Dendroaspis natriuretic peptide is degraded by a metalloproteinase in the rat kidney

Kim,Soo Mi; Kim,Sun Young; Kim,Suhn Hee; Kim,Sung Zoo

doi:10.3892/mmr.2013.1871

Dendroaspis natriuretic peptide is degraded by a metalloproteinase in the rat kidney

Authors:
- Soo Mi Kim
- Sun Young Kim
- Suhn Hee Kim
- Sung Zoo Kim
View Affiliations

Affiliations: Department of Physiology, Institute for Medical Sciences, Chonbuk National University Medical School, Jeonju, Jeonbuk 561‑180, Republic of Korea
Published online on: December 17, 2013 https://doi.org/10.3892/mmr.2013.1871
Pages: 1037-1043

Metrics: Total Views: 0 (Spandidos Publications: | PMC Statistics: )

Metrics: Total PDF Downloads: 0 (Spandidos Publications: | PMC Statistics: )

Cited By (CrossRef): 0 citations Loading Articles...

Abstract

Our previous study demonstrated that the concentration of dendroaspis natriuretic peptide (DNP) was markedly higher than that of atrial NP (ANP) in rabbit plasma, indicating that DNP has a different metabolic rate from other NPs. Therefore, the metabolic characteristics of DNP in mammals require further analysis. The stabilities of NPs were determined by incubating 125I‑labeled ANP, brain NP (BNP), C‑type NP (CNP) and DNP at 37˚C for 1, 2 and 4 h, and analyzing their profiles by reversed‑phase high‑performance liquid chromatography. 125I‑labeled ANP, BNP and CNP were quickly degraded in rat plasma, while 125I‑labeled DNP was stable for 4 h. The relative stability of the peptides following incubation in rat plasma followed the rank order of: DNP>>>ANP≥BNP>>CNP. Organs were also examined for the degradation of DNP, including the spleen, kidney, liver, heart and lung. The physiological target organ for the degradation of DNP was observed to be the kidney. Furthermore, degradation of DNP in the kidney was attenuated by phenanthroline, a metalloproteinase inhibitor. Therefore, these results indicate that DNP has a longer stability in plasma and that it may have strong therapeutic applications in cardiac disease.

View Figures

View References

1	de Bold AJ: Atrial natriuretic factor: a hormone produced by the heart. Science. 230:767–770. 1985.PubMed/NCBI
2	de Bold AJ: Atrial natriuretic factor: an overview. Fed Proc. 45:2081–2085. 1986.
3	Sudoh T, Kangawa K, Minamino N and Matsuo H: A new natriuretic peptide in porcine brain. Nature. 332:78–81. 1988. View Article : Google Scholar : PubMed/NCBI
4	Sudoh T, Minamino N, Kangawa K and Matsuo H: C-type natriuretic peptide (CNP): a new member of natriuretic peptide family identified in porcine brain. Biochem Biophys Res Commun. 168:863–870. 1990. View Article : Google Scholar : PubMed/NCBI
5	Schweitz H, Vigne P, Moinier D, Frelin C and Lazdunski M: A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps). J Biol Chem. 267:13928–13932. 1992.PubMed/NCBI
6	Nakao K, Mukoyama M, Hosoda K, et al: Biosynthesis, secretion, and receptor selectivity of human brain natriuretic peptide. Can J Physiol Pharmacol. 69:1500–1506. 1991. View Article : Google Scholar : PubMed/NCBI
7	Stoupakis G and Klapholz M: Natriuretic peptides: biochemistry, physiology, and therapeutic role in heart failure. Heart Dis. 5:215–223. 2003. View Article : Google Scholar : PubMed/NCBI
8	Scotland RS, Ahluwalia A and Hobbs AJ: C-type natriuretic peptide in vascular physiology and disease. Pharmacol Ther. 105:85–93. 2005. View Article : Google Scholar : PubMed/NCBI
9	Januszewicz A: The natriuretic peptides in hypertension. Curr Opin Cardiol. 10:495–500. 1995. View Article : Google Scholar
10	Kim SM, Kim YA, Kim SY, Kim SH, Cho KW and Kim SZ: Presence of dendroaspis natriuretic peptide and its binding to NPR-A receptor in rabbit kidney. Regul Pept. 167:42–49. 2011. View Article : Google Scholar : PubMed/NCBI
11	Cho KW, Kim SH, Kim CH and Seul KH: Mechanical basis of ANP secretion in beating atria: atrial stroke volume and ECF translocation. Am J Physiol. 268:R1129–R1136. 1995.PubMed/NCBI
12	Morris BJ: Specific radioactivity of radioimmunoassay tracer determined by self-displacement: a re-evaluation. Clin Chim Acta. 73:213–216. 1976. View Article : Google Scholar : PubMed/NCBI
13	Joseph LJ, Desai KB, Mehta MN and Mathiyarasu R: Measurement of specific activity of radiolabelled antigens by a simple radioimmunoassay technique. Int J Rad Appl Instrum B. 15:589–590. 1988. View Article : Google Scholar : PubMed/NCBI
14	Kim SM, Kim SY, Kim SH, Cho KW and Kim SZ: Renal actions of dendroaspis natriuretic peptide in rabbits. Peptides. 33:59–66. 2012. View Article : Google Scholar : PubMed/NCBI
15	Tan AC, Rosmalen FM, Theelen BG, Kloppenborg PW, Benraad HB and Benraad TJ: Atrial natriuretic peptide - the influence of various physiological and sampling conditions. Ann Clin Biochem. 24:500–507. 1987. View Article : Google Scholar : PubMed/NCBI
16	Rugg EL, Aiton JF and Cramb G: Degradation of [125I]-atrial natriuretic peptide by a soluble metallopeptidase isolated from rat ventricular myocytes. Biochem Biophys Res Commun. 152:294–300. 1988.
17	Olins GM, Spear KL, Siegel NR, Reinhard EJ and Zurcher-Neely HA: Atrial peptide inactivation by rabbit-kidney brush-border membranes. Eur J Biochem. 170:431–434. 1987. View Article : Google Scholar : PubMed/NCBI
18	Lisy O, Jougasaki M, Schirger JA, Chen HH, Barclay PT and Burnett JC Jr: Neutral endopeptidase inhibition potentiates the natriuretic actions of adrenomedullin. Am J Physiol. 275:F410–F414. 1998.PubMed/NCBI
19	Dussaule JC: Natriuretic factors of cardiac origin: renal effects. Rev Prat. 43(20 Suppl): 13–17. 1993.(In French).
20	Stephenson SL and Kenny AJ: The hydrolysis of alpha-human atrial natriuretic peptide by pig kidney microvillar membranes is initiated by endopeptidase-24.11. Biochem J. 243:183–187. 1987.PubMed/NCBI
21	Stephenson SL and Kenny AJ: The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme ‘endopeptidase-2’ and by rat microvillar membranes. Biochem J. 255:45–51. 1988.PubMed/NCBI
22	Johnson GR, Arik L and Foster CJ: Metabolism of 125I-atrial natriuretic factor by vascular smooth muscle cells. Evidence for a peptidase that specifically removes the COOH-terminal tripeptide. J Biol Chem. 264:11637–11642. 1989.
23	Erdös EG and Skidgel RA: Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones. FASEB J. 3:145–151. 1989.
24	Erdös EG, Wagner B, Harbury CB, Painter RG, Skidgel RA and Fa XG: Down-regulation and inactivation of neutral endopeptidase 24.11 (enkephalinase) in human neutrophils. J Biol Chem. 264:14519–14523. 1989.
25	Yandle TG, Brennan SO, Espiner EA, Nicholls MG and Richards AM: Endopeptidase-24.11 in human plasma degrades atrial natriuretic factor (ANF) to ANF(99-105/106-126). Peptides. 10:891–894. 1989. View Article : Google Scholar : PubMed/NCBI
26	Tamburini PP, Koehn JA, Gilligan JP, et al: Rat vascular tissue contains a neutral endopeptidase capable of degrading atrial natriuretic peptide. J Pharmacol Exp Ther. 251:956–961. 1989.PubMed/NCBI
27	Bourne A and Kenny AJ: The hydrolysis of brain and atrial natriuretic peptides by porcine choroid plexus is attributable to endopeptidase-24.11. Biochem J. 271:381–385. 1990.PubMed/NCBI
28	Vanneste Y, Pauwels S, Lambotte L and Deschodt-Lanckman M: In vivo metabolism of brain natriuretic peptide in the rat involves endopeptidase 24.11 and angiotensin converting enzyme. Biochem Biophys Res Commun. 173:265–271. 1990. View Article : Google Scholar : PubMed/NCBI
29	Chen HH, Lainchbury JG and Burnett JC Jr: Natriuretic peptide receptors and neutral endopeptidase in mediating the renal actions of a new therapeutic synthetic natriuretic peptide dendroaspis natriuretic peptide. J Am Coll Cardiol. 40:1186–1191. 2002. View Article : Google Scholar