Biological effects of rat iso-atrial natriuretic peptide and brain natriuretic peptide are indistinguishable from each other

Dennis A Wigle, B. M. Bennett, D. B. Jennings, I. R. Sarda, T. G. Flynn, S. C. Pang

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Rat brain natriuretic peptide (rBNP) and iso-atrial natriuretic peptide (iso-rANP) were discovered independently by two research laboratories. They are considered to be members of the B-type natriuretic peptides. Except for the Gln/Leu substitution at position 44, the amino acid sequence of iso-rANP is identical with that of the C-terminal 45 amino acids of rat pro-BNP and with the 5-kDa cardiac peptide from rat atria. To determine whether this amino acid substitution can modify the known biological effects of rBNP and iso-rANP, the present investigation examined the cardiovascular and renal responses, vasorelaxant effect, receptor binding characteristics, and cyclic GMP production by the two peptides in relation to that of rat atrial natriuretic peptide (rANP). Results indicate that rBNP and iso-rANP are indistinguishable from each other in terms of these known biological activities of atrial natriuretic peptide. We therefore conclude that rBNP and iso-rANP are identical peptides and that the amino acid substitution at position 44 represents a polymorphic form of the rat B-type natriuretic peptide.

Original languageEnglish (US)
Pages (from-to)1525-1528
Number of pages4
JournalCanadian Journal of Physiology and Pharmacology
Volume70
Issue number11
StatePublished - 1992
Externally publishedYes

Fingerprint

Brain Natriuretic Peptide
Amino Acid Substitution
Peptides
Cyclic GMP
Atrial Natriuretic Factor
Vasodilator Agents
Amino Acid Sequence
iso-atrial natriuretic peptide
rat atrial natriuretic peptide
Kidney
Amino Acids
rat natriuretic peptide precursor type B
Research

Keywords

  • atrial natriuretic peptide
  • brain natriuretic peptide
  • cardiovascular response
  • cyclic GMP
  • receptor binding
  • vasorelaxation

ASJC Scopus subject areas

  • Physiology
  • Pharmacology

Cite this

Biological effects of rat iso-atrial natriuretic peptide and brain natriuretic peptide are indistinguishable from each other. / Wigle, Dennis A; Bennett, B. M.; Jennings, D. B.; Sarda, I. R.; Flynn, T. G.; Pang, S. C.

In: Canadian Journal of Physiology and Pharmacology, Vol. 70, No. 11, 1992, p. 1525-1528.

Research output: Contribution to journalArticle

Wigle, Dennis A ; Bennett, B. M. ; Jennings, D. B. ; Sarda, I. R. ; Flynn, T. G. ; Pang, S. C. / Biological effects of rat iso-atrial natriuretic peptide and brain natriuretic peptide are indistinguishable from each other. In: Canadian Journal of Physiology and Pharmacology. 1992 ; Vol. 70, No. 11. pp. 1525-1528.
@article{08e2d2929ec84048ab8a5680693230da,
title = "Biological effects of rat iso-atrial natriuretic peptide and brain natriuretic peptide are indistinguishable from each other",
abstract = "Rat brain natriuretic peptide (rBNP) and iso-atrial natriuretic peptide (iso-rANP) were discovered independently by two research laboratories. They are considered to be members of the B-type natriuretic peptides. Except for the Gln/Leu substitution at position 44, the amino acid sequence of iso-rANP is identical with that of the C-terminal 45 amino acids of rat pro-BNP and with the 5-kDa cardiac peptide from rat atria. To determine whether this amino acid substitution can modify the known biological effects of rBNP and iso-rANP, the present investigation examined the cardiovascular and renal responses, vasorelaxant effect, receptor binding characteristics, and cyclic GMP production by the two peptides in relation to that of rat atrial natriuretic peptide (rANP). Results indicate that rBNP and iso-rANP are indistinguishable from each other in terms of these known biological activities of atrial natriuretic peptide. We therefore conclude that rBNP and iso-rANP are identical peptides and that the amino acid substitution at position 44 represents a polymorphic form of the rat B-type natriuretic peptide.",
keywords = "atrial natriuretic peptide, brain natriuretic peptide, cardiovascular response, cyclic GMP, receptor binding, vasorelaxation",
author = "Wigle, {Dennis A} and Bennett, {B. M.} and Jennings, {D. B.} and Sarda, {I. R.} and Flynn, {T. G.} and Pang, {S. C.}",
year = "1992",
language = "English (US)",
volume = "70",
pages = "1525--1528",
journal = "Canadian Journal of Physiology and Pharmacology",
issn = "0008-4212",
publisher = "National Research Council of Canada",
number = "11",

}

TY - JOUR

T1 - Biological effects of rat iso-atrial natriuretic peptide and brain natriuretic peptide are indistinguishable from each other

AU - Wigle, Dennis A

AU - Bennett, B. M.

AU - Jennings, D. B.

AU - Sarda, I. R.

AU - Flynn, T. G.

AU - Pang, S. C.

PY - 1992

Y1 - 1992

N2 - Rat brain natriuretic peptide (rBNP) and iso-atrial natriuretic peptide (iso-rANP) were discovered independently by two research laboratories. They are considered to be members of the B-type natriuretic peptides. Except for the Gln/Leu substitution at position 44, the amino acid sequence of iso-rANP is identical with that of the C-terminal 45 amino acids of rat pro-BNP and with the 5-kDa cardiac peptide from rat atria. To determine whether this amino acid substitution can modify the known biological effects of rBNP and iso-rANP, the present investigation examined the cardiovascular and renal responses, vasorelaxant effect, receptor binding characteristics, and cyclic GMP production by the two peptides in relation to that of rat atrial natriuretic peptide (rANP). Results indicate that rBNP and iso-rANP are indistinguishable from each other in terms of these known biological activities of atrial natriuretic peptide. We therefore conclude that rBNP and iso-rANP are identical peptides and that the amino acid substitution at position 44 represents a polymorphic form of the rat B-type natriuretic peptide.

AB - Rat brain natriuretic peptide (rBNP) and iso-atrial natriuretic peptide (iso-rANP) were discovered independently by two research laboratories. They are considered to be members of the B-type natriuretic peptides. Except for the Gln/Leu substitution at position 44, the amino acid sequence of iso-rANP is identical with that of the C-terminal 45 amino acids of rat pro-BNP and with the 5-kDa cardiac peptide from rat atria. To determine whether this amino acid substitution can modify the known biological effects of rBNP and iso-rANP, the present investigation examined the cardiovascular and renal responses, vasorelaxant effect, receptor binding characteristics, and cyclic GMP production by the two peptides in relation to that of rat atrial natriuretic peptide (rANP). Results indicate that rBNP and iso-rANP are indistinguishable from each other in terms of these known biological activities of atrial natriuretic peptide. We therefore conclude that rBNP and iso-rANP are identical peptides and that the amino acid substitution at position 44 represents a polymorphic form of the rat B-type natriuretic peptide.

KW - atrial natriuretic peptide

KW - brain natriuretic peptide

KW - cardiovascular response

KW - cyclic GMP

KW - receptor binding

KW - vasorelaxation

UR - http://www.scopus.com/inward/record.url?scp=0027052062&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027052062&partnerID=8YFLogxK

M3 - Article

VL - 70

SP - 1525

EP - 1528

JO - Canadian Journal of Physiology and Pharmacology

JF - Canadian Journal of Physiology and Pharmacology

SN - 0008-4212

IS - 11

ER -