Chemical structure of angiotensin in the turtle, Pseudemys scripta

doi:10.1016/0016-6480(84)90236-3

General and Comparative Endocrinology

Volume 53, Issue 1, January 1984, Pages 159-162

https://doi.org/10.1016/0016-6480(84)90236-3 Get rights and content

Abstract

The chemical structure of angiotensin generated by incubating kidney extract with homologous plasma from the turtle, Pseudemys scripta, has been analyzed. The turtle angiotensin was proposed to be [Asp¹, Val⁵, His⁹] ANG I by its amino acid composition and by its fluorescent peptide mapping. It was the same structure as angiotensin I in the ox and the sheep. The N-terminal amino acid of the turtle angiotensin was not blocked, unlike that of another reptilian angiotensin found in the snake, Elaphe climacophora.

References (8)

Y. Hasegawa et al.
Chemical structure of angiotensin in the bullfrog Rana catesbeiana
Gen. Comp. Endocrinol
(1983)
T. Nakajima et al.
Examination of angiotensin-like substances from renal and extrarenal sources in mammalian and nonmammalian species
Gen. Comp. Endocrinol
(1971)
G.A. Stephens
Blockade of angiotensin pressor activity in the freshwater turtle
Gen. Comp. Endocrinol
(1981)
Y. Takemoto et al.
Chemical structures of angiotensins formed by incubating plasma with the kidney and the corpuscles of Stannius in the chum salmon, Oncorhynchus keta
Gen. Comp. Endocrinol
(1983)

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Cited by (19)

Pressor responses to alligator Angiotensin I and some analogs in the spectacled caiman (Caiman crocodilus)
2006, General and Comparative Endocrinology
Discovery of the chemical structure of alligator (Alligator mississipiensis) [Asp¹, Val⁵, Ala⁹]-Angiotensin I (ANG I) has permitted the investigation of cardiovascular responses to this peptide and its analogs in spectacled caimans (Caiman crocodilus), close relatives of alligators. ANG I and [Asp¹, Val⁵]- Angiotensin II (ANG II) i.v. gave dose-dependent increases in mean arterial pressure but there was no pressor response to [Val⁴]-ANG III (ANG III). Pressor responses to a series of doses of ANG II were compared with a range of doses of norepinephrine (NE) and epinephrine (E) which were found to be only about 1/100 as potent as ANG II on a molar basis. The replacement of d-leu¹⁰in the alligator ANG I molecule with l-leu¹⁰ almost stopped its conversion to ANG II and attenuated the pressor response. [Asp¹, Val⁵, Ala⁹]-ANG I (1–9), and ANG (1–7) both failed to increase arterial blood pressure, even at the relatively high non-physiological test dose of 194 pmol kg bw⁻¹ i.v. Captopril blocked angiotensin converting enzyme (ACE) and prevented the pressor response to ANG I whereas the mammalian AT₁ inhibitor Losartan attenuated, but did not completely block the pressor response to ANG II. These are the first experiments which test the cardiovascular responses to alligator ANG I and its analogues in any crocodilian species.
Isolation, synthesis, and biological activity of flounder [Asn1, Ile5, Thr9] angiotensin I
2003, General and Comparative Endocrinology
A novel angiotensin I (ANG I) has been isolated from incubates of plasma and kidney extracts of the flounder, Platichthys flesus, using ion-exchange, gel-permeation, and reverse-phase high performance liquid chromatography (HPLC). Its sequence was determined as H–Asn–Arg–Val–Tyr–Ile–His–Pro–Phe–Thr–Leu–OH by sequence analysis and mass spectrometry. No vasopressor activity was detected at the elution position of [Asp¹] ANG I in ion-exchange HPLC. The sequence was confirmed by identity of the elution position with the synthetic peptide in two different HPLC systems. When compared with ANG I isolated from other teleost fish, flounder ANG I uniquely has an isoleucine at position 5 rather than valine. Injection of angiotensin II (ANG II) into chronically cannulated flounder resulted in a dose-dependent pressor response, native [ $Asn^{1}, Ile^{5}$ ] ANG II, was found to elicit pressor responses comparable with those seen when teleost [ $Asn^{1}, Val^{5}$ ] ANG II and human [ $Asp^{1}, Ile^{5}$ ] ANG II were injected into flounder over the dose range 0.02–1.00 nmol/kg⁻¹. Plasma concentrations of the neurohypophysial peptide AVT were measured in chronically cannulated flounder following the injection of ANG II to examine the effect of ANG II on circulating AVT concentration. The injection of [ $Asn^{1}, Ile^{5}$ ] ANG II (1 nmol kg⁻¹) or [ $Asp^{1}, Ile^{5}$ ] ANG II (2.5 nmol kg⁻¹) resulted in a significant fall in the circulating levels of AVT suggesting that ANG II either directly or indirectly negatively influences AVT secretion.
Angiotensin receptors - Evolutionary overview and perspectives
2001, Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology
The structure of the angiotensin molecule has been well preserved throughout the vertebrate scale with some amino acid variations. Specific angiotensin receptors (AT receptors) that mediate important physiological functions have been noted in a variety of tissues and species. Physiological and pharmacological characterization of AT receptors and, more recently, molecular cloning studies have elucidated the presence of AT receptor subtypes. Comparative studies suggest that an AT receptor subtype homologous to the mammalian type 1 receptor subtype (AT₁), though pharmacologically distinct, is present in amphibians and birds, whereas AT receptors cloned from teleosts show low homology to both AT₁ and AT₂ receptor subtypes. Furthermore, receptors differing from both the AT₁-homologue receptor and AT₂ receptor exist in some non-mammalian species. This may suggest that the prototype AT receptor evolved in primitive vertebrates and diverged to more than one type of AT receptor subtype during phylogeny. Furthermore, phenotypic modulation of AT receptors appears to occur during individual development/maturation.
Isolation and identification of angiotensin-like peptides from the plasma of the snake Bothrops jararaca
1996, Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Two distinct hypertensive peptides were purified and characterized from Bothrops jararaca (Bj) plasma incubated at pH 4, 37°C, 24 hr. These peptides were active on rat and Bj blood pressure, on rat isolated uterus, on guinea pig isolated ileum and on Bj isolated duodenum. At the releasing conditions no further activities were found for kininases, angiotensinases or angiotensin converting enzymes. The peptides were purified by ethanol/ether extraction, Sephadex G-25 gel filtration, semipreparative reverse-phase (C-18) HPLC and analytical (C-18) HPLC. The amino-acid sequences of the purified peptides corresponded to (Ile⁵)AII and (Val⁵-Tyr⁹)AI and their molecular masses were confirmed by mass spectrometry as 1046.6 and 1348.0 respectively. The presence of those two angiotensins on Bj plasma may have some evolutionary significance since (Ile⁵)AII is known as a mammalian angiotensin and (Val⁵)AII as a non-mammalian one.
New Angiotensin I Isolated from a Reptile, Alligator mississippiensis
1993, General and Comparative Endocrinology
Angiotensin I (ANG I) of the American alligator Alligator mississippiensis was isolated from incubates of homologous plasma and kidney extract, and its amino acid sequence was determined as H-Asp-Arg-Val-Tyr-Val-His-Pro-Phe-Ala-Leu-OH. The presence of strongly hydrophobic alanine at position 9 is unusual among ANGs I sequenced to date. Since alanine can be converted to serine by a one-point mutation of the triplet nucleotides, the phylogenetic proximity of the alligator to birds, whose ANG I has serine at position 9, is confirmed by the chemical evolution of the hormone structure. The alligator [Asp¹,Val⁵,Ala⁹] ANG I increased arterial blood pressure of conscious alligators, but it was no more potent than avian [Asp¹,Val⁵,Ser⁹ ANG I. The alligator ANG I was also equipotent to the homologous ANG I in the quail and rat. It is concluded that substitutions at position 9 have little influence on the vasopressor activity of ANG I.
The pressor response to exogenous angiotensin I and its blockade by angiotensin II analogues in the American alligator
1992, General and Comparative Endocrinology
We examined the pressor response to exogenous, nonnative angiotensin I (ANG I; bullfrog, turtle, and fowl) in the conscious American alligator, Alligator mississippiensis. In addition, the inhibitory effects of three ANG II analogues ([Sar¹, Ala⁸], [Sar¹, Thr⁸], and [Sar¹, Ile⁸]ANG II) on the pressor responses to angiotensin I (fowl ANG I, [Asp¹, Val⁵, Ser⁹]) were also examined. Intravenous administration of bullfrog, turtle, and fowl ANG I at 0.1, 0.5, and 1.0 μg/kg produced dose-dependent increases in arterial blood pressure. [Val⁵]ANG II at 0.05, 0.1, and 0.5 μg/kg, or NE at 2 μg/kg also produced dose-dependent increases in blood pressure. [Sar¹, Ile⁸]ANG II and [Sar¹, Ala⁸]ANG II (10 μg/kg/min) both attenuated the pressor response to fowl ANG I whereas [Sar¹, Thr⁸]ANG II (10 μg/kg/min) produced no significant blockade. These data demonstrate: (1) All three exogenous ANG I molecules exert potent vasopressor responses in the alligator, (2) [Sar¹, Ile⁸]ANG II is the most effective ANG antagonist, and (3) the alligator appears to possess a renin-angiotensin system similar to that found in other vertebrates.

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General and Comparative Endocrinology

Abstract

References (8)

Chemical structure of angiotensin in the bullfrog Rana catesbeiana

Gen. Comp. Endocrinol

Examination of angiotensin-like substances from renal and extrarenal sources in mammalian and nonmammalian species

Gen. Comp. Endocrinol

Blockade of angiotensin pressor activity in the freshwater turtle

Gen. Comp. Endocrinol

Chemical structures of angiotensins formed by incubating plasma with the kidney and the corpuscles of Stannius in the chum salmon, Oncorhynchus keta

Gen. Comp. Endocrinol

Cited by (19)

Pressor responses to alligator Angiotensin I and some analogs in the spectacled caiman (Caiman crocodilus)

Isolation, synthesis, and biological activity of flounder [Asn<sup>1</sup>, Ile<sup>5</sup>, Thr<sup>9</sup>] angiotensin I

Angiotensin receptors - Evolutionary overview and perspectives

Isolation and identification of angiotensin-like peptides from the plasma of the snake Bothrops jararaca

New Angiotensin I Isolated from a Reptile, Alligator mississippiensis

The pressor response to exogenous angiotensin I and its blockade by angiotensin II analogues in the American alligator