Abstract
Angiotensin I (ANG I) was produced from the incubation of lungfish plasma with homologous kidney extracts. The purified peptide was found to have the sequence of H-Asn-Arg-Val-Tyr-Val-His-Pro-Phe-Thr-Leu-OH, which is homologous for the first eight residues with all teleost angiotensins so far sequenced, although lungfish generally possess tetrapod-type hormones. The lungfish decapeptide (ANG I) induced dose-dependent increases in arterial pressure in the rat. The lungfish octapeptide (ANG II) released aldosterone from kidney-adrenal tissue in vitro in a dose-dependent manner and induced dose-dependent increases in arterial pressure of the lung fish. Substitution of asparagine with aspartic acid in the first position (tetrapod-type ANG II) did not alter the blood pressure response significantly, but a second substitution of the valine in the (5)-position with isoleucine (ANG II form found in human and rat) abolished the rise in arterial pressure in lung fish over the same dose range.
Original language | English |
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Pages (from-to) | 206-212 |
Number of pages | 7 |
Journal | General and Comparative Endocrinology |
Volume | 114 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1999 |
Keywords
- Aldosterone
- Angiotensin
- Lungfish
- Neoceratodus
- Vasopressor