Atrial Natriuretic Peptide (ANP) (1-28), human, porcine Acetate

Modify Date: 2024-01-02 15:23:14

Atrial Natriuretic Peptide (ANP) (1-28), human, porcine Acetate Structure
Atrial Natriuretic Peptide (ANP) (1-28), human, porcine Acetate structure
Common Name Atrial Natriuretic Peptide (ANP) (1-28), human, porcine Acetate
CAS Number 1366000-58-9 Molecular Weight 3140.5
Density N/A Boiling Point N/A
Molecular Formula C127H203N45O39S3.C2H4O2 Melting Point N/A
MSDS N/A Flash Point N/A

 Use of Atrial Natriuretic Peptide (ANP) (1-28), human, porcine Acetate


Atrial Natriuretic Peptide (ANP) (1-28), human, porcine is a 28-amino acid hormone, that is normally produced and secreted by the human heart in response to cardiac injury and mechanical stretch. ANP (1-28) inhibits endothelin-1 secretion in a dose-dependent way.

 Names

Name Atrial Natriuretic Peptide (ANP) (1-28), human, porcine Acetate

  Biological Activity

Description Atrial Natriuretic Peptide (ANP) (1-28), human, porcine is a 28-amino acid hormone, that is normally produced and secreted by the human heart in response to cardiac injury and mechanical stretch. ANP (1-28) inhibits endothelin-1 secretion in a dose-dependent way.
Related Catalog
Target

Endothelin-1[1]

In Vitro Atrial natriuretic peptide (ANP) is a diuretic, natriuretic, and vasodilatory peptide hormone originally isolated from mammalian hearts. In cultured porcine endothelial cells the inhibition by porcine ANP (1-28) of immunoreactive endothelin-1 secretion after stimulation with Angiotensin II (Ang II) is paralleled by an increase in the cellular cGMP level. Porcine ANP (1-28) strongly inhibits immunoreactive endothelin-1 secretion in porcine aorta after stimulation with Ang II[1]. ANP is a cardiac hormone involved in electrolyte and fluid homeostasis. The inhibition by ANP of endothelin-1 secretion stimulated by angiotensin II (ANGII) and thrombin using cultured human umbilical-vein endothelial cells. Human ANP (1-28) inhibits immunoreactive (ir)-endothelin-1 secretion and increases cyclic GMP in the human umbilical-vein endothelial cells[2]. In glomeruli from normal rats, Human 125I-ANP (1-28) binds to a single population of high affinity receptors with a mean equilibrium dissociation constant of 0.46 nM. Human ANP (1-28) binds to the glomerular ANP receptor with high affinity stimulated cGMP accumulation. Human ANP (1-28) markedly stimulates cGMP generation, but not cAMP generation in normal rat glomeruli[3].
References

[1]. Kohno M, et al. Atrial and brain natriuretic peptides inhibit the endothelin-1 secretory response to angiotensin II in porcine aorta. Circ Res. 1992 Feb;70(2):241-7.

[2]. Kohno M, et al. Inhibition by atrial and brain natriuretic peptides of endothelin-1 secretion after stimulation with angiotensin II and thrombin of cultured human endothelial cells. J Clin Invest. 1991 Jun;87(6):1999-2004.

[3]. Ballermann BJ, et al. Physiologic regulation of atrial natriuretic peptide receptors in rat renal glomeruli. J Clin Invest. 1985 Dec;76(6):2049-56.

 Chemical & Physical Properties

Molecular Formula C127H203N45O39S3.C2H4O2
Molecular Weight 3140.5
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