ANP, BNP and CNP: Physiology and Pharmacology of the Cardiorenal Axis

Candace Y W Lee, John C Jr. Burnett

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

Abstract

The three mammalian natriuretic peptides (NPs), A-type natriuretic peptide (ANP), B-type natriuretic peptide (BNP), and C-type natriuretic peptide (CNP), are genetically distinct but share structural similarities. Human ANP, BNP, and CNP are synthesized as preprohormones, which are subsequently split into prohormones by proteolytic cleavage of an N-terminal signal peptide. Human prepro-ANP is a 151-amino acid (AA) peptide that is cleaved to the 126-AA pro-ANP, whereas human prepro-BNP is a 134-AA peptide that is cleaved to the 108-AA pro-BNP. Pro-ANP and pro-BNP are stored in secretory granules in atrial cardiomyocytes and are cleaved to form ANP and BNP, respectively, upon secretion. The conversion of pro-ANP to ANP is mediated by corin, a transmembrane cardiac serine protease. Both human ANP, a 28-AA peptide, and human BNP, a 32-AA peptide, are released from the myocardium in response to various physiologic and pathophysiologic stimuli, such as myocardial wall stretch. Human pro-CNP consists of 103 AA residues and is processed by furin, an intracellular endoprotease, to the mature 53-AA CNP. CNP-53, which is found primarily in the brain, the heart, and endothelial cells, may be further cleaved to CNP-22.

Original languageEnglish (US)
Title of host publicationTextbook of Nephro-Endocrinology
PublisherElsevier Inc.
Pages287-307
Number of pages21
ISBN (Print)9780123738707
DOIs
StatePublished - 2008

Fingerprint

C-Type Natriuretic Peptide
Natriuretic Peptides
Brain Natriuretic Peptide
Pharmacology
Amino Acids
Peptides
polypeptide C
Furin
Secretory Vesicles
Serine Proteases
Protein Sorting Signals
Cardiac Myocytes
Myocardium
Endothelial Cells

ASJC Scopus subject areas

  • Dentistry(all)
  • Medicine(all)

Cite this

ANP, BNP and CNP : Physiology and Pharmacology of the Cardiorenal Axis. / Lee, Candace Y W; Burnett, John C Jr.

Textbook of Nephro-Endocrinology. Elsevier Inc., 2008. p. 287-307.

Research output: Chapter in Book/Report/Conference proceedingChapter

Lee, Candace Y W ; Burnett, John C Jr. / ANP, BNP and CNP : Physiology and Pharmacology of the Cardiorenal Axis. Textbook of Nephro-Endocrinology. Elsevier Inc., 2008. pp. 287-307
@inbook{87ca316302ed4f889e7cccf004965f6e,
title = "ANP, BNP and CNP: Physiology and Pharmacology of the Cardiorenal Axis",
abstract = "The three mammalian natriuretic peptides (NPs), A-type natriuretic peptide (ANP), B-type natriuretic peptide (BNP), and C-type natriuretic peptide (CNP), are genetically distinct but share structural similarities. Human ANP, BNP, and CNP are synthesized as preprohormones, which are subsequently split into prohormones by proteolytic cleavage of an N-terminal signal peptide. Human prepro-ANP is a 151-amino acid (AA) peptide that is cleaved to the 126-AA pro-ANP, whereas human prepro-BNP is a 134-AA peptide that is cleaved to the 108-AA pro-BNP. Pro-ANP and pro-BNP are stored in secretory granules in atrial cardiomyocytes and are cleaved to form ANP and BNP, respectively, upon secretion. The conversion of pro-ANP to ANP is mediated by corin, a transmembrane cardiac serine protease. Both human ANP, a 28-AA peptide, and human BNP, a 32-AA peptide, are released from the myocardium in response to various physiologic and pathophysiologic stimuli, such as myocardial wall stretch. Human pro-CNP consists of 103 AA residues and is processed by furin, an intracellular endoprotease, to the mature 53-AA CNP. CNP-53, which is found primarily in the brain, the heart, and endothelial cells, may be further cleaved to CNP-22.",
author = "Lee, {Candace Y W} and Burnett, {John C Jr.}",
year = "2008",
doi = "10.1016/B978-0-12-373870-7.00020-X",
language = "English (US)",
isbn = "9780123738707",
pages = "287--307",
booktitle = "Textbook of Nephro-Endocrinology",
publisher = "Elsevier Inc.",

}

TY - CHAP

T1 - ANP, BNP and CNP

T2 - Physiology and Pharmacology of the Cardiorenal Axis

AU - Lee, Candace Y W

AU - Burnett, John C Jr.

PY - 2008

Y1 - 2008

N2 - The three mammalian natriuretic peptides (NPs), A-type natriuretic peptide (ANP), B-type natriuretic peptide (BNP), and C-type natriuretic peptide (CNP), are genetically distinct but share structural similarities. Human ANP, BNP, and CNP are synthesized as preprohormones, which are subsequently split into prohormones by proteolytic cleavage of an N-terminal signal peptide. Human prepro-ANP is a 151-amino acid (AA) peptide that is cleaved to the 126-AA pro-ANP, whereas human prepro-BNP is a 134-AA peptide that is cleaved to the 108-AA pro-BNP. Pro-ANP and pro-BNP are stored in secretory granules in atrial cardiomyocytes and are cleaved to form ANP and BNP, respectively, upon secretion. The conversion of pro-ANP to ANP is mediated by corin, a transmembrane cardiac serine protease. Both human ANP, a 28-AA peptide, and human BNP, a 32-AA peptide, are released from the myocardium in response to various physiologic and pathophysiologic stimuli, such as myocardial wall stretch. Human pro-CNP consists of 103 AA residues and is processed by furin, an intracellular endoprotease, to the mature 53-AA CNP. CNP-53, which is found primarily in the brain, the heart, and endothelial cells, may be further cleaved to CNP-22.

AB - The three mammalian natriuretic peptides (NPs), A-type natriuretic peptide (ANP), B-type natriuretic peptide (BNP), and C-type natriuretic peptide (CNP), are genetically distinct but share structural similarities. Human ANP, BNP, and CNP are synthesized as preprohormones, which are subsequently split into prohormones by proteolytic cleavage of an N-terminal signal peptide. Human prepro-ANP is a 151-amino acid (AA) peptide that is cleaved to the 126-AA pro-ANP, whereas human prepro-BNP is a 134-AA peptide that is cleaved to the 108-AA pro-BNP. Pro-ANP and pro-BNP are stored in secretory granules in atrial cardiomyocytes and are cleaved to form ANP and BNP, respectively, upon secretion. The conversion of pro-ANP to ANP is mediated by corin, a transmembrane cardiac serine protease. Both human ANP, a 28-AA peptide, and human BNP, a 32-AA peptide, are released from the myocardium in response to various physiologic and pathophysiologic stimuli, such as myocardial wall stretch. Human pro-CNP consists of 103 AA residues and is processed by furin, an intracellular endoprotease, to the mature 53-AA CNP. CNP-53, which is found primarily in the brain, the heart, and endothelial cells, may be further cleaved to CNP-22.

UR - http://www.scopus.com/inward/record.url?scp=84882508533&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84882508533&partnerID=8YFLogxK

U2 - 10.1016/B978-0-12-373870-7.00020-X

DO - 10.1016/B978-0-12-373870-7.00020-X

M3 - Chapter

AN - SCOPUS:84882508533

SN - 9780123738707

SP - 287

EP - 307

BT - Textbook of Nephro-Endocrinology

PB - Elsevier Inc.

ER -