NMR study of the possible interaction in solution of angiotensin II with a peptide encoded by angiotensin II complementary RNA.

Eaton, H. L.; Austin, Richard E.; Fesik, Stephen W.; Martin, Stephen F.

doi:10.1073/pnas.86.24.9767

Cited by 13 publications

(13 citation statements)

References 15 publications

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“…No interaction between angiotensin I1 and its antisense peptide could be found by Guillemette et al (1989), De Gasparo et ul. (1989 or Eaton et al (1989) or between adrenocorticotropin and its antisense peptide (Najem et al, 1989: Eberle andHuber, 1991). Furthermore, Biro (Segersteen et al, 1986) has recanted his original findings of the statistical significance of ligand-receptor mRNA complementarity.…”

Section: Criticism Of the Theorymentioning

confidence: 99%

Making sense from antisense: A review of experimental data and developing ideas on sense–antisense peptide recognition

Tropsha

Kizer

Chaiken

1992

J of Molecular Recognition

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Peptides encoded in the antisense strand of DNA have been predicted and found experimentally to bind to sense peptides and proteins with significant selectivity and affinity. Such sense--antisense peptide recognition has been observed in many systems, most often by detecting binding between immobilized and soluble interaction partners. Data obtained so far on sequence and solvent dependence of interaction support a hydrophobic-hydrophilic (amphipathic) model of peptide recognition. Nonetheless, the mechanistic understanding of this type of molecular recognition remains incomplete. Improving this understanding likely will require expanding the types of characteristics measured for sense--antisense peptide complexes and hence the types of analytical methods applied to such interactions. Understanding the mechanism of sense--antisense peptide recognition also may provide insights into mechanisms of native (sense) peptide and protein interactions and protein folding. Such insight may be helpful to learn how to design macromolecular recognition agents in technology for separation, diagnostics and therapeutics.

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Section: Criticism Of the Theorymentioning

confidence: 99%

Making sense from antisense: A review of experimental data and developing ideas on sense–antisense peptide recognition

Tropsha

Kizer

Chaiken

1992

J of Molecular Recognition

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“…This approach was recently used by Eaton et al 14 to study potential interactions between rat II Ang and Ang II, and we have followed their method closely. Briefly, anhydrous sodium phosphate monobasic and dibasic (Al-…”

Section: Study Dmentioning

confidence: 99%

“…13 In addition, anti-rat II Ang did not inhibit 125 I-Ang II binding to rat smooth muscle cell membranes. 13 Finally, in an elegant study, Eaton et al 14 failed to detect any interaction between Ang II and rat II Ang by NMR spectroscopy. Therefore, it remains controversial whether rat II Ang can inhibit interactions of Ang II with its receptor.…”

mentioning

confidence: 99%

Studies on the peptides encoded by rat and human angiotensin II complementary RNA.

1993

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Some evidence suggests that RNA complementary to the messenger RNA encoding a peptide hormone encodes a complementary peptide that binds the original peptide hormone. The objective of this investigation was to assess in vivo the ability of complementary angiotensin II (II Ang) peptides to block the biological effects of angiotensin II (Ang II). Increasing concentrations of rat or human II Ang were preincubated with Ang II for 2 hours, and this solution was then infused intra-arterially into the superior mesenteric artery. Human, but not rat, II Ang dose-dependently inhibited Ang N-induced mesenteric vasoconstriction. The in vivo inhibitory potencies of human II Ang and [Sar',Ile 8 ] Ang II, with respect to inhibition of the pressor response to Ang II, were compared by infusing intravenously increasing doses of each blocker and determining their effects on a fixed intravenous dose of Ang II. Although human II Ang could abolish the pressor response to Ang II, [Sar',Ile 8 ] Ang II was approximately 100 times more potent in this regard. A fixed dose of human II Ang (150 /ig/min i.v.) inhibited the effects of increasing doses of Ang II on mesenteric vascular resistance, arterial blood pressure, and aldosterone secretion. The 'H nuclear magnetic resonance spectra of human II Ang and Ang II were determined both separately and when combined in the same cuvette. The spectrum obtained by overlaying the separate spectra for these two peptides was the same as the spectrum obtained from the mixture of these two peptides in the same cuvette. These studies indicate that human, but not rat, II Ang blocks the in vivo effects of Ang II; however, this blockade is mediated by receptor antagonism and not via direct binding to Ang II.

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“…On this basis, the peptide coded by the complementary nucleo tide sequence of angiotensin II was synthesized, and anti bodies were raised against this peptide. These antibodies allowed to purify and characterize a 66-kD protein which seems to be an angiotensin-II-binding protein [20], How ever, a recent NMR study demonstrating the absence of physical interaction between angiotensin II and its anti peptide introduced some doubt about the scientific reality of this approach [21].…”

Section: Analogical Cloningmentioning

confidence: 99%

The Difficult Challenge of Cloning the Angiotensin II Receptor

Weber

Monnot²,

Bihoreau³

et al. 1990

Horm Res

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The vasopressor peptide angiotensin II exerts its cellular effects through a membrane-bound receptor coupled to a G protein. Biochemical and pharmacological analyses of this receptor already identify two different membrane-bound receptors and one cytosoluble angiotensin-II-binding protein. Nevertheless, the purification of the membrane-bound form(s) appears to be difficult. In the absence of purified protein, two cloning strategies of the gene have been explored: (1) expression cloning, identifying the functions of the protein expressed from a cDNA library in COS cells or Xenopus oocytes, has been unsuccessful until now; (2) analogical cloning, trying to identify related members of the seven transmembrane segment receptor family, which could be related to angiotensin receptors, identifies the mas oncogene and two related genes. However, there are accumulating data to exclude their involvement in angiotensin binding.

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NMR study of the possible interaction in solution of angiotensin II with a peptide encoded by angiotensin II complementary RNA.

Abstract: The potential binding of angiotensin II (AspArg-Val-Tyr-Ile-His-Pro-Phe) (All) to a peptide encoded by its complementary RNA (Lys-Gly-Val-Asp-Val-Tyr-Ala-Val)

Cited by 13 publications

References 15 publications

Making sense from antisense: A review of experimental data and developing ideas on sense–antisense peptide recognition

Making sense from antisense: A review of experimental data and developing ideas on sense–antisense peptide recognition

Studies on the peptides encoded by rat and human angiotensin II complementary RNA.

The Difficult Challenge of Cloning the Angiotensin II Receptor

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