Atrial Natriuretic Peptide (ANP) (1-28), rat
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Atrial Natriuretic Peptide (ANP) (1-28), rat

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Atrial natriuretic factor (1-28) (rat) is a 28 amino acid peptide corresponding to the rat protein sequence. It is an endogenous peptide synthesized in myoendocrine cells of the heart from which it is released into the circulation. It has effects on the renal and cardiovascular systems that decrease vasoconstriction, increase sodium excretion and inhibit renin secretion. It decreases plasma renin activity and cAMP levels in anesthetized rats and increases cGMP levels at 8 µg/kg. It also inhibits the arginine vasopressin-induced increase in mean arterial blood pressure in spontaneously hypertensive and control rats when administered intracerebroventricularly at a dose of 150 ng. It produces diuretic, natriuretic and vasodilatory effects through stimulation of guanylate cyclase-linked NPR-A receptors. It plays an important role in blood volume and blood pressure regulation.

Category
Peptide Inhibitors
Catalog number
BAT-010445
CAS number
88898-17-3
Molecular Formula
C128H205N45O39S2
Molecular Weight
3062.41
Atrial Natriuretic Peptide (ANP) (1-28), rat
IUPAC Name
(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(4R,10S,16S,19S,22S,28S,31S,34S,37S,40S,49S,52R)-52-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-19-(3-amino-3-oxopropyl)-49-benzyl-28,37-bis[(2S)-butan-2-yl]-31,40-bis(3-carbamimidamidopropyl)-34-(carboxymethyl)-16-(hydroxymethyl)-22-methyl-10-(2-methylpropyl)-6,9,12,15,18,21,24,27,30,33,36,39,42,45,48,51-hexadecaoxo-1,2-dithia-5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50-hexadecazacyclotripentacontane-4-carbonyl]amino]-4-oxobutanoyl]amino]-3-hydroxypropanoyl]amino]-3-phenylpropanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-(4-hydroxyphenyl)propanoic acid
Synonyms
Atrial natriuretic factor (1-28) (rat); rANP; Atrial Natriuretic Peptide rat; Cardiodilatin-126; Atrial Natriuretic Factor (1-28) (mouse, rabbit, rat); rANF (1-28); H-Ser-Leu-Arg-Arg-Ser-Ser-Cys(1)-Phe-Gly-Gly-Arg-Ile-Asp-Arg-Ile-Gly-Ala-Gln-Ser-Gly-Leu-Gly-Cys(1)-Asn-Ser-Phe-Arg-Tyr-OH; L-seryl-L-leucyl-L-arginyl-L-arginyl-L-seryl-L-seryl-L-cysteinyl-L-phenylalanyl-glycyl-glycyl-L-arginyl-L-isoleucyl-L-alpha-aspartyl-L-arginyl-L-isoleucyl-glycyl-L-alanyl-L-glutaminyl-L-seryl-glycyl-L-leucyl-glycyl-L-cysteinyl-L-asparagyl-L-seryl-L-phenylalanyl-L-arginyl-L-tyrosine (7->23)-disulfide; ANF; ANP; α-Atriopeptin (rat)
Appearance
White or Off-white Lyophilized Powder
Purity
≥95%
Density
1.5±0.1 g/cm3
Sequence
SLRRSSCFGGRIDRIGAQSGLGCNSFRY (Disulfide bridge: Cys7-Cys23)
Storage
Store in a cool and dry place and at 2-8°C for short term (days to weeks) or store at -20°C for long term (months to years)
Solubility
Soluble in Acetic Acid
InChI
InChI=1S/C128H205N45O39S2/c1-10-64(7)99-121(209)151-52-94(183)152-66(9)101(189)156-77(36-37-91(130)180)109(197)167-85(56-175)105(193)150-53-96(185)154-78(43-62(3)4)103(191)149-54-97(186)155-89(119(207)164-82(48-92(131)181)114(202)169-86(57-176)116(204)163-81(46-68-25-16-13-17-26-68)113(201)159-74(29-20-40-144-126(136)137)107(195)166-84(123(211)212)47-69-32-34-70(179)35-33-69)60-213-214-61-90(171-118(206)88(59-178)170-117(205)87(58-177)168-108(196)75(30-21-41-145-127(138)139)157-106(194)73(28-19-39-143-125(134)135)158-112(200)79(44-63(5)6)161-102(190)71(129)55-174)120(208)162-80(45-67-23-14-12-15-24-67)104(192)148-50-93(182)147-51-95(184)153-72(27-18-38-142-124(132)133)110(198)173-100(65(8)11-2)122(210)165-83(49-98(187)188)115(203)160-76(111(199)172-99)31-22-42-146-128(140)141/h12-17,23-26,32-35,62-66,71-90,99-100,174-179H,10-11,18-22,27-31,36-61,129H2,1-9H3,(H2,130,180)(H2,131,181)(H,147,182)(H,148,192)(H,149,191)(H,150,193)(H,151,209)(H,152,183)(H,153,184)(H,154,185)(H,155,186)(H,156,189)(H,157,194)(H,158,200)(H,159,201)(H,160,203)(H,161,190)(H,162,208)(H,163,204)(H,164,207)(H,165,210)(H,166,195)(H,167,197)(H,168,196)(H,169,202)(H,170,205)(H,171,206)(H,172,199)(H,173,198)(H,187,188)(H,211,212)(H4,132,133,142)(H4,134,135,143)(H4,136,137,144)(H4,138,139,145)(H4,140,141,146)/t64-,65-,66-,71-,72-,73-,74-,75-,76-,77-,78-,79-,80-,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,99-,100-/m0/s1
InChI Key
QGFSVPWZEPKNDV-BRTFOEFASA-N
Canonical SMILES
CCC(C)C1C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NCC(=O)NC(CSSCC(C(=O)NC(C(=O)NCC(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)N1)CCCNC(=N)N)CC(=O)O)C(C)CC)CCCNC(=N)N)CC2=CC=CC=C2)NC(=O)C(CO)NC(=O)C(CO)NC(=O)C(CCCNC(=N)N)NC(=O)C(CCCNC(=N)N)NC(=O)C(CC(C)C)NC(=O)C(CO)N)C(=O)NC(CC(=O)N)C(=O)NC(CO)C(=O)NC(CC3=CC=CC=C3)C(=O)NC(CCCNC(=N)N)C(=O)NC(CC4=CC=C(C=C4)O)C(=O)O)CC(C)C)CO)CCC(=O)N)C
1. Activation of protein kinase A by atrial natriuretic peptide in neonatal rat cardiac fibroblasts: role in regulation of the local renin-angiotensin system
Manuela Smith, Kenneth M Baker, David E Dostal, Rajesh Kumar, Sandhya Sanghi Regul Pept . 2005 Dec 15;132(1-3):1-8. doi: 10.1016/j.regpep.2005.06.007.
There is an inverse relationship between renin and atrial natriuretic peptide (ANP) levels in the plasma. Since both the ANP and renin-angiotensin system (RAS) are upregulated in development and cardiac hypertrophy, we tested whether ANP differentially regulates RAS in cardiac cells. Cardiac fibroblasts isolated from neonatal rats were treated with ANP(1-28), a biologically active fragment of ANP. Renin and angiotensinogen (Ao) mRNA levels were measured by quantitative multiplex RT-PCR and protein levels determined by Western blot analysis. ANP(1-28) increased renin and Ao mRNA levels (737+/-131% and 178+/-51.3%) with EC50 values of 4.12+/-0.3 and 8.67+/-0.22 nmol/L, respectively. At the protein level, secretion of renin and Ao was significantly enhanced resulting in approximately 4-fold increase in ANG II level in the medium. The effect of ANP(1-28) on renin and Ao mRNA expression were reproduced by 8-bromo-cyclic GMP. Inhibition of protein kinase G (PKG) with KT5823 blunted ANP(1-28)-induced upregulation of renin, but not Ao mRNA, while inhibition of protein kinase A (PKA) with KT5720 attenuated the upregulation of both renin and Ao mRNA. These findings suggest that unlike in plasma, ANP positively regulates the RAS in cardiac fibroblasts, which may have a significant role in development of the fetal heart.
2. Localization of atrial natriuretic peptide receptors in the rat tongue and hard palate
B K Park, S H Kim, C Oh, M S Lee, K W Cho, S Z Kim, J D Lee, E S Cho Arch Oral Biol . 1998 Aug;43(8):611-8. doi: 10.1016/s0003-9969(98)00039-9.
Atrial natriuretic peptide (ANP) receptors were characterized in rat oral mucosa using quantitative in vitro autoradiography and activation of particulate guanylyl cyclase (GC) by natriuretic peptides. Competition-binding analysis performed by quantitative in vitro autoradiography demonstrated specific [125I]rANP(1-28) binding sites in the tongue and hard palate. The precise location of this binding was revealed on the basal and parabasal cells of the epithelia by microautoradiography. The dissociation constant (Kd) and maximal binding capacity (Bmax) of these sites were 3.34+/-1.35 nM and 2.71+/-2.21 fmol/mm2 on the epithelium of the tongue, and 4.09+/-1.52 nM and 3.45+/-3.01 fmol/mm2 on the epithelium of the hard palate, respectively. Receptor subtypes were characterized by competition with des [Gln18, Ser19, Gly20, Leu21, Gly22] ANP(4-23) (C-ANP), a specific ligand for the clearance receptor (NPR-C). These binding sites were displaced by C-ANP with inhibition constant (Ki) of 8.96+/-3.18 nM and Bmax of 2.89+/-2.45 fmol/mm2 on the epithelium of the tongue, and Ki of 9.12+/-2.71 nM and Bmax of 3.08+/-2.94 fmol/mm2 on the epithelium of the hard palate, respectively. Production of cyclic GMP by particulate GC in the epithelial membranes of the tongue and hard palate was stimulated by rANP(1-28), porcine brain natriuretic peptide (BNP)(1-26), and C-type natriuretic peptide (CNP)(1-22) in a dose-dependent manner. These results indicate that ANP-binding sites in the epithelium of the tongue and hard palate are mainly clearance receptors (NPR-C) but biological receptors (NPR-A and/or NPR-B) with GC activity are also present, and suggest that ANP may have a role in the proliferation of the oral epithelial cells, especially in the tongue and hard palate.
3. Evidence for atrial natriuretic peptide-(5-28) production by macrophages of the rat spleen: an immunochemical and nonradioactive in situ hybridization approach
W Q Huang, M Throsby, D Lee, Z Y Yang, D L Copolov, A T Lim Endocrinology . 1991 Aug;129(2):991-1000. doi: 10.1210/endo-129-2-991.
Atrial natriuretic peptide (ANP), a 28-amino acid peptide, is produced and secreted by cardiac atriocytes to modulate cardiovascular functions. Recently, biologically active receptors for ANP have been demonstrated in the spleen; we report here the production of ANP-(5-28) and its 15-kDa (K) mol wt (Mr) presumptive precursors by macrophages of rat splenic tissues. Splenic, hypothalamic, and heart tissues were collected from adult male Sprague-Dawley rats and acid extracted for ANP assay. The splenic content of immunoreactive (ir) ANP (mean +/- SEM, 428 +/- 68 pg/tissue; n = 7) was approximately a fifth of that found in the hypothalamus and about 4 orders of magnitude lower than that in the heart of the same animals. The Sephadex G-50 column profile of splenic extracts revealed two immunoreactive peaks; the major peak eluted in positions consistent with 15K Mr, while a minor peak coeluted with synthetic rat ANP-(1-28) of 3K Mr. HPLC analysis of the 3K Mr species showed a single peak of immunoreactivity, which eluted with a retention time similar to that of ANP-(5-28). In rat splenic sections, immunoperoxidase localization of ir-ANP revealed positive cells sparsely distributed in marginal sinuses and the red pulp of the tissue; employing a double staining technique, S22, a surface marker for macrophages, was colocalized on the same splenocytes. Furthermore, colorimetric in situ hybridization with antisense oligonucleotide probes labeled with digoxigenin, identified specific signals for pro-ANP mRNA in splenocytes of tissue sections. In monolayer cultures of vehicle-treated splenocytes, approximately 87% of the adherent cells stained positive for S22; this marker was colocalized with ir-ANP in approximately 15% of the cells. Twenty-four-hour treatment with lipopolysaccharide (50 micrograms/ml), a bacterial endotoxin, tripled the proportion of adherent cells (32 +/- 4%; P less than 0.01) staining positive for ir-ANP over that in control cultures (mean +/- SEM, 11 +/- 3%; 10(4) cells/sample; n = 5). Furthermore, an equivalent dose of lipopolysaccharide, but not Concanavalin-A (50 micrograms/ml), quadrupled ir-ANP content compared to that in vehicle-treated cultures (less than 5 pg/well). Thus, our findings suggest that ANP-(5-28) is produced by a small population of splenic macrophages and raise the possibility that the peptide may play a signalling role at the tissue level.
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