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Natriuretic peptides inhibit adenylyl cyclase activity in dispersed eel gill cells

Callahan, W., Nankervis, S. and Toop, T. 2004, Natriuretic peptides inhibit adenylyl cyclase activity in dispersed eel gill cells, Journal of comparative physiology b: biochemical, systemic, and environmental physiology, vol. 174, no. 3, pp. 275-280, doi: 10.1007/s00360-003-0412-2.

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Title Natriuretic peptides inhibit adenylyl cyclase activity in dispersed eel gill cells
Author(s) Callahan, W.
Nankervis, S.
Toop, T.
Journal name Journal of comparative physiology b: biochemical, systemic, and environmental physiology
Volume number 174
Issue number 3
Start page 275
End page 280
Publisher Springer-Verlag
Place of publication Heidelberg, Germany
Publication date 2004-04
ISSN 0174-1578
1432-136X
Keyword(s) adenylyl cyclase
natriuretic peptide receptor
gill
eel
guanylyl cyclase
Summary The effect of natriuretic peptides on forskolin-evoked adenylyl cyclase activity was investigated in dispersed gill cells from the Australian short-finned eel (Anguilla australis). Molecular cloning techniques were employed to identify the putative G-protein-activating motif within the intracellular domain of the eel natriuretic peptide C receptor. Eel ANP, eel CNP and the NPR-C-specific C-ANF inhibited the forskolin-stimulated production of cyclic AMP. This effect was abolished by pretreatment of cells with pertussis toxin. Eel VNP was without effect on adenylyl cyclase activity. PCR and molecular cloning indicated that the intracellular domain of A. australis NPR-C has the same amino acid sequence as Anguilla japonica. Alignment of these sequences with Rattus norvegicus NPR-C indicated conservation of the putative G-protein-activating motif BB...BBXXB (B=basic, X=nonbasic residues). These data suggest that branchially-expressed NPR-C may play a physiological role additional to that of ligand clearance.
Language eng
DOI 10.1007/s00360-003-0412-2
Field of Research 070401 Aquaculture
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2004, Springer-Verlag
Persistent URL http://hdl.handle.net/10536/DRO/DU:30002693

Document type: Journal Article
Collection: School of Biological and Chemical Sciences
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