Natriuretic Peptides in Antarctic Teleosts and Cardiac Receptors
211
of binding sites specific for both ANP and BNP, and interacting with
BNP at different affinities was observed in the mammalian heart [28,29].
Recently, pBNP was shown to specifically bind two types ofNPRs in the
rectal gland of the elasmobranch Squalus acanthias [30]. Although BNP
has not yet been identified in fish, its high sequence homology with
respect to the other piscine NPs [31] suggests that in the various cardiac
regions of both notothenioids, and particularly in the atrium of T
bernacchii, NP sites able to bind a BNP-like peptide exist.
Since homologous NPs from both T bernacchii and C. hamatus are not
available, caution must be exercised in analyzing the results using
heterologous ligands. However, the present data are of interest in
relation to the presence of a heterogeneous NP system in Antarctic
teleosts whose potential physiological significance needs to be further
investigated.
Acknowledgments
This research was supported by the Italian National Programme for Antarctic
Research (PNRA) (B. Tota).
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