14-3-3.a is involved in osmosensory signal transduction by showing that its mRNA and protein levels in gill epithelium, but not in any other tissue analyzed, increase two- to fourfold within 24h of salinity transfer of fish from sea water to fresh water. These data are clear evidence for an important role of 14-3-3.a in the remodeling of gill epithelium during transition of euryhaline fish between plasma-hyperosmotic and plasma-hyposmotic environments.

Ca2+ transport by opercular epithelium of the fresh water adapted euryhaline teleost, Fundulus heteroclitus

1995 ◽  
Vol 165 (4) ◽  
pp. 268-277 ◽  
Author(s):  
W. S. Marshall ◽  
S. E. Bryson ◽  
J. S. Burghardt ◽  
P. M. Verbost
Keyword(s):  
Fresh Water ◽  
Fundulus Heteroclitus ◽  
Euryhaline Teleost

Focal adhesion kinase and osmotic responses in ionocytes of Fundulus heteroclitus, a euryhaline teleost fish

2020 ◽  
Vol 241 ◽  
pp. 110639
Author(s):  
Breton Fougere ◽  
Katelyn R. Barnes ◽  
Magen E. Francis ◽  
Lauren N. Claus ◽  
Regina R.F. Cozzi ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Teleost Fish ◽  
Fundulus Heteroclitus ◽  
Euryhaline Teleost

A divergent CFTR homologue: highly regulated salt transport in the euryhaline teleost F. heteroclitus

1998 ◽  
Vol 274 (3) ◽  
pp. C715-C723 ◽  
Author(s):  
Thomas D. Singer ◽  
Stephen J. Tucker ◽  
William S. Marshall ◽  
Christopher F. Higgins
Keyword(s):  
Fundulus Heteroclitus ◽  
Xenopus Oocytes ◽  
Molecular Level ◽  
Protein Product ◽  
Salt Transport ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Euryhaline Teleost ◽  
Cystic Fibrosis Transmembrane

The killifish, Fundulus heteroclitus, is a euryhaline teleost fish capable of adapting rapidly to transfer from freshwater (FW) to four times seawater (SW). To investigate osmoregulation at a molecular level, a 5.7-kilobase cDNA homologous to human cystic fibrosis transmembrane conductance regulator (hCFTR) was isolated from a gill cDNA library from SW-adapted killifish. This cDNA encodes a protein product (kfCFTR) that is 59% identical to hCFTR, the most divergent form of CFTR characterized to date. Expression of kfCFTR in Xenopus oocytes generated adenosine 3′,5′-cyclic monophosphate-activated, Cl−-selective currents similar to those generated by hCFTR. In SW-adapted killifish, kfCFTR was expressed at high levels in the gill, opercular epithelium, and intestine. After abrupt exposure of FW-adapted killifish to SW, kfCFTR expression in the gill increased severalfold, suggesting a role for kfCFTR in salinity adaptation. Under similar conditions, plasma Na+levels rose significantly after 8 h and then fell, although it is not known whether these changes are directly responsible for the changes in kfCFTR expression. The killifish provides a unique opportunity to understand teleost osmoregulation and the role of CFTR.

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