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Atrial Natriuretic Peptide rat, also known as cardiac natriuretic hormone and atrial natriuretic peptide, belongs to the family of natriuretic peptides. Atrial Natriuretic Peptide rat is a kind of active polypeptide synthesized, stored and secreted by the atria, which is also known as atrial natriuretic factor (ANF) or atrial natriuretic peptide (ANP). It has powerful natriuretic, diuretic, vasodilatory, blood pressure-lowering and antirenalin-angiotensin system and antidiuretic hormone effects. Measurement of serum ANP activity is used to diagnose and monitor the course and outcome of patients with heart failure.
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Atrial Natriuretic Peptide rat is mainly secreted by atrial myocytes, brain natriuretic peptide is mainly secreted by ventricular myocytes, and C-type natriuretic peptide is mainly secreted by vascular endothelial cells and exerts vasodilatory and antiproliferative effects locally. Plasma cardiac natriuretic peptide has multiple effects of vasodilation, diuresis, and antagonism of neuroendocrine hormones.
Since atrial dilatation is the main trigger for AVP release, the concentration of ANP is closely related to left atrial pressure and pulmonary artery systolic pressure.
Elevated: seen in essential hypertension, coronary artery disease, heart failure, supraventricular tachycardia, premature cirrhosis, bronchial asthma, chronic obstructive pulmonary disease, aldosteronism, and renal disease. In acute infarction, elevated ANP has a unique predictive value for LV dysfunction and mortality in AMI, and elevated concentrations of ANP in patients with acute myocardial infarction in the subacute phase suggest a poor long-term prognosis.
Decreased: seen in hyperthyroidism, atrial fibrillation.
Atrial Natriuretic Peptide rat Precautions
Sample collection should be done under the same conditions as much as possible, e.g., at the same time every day, after lying supine and still for 15min, in order to have comparable results.
Excessive activity and tachycardia will increase ANP.
Liver and kidney disease should be excluded, where ANP can accumulate due to who retention.
| Density | 1.54±0.1 g/cm3(Predicted) |
| Storage condition | -20°C |
| Water solubility | Soluble to 1 mg/ml in water |
| Purity(HPLC) | ≥98.0% |
| Acetate content | ≤12.0% |
| Water content | ≤8.0 |
| Peptide content | ≥80.0 |
| Endotoxin | ≤50EU/mg |
| Amino acid composition analysis | ≤±10% |
| appearances | white powder |
Atrial Natriuretic Peptide rat is a peptide hormone synthesized by the heart when the ventricular wall is dilated or strained. It is an important hormone in the regulation of body fluids, body sodium balance, blood pressure, and can also play a role in protecting the heart. When the ventricular wall is dilated or stretched, cardiac natriuretic peptide is released into the bloodstream, which in turn has the effect of maintaining heart function and dilating blood vessels. If the level of cardiac natriuretic peptide increases, it may cause an increase in the load on the heart, which can lead to heart failure.
The main efficacy of Atrial Natural Peptide rat
balanced dilatation of arteries and veins, lowering the anterior and posterior load on the heart, rapid relief of dyspnea and systemic symptoms, no drug resistance.
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moderate diuresis and sodium excretion, reducing circulating volume load, increasing renal filtration degree without increasing renal burden.
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Comprehensively antagonize the cardiotoxicity produced by excessive activation of the neuroendocrine system.
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Delay cardiac remodeling, prevent myocardial hyperplasia, hypertrophy and interstitial fibrosis, and reduce long-term morbidity and mortality.
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No positive inotropic and positive heart rate effects, no increase in myocardial oxygen consumption, no arrhythmogenic effects.
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Atrial Natriuretic Peptide rat is an important peptide hormone that plays a key role in regulating fluid balance and blood pressure. The following is a common synthesis method.
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Atrial Natriuretic Peptide rat synthesis steps:
usually, atrial natriuretic peptide can be synthesized by solid-phase synthesis (solid-phase synthesis) or liquid-phase synthesis (solution-phase synthesis). In solid-phase synthesis, the peptide chain is constructed by gradually adding amino acids to the carrier.
The sequence of an ANP is relatively short and known, usually consisting of 28 amino acid residues.
During synthesis, each amino acid requires appropriate protecting groups to avoid side reactions. These protecting groups need to be removed after the synthesis is complete to allow the amino acid to be attached to the peptide chain.
The peptide chain is synthesized step-by-step in the order of the ANP sequence according to the selected synthesis method and equipment. Each amino acid addition requires repeated steps of protection, coupling, and deprotection.
After the synthesis is completed, the peptide needs to be purified and characterized to ensure the purity and correct structure of the product.
Atrial natriuretic peptide rat is a polypeptide hormone synthesized by rat atrial cells and belongs to the natriuretic peptide family. It is highly similar in structure to human atrial natriuretic peptide (hANP) but there are species differences. The study of its chemical properties is of great significance for understanding its physiological functions and potential applications. The following analysis is conducted from four dimensions: molecular structure, physicochemical properties, receptor binding, and biological activity.
Molecular Structure: Composition and Modification of Peptide Chains
The core structure of rANP is a linear polypeptide chain consisting of 28 amino acids (rANP(1-28)), with a molecular weight of approximately 3062.41 Da. Its sequence contains a cyclic structure composed of 17 amino acids, formed by the connection of cysteine residues at position 7 and position 23 through disulfide bonds. This cyclic structure is the key region for rANP to bind to the receptor and determines its biological activity.
Compared with human ANP, the amino acid sequence of rANP has subtle differences. For instance, the 16th position of rANP is glycine (Gly), while that of hANP is serine (Ser); the 17th position of rANP is alanine (Ala), and that of hANP is glutamic acid (Glu). These differences result in species-specific binding affinity and signal transduction efficiency between rANP and human ANP receptors.
The N-terminal of rANP is methionine (Met), and the C-terminal is tyrosine (Tyr). Its isoelectric point (pI) is approximately 8.5, indicating that it carries a positive charge under physiological pH (7.4), which may affect its electrostatic interaction with the cell membrane or receptors.
Physical and Chemical Properties: Solubility and Stability
rANP is highly soluble in water and physiological saline, with a solubility of over 10 mg/mL. Its solubility is significantly affected by pH: in acidic conditions (pH < 5), rANP may experience a decrease in solubility due to protonation; in alkaline conditions (pH > 9), disulfide bonds may break, leading to the depolymerization of the polypeptide chain. Therefore, the storage and use of rANP require strict control of the pH range (typically pH 6.0 - 8.0).
rANP is temperature-sensitive. When stored at -20℃ under refrigeration, its activity can be maintained for several years; however, at 4℃, the activity may decrease by 5% to 10% every week; at room temperature (25℃), the activity loss may exceed 30% within 24 hours. Moreover, repeated freezing and thawing can cause rANP to aggregate and form insoluble precipitates. Therefore, it is recommended to aliquot and use it only once.
rANP is highly sensitive to proteases (such as trypsin and chymotrypsin). In a solution containing 0.1% trypsin, rANP can be completely degraded within 30 minutes at 37℃. Therefore, in experimental or clinical applications, it is necessary to avoid coexistence with proteases or add protease inhibitors (such as PMSF) for protection.
Receptor Binding: The Dual Role of NPR-A and NPR-C
The rANP exerts its effects through two membrane receptors:
NPR-A (Natriuretic Peptide Receptor-A)
The binding affinity of rANP to NPR-A is high (Kd ≈ 1-10 nM), activating the guanylate cyclase activity in the intracellular segment of the receptor and catalyzing the formation of cGMP from GTP. cGMP acts as a second messenger, regulating ion channels (such as the Na⁺ channels in renal tubular epithelial cells) and enzyme activities (such as phosphodiesterase) through the activation of protein kinase G (PKG), ultimately promoting sodium excretion, diuresis, and vasodilation.
Studies have shown that the activation efficiency of rANP on rat NPR-A is 1.2-1.5 times that of hANP, which may be related to the more suitable circular structure of rANP for the rat receptor.
NPR-C (Natriuretic Peptide Receptor-C)
NPR-C has no enzymatic activity and mainly functions as a receptor for clearance, degrading rANP through endocytosis. The binding of rANP to NPR-C can trigger intracellular signal transduction (such as inhibition of adenylate cyclase), but this effect is weaker than that of NPR-A.
Through genetically engineered variants of rANP (such as rANP(G16R, A17E, Q18A)), the binding ability to NPR-C is reduced by approximately 200 times, while retaining the activation ability on NPR-A, thereby prolonging its half-life and enhancing its biological effect.
Biological Activity: Vasodilation and Sodium Excretion and Diuresis
The biological activity of rANP is mainly achieved through the cGMP pathway:
Vasodilation
rANP can dilate the aorta, renal artery, and mesenteric artery of rats, with an EC50 of approximately 0.1 - 1 nM. Its mechanisms include:
Direct relaxation of vascular smooth muscle cells;
Inhibition of vascular contraction induced by endothelin-1 (ET-1);
Reduction of vascular smooth muscle cell proliferation (through GATA4-dependent pathway to inhibit endothelin gene expression).
Na-reduction and diuresis
Intravenous injection of rANP (0.325 μg/min) can increase rat urinary sodium excretion by 3 - 5 times and urine volume by 2 - 3 times. Its action sites include:
Glomerulus: By dilating the afferent arteriole, it increases renal blood flow;
Nephron: Inhibiting Na⁺-K⁺-2Cl⁻ co-transporter (NKCC2) and Na⁺/H⁺ exchanger (NHE3), reducing Na⁺ reabsorption;
Collecting duct: Inhibiting the expression of aquaporin 2 (AQP2), reducing water reabsorption.
Blood pressure regulation
rANP can lower the mean arterial pressure of rats by 10 - 20 mmHg, with an effect lasting for 30 - 60 minutes. Its antihypertensive effect is synergistically related to vasodilation and sodium reduction, and is not dependent on changes in heart rate.
Applications and Challenges
The chemical properties of rANP make it potential for the treatment of hypertension, heart failure, and kidney diseases. However, its species specificity (lower activity on human receptors), short half-life (about 5 - 10 minutes), and proteinase sensitivity limit its clinical application. Currently, researchers are optimizing rANP through the following strategies:
Develop NPR-A selective variants (such as rANP(REA18)), reducing the clearance mediated by NPR-C;
Chemical modification (such as pegylation) to extend the half-life;
Nanocarrier delivery to enhance stability.
The chemical properties of rat atrial natriuretic peptide (rANP) reflect the typical characteristics of polypeptide hormones: structure-dependent activity, environmental sensitivity, and receptor-mediated signal transduction. A deeper understanding of its physicochemical properties and biological effects not only provides tools for basic research but also points the way for the development of new cardiovascular drugs.
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