A 52-amino acid peptide with multi-functions. It was originally isolated from PHEOCHROMOCYTOMA and ADRENAL MEDULLA but is widely distributed throughout the body including lung and kidney tissues. Besides controlling fluid-electrolyte homeostasis, adrenomedullin is a potent vasodilator and can inhibit pituitary ACTH secretion.
G-protein-coupled cell surface receptors for ADRENOMEDULLIN. They are formed by the heterodimerization of CALCITONIN RECEPTOR-LIKE PROTEIN and either RECEPTOR ACTIVITY-MODIFYING PROTEIN 2 or RECEPTOR ACTIVITY-MODIFYING PROTEIN 3.
A receptor protein that is associated with RECEPTOR ACTIVITY-MODIFYING PROTEINS. When bound to RECEPTOR ACTIVITY-MODIFYING PROTEIN 1 it forms the CALCITONIN GENE-RELATED RECEPTOR. When bound to RECEPTOR ACTIVITY-MODIFYING PROTEIN 2 or RECEPTOR ACTIVITY-MODIFYING PROTEIN 3 it forms the ADRENOMEDULLIN RECEPTOR.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
A receptor activity-modifying protein that heterodimerizes with CALCITONIN RECEPTOR-LIKE PROTEIN to form the ADRENOMEDULLIN RECEPTOR. In addition, an isoform of the ISLET AMYLOID POLYPEPTIDE RECEPTOR is formed from this protein dimerizing with the CALCITONIN RECEPTOR.
A family of proteins that bind to CELL SURFACE RECEPTORS and alter their specificity, signaling mechanism, or mode of intracellular transport.
A receptor activity-modifying protein that heterodimerizes with CALCITONIN RECEPTOR-LIKE PROTEIN to form the ADRENOMEDULLIN RECEPTOR. In addition, an isoform of the ISLET AMYLOID POLYPEPTIDE RECEPTOR is formed from this protein dimerizing with the CALCITONIN RECEPTOR.
Cell surface proteins that bind calcitonin and trigger intracellular changes which influence the behavior of cells. Calcitonin receptors outside the nervous system mediate the role of calcitonin in calcium homeostasis. The role of calcitonin receptors in the brain is not well understood.
Calcitonin gene-related peptide. A 37-amino acid peptide derived from the calcitonin gene. It occurs as a result of alternative processing of mRNA from the calcitonin gene. The neuropeptide is widely distributed in neural tissue of the brain, gut, perivascular nerves, and other tissue. The peptide produces multiple biological effects and has both circulatory and neurotransmitter modes of action. In particular, it is a potent endogenous vasodilator.
Cell surface proteins that bind CALCITONIN GENE-RELATED PEPTIDE with high affinity and trigger intracellular changes which influence the behavior of cells. CGRP receptors are present in both the CENTRAL NERVOUS SYSTEM and the periphery. They are formed via the heterodimerization of the CALCITONIN RECEPTOR-LIKE PROTEIN and RECEPTOR ACTIVITY-MODIFYING PROTEIN 1.
Cell surface receptors that bind peptide messengers with high affinity and regulate intracellular signals which influence the behavior of cells.
A receptor activity-modifying protein that is a subunit of specific G-PROTEIN COUPLED RECEPTORS. The CALCITONIN GENE-RELATED PEPTIDE RECEPTOR is formed from a dimer of this protein and CALCITONIN RECEPTOR-LIKE PROTEIN, while an isoform of the ISLET AMYLOID POLYPEPTIDE RECEPTOR is formed from this protein dimerizing with the CALCITONIN RECEPTOR.
Drugs used to cause dilation of the blood vessels.
Agents causing contraction of the pupil of the eye. Some sources use the term miotics only for the parasympathomimetics but any drug used to induce miosis is included here.
An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.
Classic quantitative assay for detection of antigen-antibody reactions using a radioactively labeled substance (radioligand) either directly or indirectly to measure the binding of the unlabeled substance to a specific antibody or other receptor system. Non-immunogenic substances (e.g., haptens) can be measured if coupled to larger carrier proteins (e.g., bovine gamma-globulin or human serum albumin) capable of inducing antibody formation.
A potent natriuretic and vasodilatory peptide or mixture of different-sized low molecular weight PEPTIDES derived from a common precursor and secreted mainly by the HEART ATRIUM. All these peptides share a sequence of about 20 AMINO ACIDS.
Drugs used in the treatment of acute or chronic vascular HYPERTENSION regardless of pharmacological mechanism. Among the antihypertensive agents are DIURETICS; (especially DIURETICS, THIAZIDE); ADRENERGIC BETA-ANTAGONISTS; ADRENERGIC ALPHA-ANTAGONISTS; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; CALCIUM CHANNEL BLOCKERS; GANGLIONIC BLOCKERS; and VASODILATOR AGENTS.
G-protein coupled receptors that are formed through the dimerization of the CALCITONIN RECEPTOR with a RECEPTOR ACTIVITY-MODIFYING PROTEIN. Their affinity for ISLET AMYLOID POLYPEPTIDE is dependent upon which of several receptor activity-modifying protein subtypes they are bound to.

Role of nitric oxide-cGMP pathway in adrenomedullin-induced vasodilation in the rat. (1/693)

We previously reported that adrenomedullin (AM), a potent vasodilator peptide discovered in pheochromocytoma cells, stimulates nitric oxide (NO) release in the rat kidney. To further investigate whether the NO-cGMP pathway is involved in the mechanisms of AM-induced vasodilation, we examined the effects of E-4021, a cGMP-specific phosphodiesterase inhibitor, on AM-induced vasorelaxation in aortic rings and perfused kidneys isolated from Wistar rats. We also measured NO release from the kidneys using a chemiluminescence assay. AM (10(-10) to 10(-7) mol/L) relaxed the aorta precontracted with phenylephrine in a dose-dependent manner. Denudation of endothelium (E) attenuated the vasodilatory action of AM (10(-7) mol/L AM: intact (E+) -25.7+/-5.2% versus denuded (E-) -7. 8+/-0.6%, P<0.05). On the other hand, pretreatment with 10(-8) mol/L E-4021 augmented AM-induced vasorelaxation in the intact aorta (-49. 0+/-7.9%, P<0.05) but not in the denuded one. E-4021 also enhanced acetylcholine (ACh)-induced vasorelaxation in the rat intact aorta (10(-7) mol/L ACh -36.6+/-8.4% versus 10(-8) mol/L E-4021+10(-7) mol/L ACh -62.7+/-3.1%, P<0.05). In perfused kidneys, AM-induced vasorelaxation was also augmented by preincubation with E-4021 (10(-9) mol/L AM -15.4+/-0.6% versus 10(-8) mol/L E-4021+10(-9) mol/L AM -23.6+/-1.2%, P<0.01). AM significantly increased NO release from rat kidneys (DeltaNO: +11.3+/-0.8 fmol. min-1. g-1 kidney at 10(-9) mol/L AM), which was not affected by E-4021. E-4021 enhanced ACh-induced vasorelaxation (10(-9) mol/L ACh -9.7+/-1.7% versus 10(-8) mol/L E-4021+10(-9) mol/L ACh -18.8+/-2.9%, P<0.01) but did not affect ACh-induced NO release from the kidneys. In the aorta and the kidney, 10(-4) mol/L of NG-nitro-L-arginine methyl ester, an NO synthase inhibitor, and 10(-5) mol/L of methylene blue, a guanylate cyclase inhibitor, reduced the vasodilatory effect of AM. These results suggest that the NO-cGMP pathway is involved in the mechanism of AM-induced vasorelaxation, at least in the rat aorta and kidney.  (+info)

Adrenomedullin is upregulated in the heart and aorta during the early and late stages of sepsis. (2/693)

Although circulating levels of adrenomedullin (ADM), a newly reported vasodilatory peptide with 52 amino acid residues in the human and 50 amino acid residues in the rat, are elevated during the early and late stages of sepsis, ADM levels in cardiovascular tissues and its precise localization remain to be determined. To study this, rats were subjected to sepsis by cecal ligation and puncture (CLP), followed by administration of 3 ml/100 g b.wt. normal saline to these and sham-operated animals. The heart and thoracic aorta were harvested at 5 h (i.e. the early stage of sepsis) and 20 h (late sepsis) after CLP. Tissue levels of ADM were determined by radioimmunoassay. The localization of ADM in the left ventricle and thoracic aorta was examined by using immunohistochemistry and electron microscopy techniques. The results indicated that ADM levels in the heart and thoracic aorta increased significantly at 5 h after CLP and remained elevated at 20 h after the onset of sepsis. Immunohistochemistry findings showed that ADM immunoreaction products were localized in the cytoplasm of the cardiac myocytes and aortic endothelial cells. Using electron microscopy, ADM immunoreaction products were found in the cytoplasmic matrixes. The immunostainings were also associated with the outer membranes of mitochondria and vesicles of the myocytes as well as vascular endothelial cells. It appears that the cardiovascular tissues, among other organ systems, contribute to the increased levels of plasma ADM under those conditions. Since ADM is localized in different cell populations in the heart and the large blood vessel (i.e. myocytes versus vascular endothelial cells), this peptide may play a differential role in regulating cardiac and vascular functions during sepsis as an autocrine and/or paracrine mediator.  (+info)

Proadrenomedullin N-terminal 20 peptide hyperpolarizes the membrane by activating an inwardly rectifying K+ current in differentiated PC12 cells. (3/693)

The mechanism of proadrenomedullin N-terminal 20 peptide (PAMP)-induced inhibition of catecholamine release from adrenergic nerve was investigated in nerve growth factor-treated PC12 cells that have differentiated characteristics somewhat similar to noradrenergic neurons. The effect of PAMP on the excitability of these cells was investigated with the use of perforated whole-cell clamp. PAMP hyperpolarized the membrane by increasing a K+ conductance in a dose-dependent manner. The current-voltage relationship (I-V) relationship of the PAMP-induced K+ conductance exhibited inward-going rectification. The activation was abolished by microinjecting GDPbetaS into the cells or pretreating the cells with pertussis toxin. These results indicate that a pertussis toxin-sensitive G protein is involved in the signal transduction. The PAMP-induced activation of the K+ conductance was attenuated by microinjecting antibody against the carboxyl terminus of Galphai3, but it was not influenced by microinjecting antibody against the common carboxyl termini of Galphai1 and Galphai2, which indicated that the G protein coupling the PAMP receptor to the inwardly rectifying K+ current is Galphai3. The PAMP-induced hyperpolarization may inhibit the catecholamine release from the neurons by attenuating the action potential frequency.  (+info)

Coronary sinus adrenomedullin rises in response to myocardial injury. (4/693)

Human adrenomedullin (ADM), a peptide comprising 52 amino acids, is a circulating hormone with vasodilator properties. We have evaluated its release by the heart following ischaemic myocardial damage, as indicated by elevated levels of the cardiospecific protein troponin-T (Tn-T) during cardiopulmonary bypass. ADM (pg/ml) and Tn-T (ng/ml) were measured in coronary sinus blood before and after aortic cross-clamp and in venous blood 6 h after surgery in 22 coronary-bypass patients. Based on the pre- and post-clamp Tn-T levels in the coronary sinus, the patients were divided into group I (no change; n=10) and group II (two times increase; n=12). Baseline ADM (362.7+/-106.2 and 303+/-58.7 pg/ml in groups I and II respectively; means+/-S.D.) and Tn-T (0.66+/-0.14 and 0.57+/-0.13 ng/ml respectively) levels were similar in both groups. In group I, the post-clamp ADM (317.6+/-80.8 pg/ml) and Tn-T (0.68+/-0.15 ng/ml) levels did not change significantly. In group II, the post-clamp ADM levels rose significantly above the baseline, mimicking the change in Tn-T (ADM, 541.4+/-89.4 pg/ml; Tn-T, 1.37+/-0.31 ng/ml; P=0.009). After 6 h, the systemic Tn-T levels were similar in both groups (2. 09+/-0.44 and 1.95+/-0.52 ng/ml in groups I and II respectively). We suggest that: (1) minor degrees of myocardial ischaemic damage result in release of ADM by the heart, and (2) ADM may play a protective role in the myocardium during an ischaemic insult. This suggests a possible therapeutic role for ADM in the management of intra-operative myocardial ischaemia.  (+info)

Effects of adrenomedullin and PAMP on adrenal catecholamine release in dogs. (5/693)

We examined the effects of proadrenomedullin-derived peptides on the release of adrenal catecholamines in response to cholinergic stimuli in pentobarbital sodium-anesthetized dogs. Drugs were administered into the adrenal gland through the phrenicoabdominal artery. Splanchnic nerve stimulation (1, 2, and 3 Hz) and ACh injection (0.75, 1.5, and 3 microgram) produced frequency- or dose-dependent increases in adrenal catecholamine output. These responses were unaffected by infusion of adrenomedullin (1, 3, and 10 ng. kg-1. min-1) or its selective antagonist adrenomedullin-(22-52) (5, 15, and 50 ng. kg-1. min-1). Proadrenomedullin NH2-terminal 20 peptide (PAMP; 5, 15, and 50 ng. kg-1. min-1) suppressed both the splanchnic nerve stimulation- and ACh-induced increases in catecholamine output in a dose-dependent manner. PAMP also suppressed the catecholamine release responses to the nicotinic agonist 1, 1-dimethyl-4-phenylpiperazinium (0.5, 1, and 2 microgram) and to muscarine (0.5, 1, and 2 microgram), although the muscarine-induced response was relatively resistant to PAMP. These results suggest that PAMP, but not adrenomedullin, can act as an inhibitory regulator of adrenal catecholamine release in vivo.  (+info)

Hypoxia-induced adrenomedullin production in the kidney. (6/693)

BACKGROUND: Adrenomedullin (AM) is a newly discovered peptide that has a potent vasorelaxant activity. To investigate its potential roles in hypoxia-induced renal injury, we examined whether AM production in the kidney increased under hypoxic conditions. METHODS: The AM transcript levels in Madin-Darby canine kidney (MDCK) cells, rat vascular smooth muscle cells (VSMCs), and rat mesangial cells were assessed by Northern blot analyses under normoxic and hypoxic conditions. The AM peptide in culture media was measured by radioimmunoassay. The effects of hypoxia on accumulation of cAMP in VSMCs were also examined. The stability of AM transcripts under normoxic and hypoxic conditions was compared in the presence of actinomycin D. The effects of hypoxia on AM promoter activity was assessed by transient transfection assays using the AM promoter subcloned upstream of luciferase gene. RESULTS: The expression of AM transcripts increased significantly in MDCK cells, rat VSMCs, and rat mesangial cells under hypoxic conditions without changes in the stability of AM transcripts; however, the AM promoter activity under hypoxic was not elevated significantly. The accumulation of AM peptide in culture media also increased significantly under hypoxic conditions in MDCK cells (2.2 +/- 0.1 fmol/10(5) cells in normoxia vs. 3.5 +/- 0.3 fmol/10(5) cells in hypoxia, 6 hr after hypoxia induction, P < 0.001), and in rat VSMCs (5.5 +/- 0.3 fmol/10(5) cells in normoxia vs. 7.8 +/- 0.4 fmol/10(5) cells in hypoxia, 8 hr after hypoxia induction, P < 0.01). Under hypoxic conditions, cAMP levels in rat VSMCs increased significantly compared with those under normoxic conditions (13.3 +/- 1.4 pmol/well vs. 4.6 +/- 0.4 pmol/well, P < 0.01). CONCLUSIONS: Renal parenchymal cells as well as renal vessels may produce AM under hypoxic conditions.  (+info)

Characterization of receptors for calcitonin gene-related peptide and adrenomedullin on the guinea-pig vas deferens. (7/693)

1. The receptors which mediate the effects of calcitonin gene-related peptide (CGRP), amylin and adrenomedullin on the guinea-pig vas deferens have been investigated. 2. All three peptides cause concentration dependant inhibitions of the electrically stimulated twitch response (pD2s for CGRP, amylin and adrenomedullin of 7.90+/-0.11, 7.70+/-0.19 and 7.25+/-0.10 respectively). 3. CGRP8-37 (1 microM) and AC187 (10 microM) showed little antagonist activity against adrenomedullin. 4. Adrenomedullin22-52 by itself inhibited the electrically stimulated contractions of the vas deferens and also antagonized the responses to CGRP, amylin and adrenomedullin. 5. [125I]-adrenomedullin labelled a single population of binding sites in vas deferens membranes with a pIC50 of 8.91 and a capacity of 643 fmol mg(-1). Its selectivity profile was adrenomedullin> AC187>CGRP=amylin. It was clearly distinct from a site labelled by [125I]-CGRP (pIC50=8.73, capacity=114 fmol mg(-1), selectivity CGRP>amylin=AC187>adrenomedullin). [125I]-amylin bound to two sites with a total capacity of 882 fmol mg(-1). 6. Although CGRP has been shown to act at a CGRP2 receptor on the vas deferens with low sensitivity to CGRP8-37, this antagonist displaced [125I]-CGRP with high affinity from vas deferens membranes. This affinity was unaltered by increasing the temperature from 4 degrees C to 25 degrees C, suggesting the anomalous behaviour of CGRP8-37 is not due to temperature differences between binding and functional assays.  (+info)

Central adrenomedullin augments the baroreceptor reflex in conscious rabbits. (8/693)

We examined the roles of central adrenomedullin, proadrenomedullin N-terminal 20 peptide (PAMP), and calcitonin gene-related peptide (CGRP) on the baroreceptor reflex in conscious rabbits. Intracerebroventricular injection of adrenomedullin (0.2 and 1 nmol/80 microL) elicited dose-related increases in arterial pressure and renal sympathetic nerve activity. On the other hand, a subpressor dose of intracerebroventricular infusion of adrenomedullin (1 nmol/300 microL per hour) caused significant increases in baroreflex sensitivities assessed by renal sympathetic nerve activity and heart rate compared with vehicle infusion (Gmax; -14.9+/-1.7 versus -8.0+/-0.7%/mm Hg, P<0.01, and -8.1+/-0.8 versus -5.1+/-0.5 bpm/mm Hg, P<0.01, respectively). Intracerebroventricular infusion of CGRP (1 nmol/300 microL per hour), which is structurally homologous to adrenomedullin, also enhanced the baroreflex controls of renal sympathetic nerve activity and heart rate. However, the intracerebroventricular infusion of PAMP (30 nmol/300 microL per hour) failed to alter the baseline levels of arterial pressure and baroreflex sensitivities. These results suggest that central adrenomedullin and CGRP, but not PAMP, participate in cardiovascular regulation to augment the baroreflex controls of renal sympathetic nerve activity and heart rate in conscious rabbits.  (+info)

Adrenomedullin is a hormone that is produced and released by the adrenal glands, specifically from the chromaffin cells in the adrenal medulla. It is a small peptide made up of 52 amino acids and has various physiological functions, including vasodilation, bronchodilation, and inhibition of cell growth.

Adrenomedullin acts as a potent vasodilator by binding to specific G protein-coupled receptors in the vascular smooth muscle cells, leading to relaxation of the blood vessels. It also has a role in regulating blood pressure and fluid balance in the body.

In addition to its effects on the cardiovascular system, adrenomedullin has been shown to have anti-inflammatory and neuroprotective properties. It is involved in various physiological processes such as wound healing, tissue repair, and angiogenesis (the formation of new blood vessels).

Abnormal levels of adrenomedullin have been implicated in several disease states, including hypertension, heart failure, sepsis, and cancer. Therefore, measuring adrenomedullin levels in the body can provide valuable diagnostic and prognostic information for these conditions.

Adrenomedullin receptors are a type of G protein-coupled receptor (GPCR) that bind to and are activated by the peptide hormone adrenomedullin. There are two main types of adrenomedullin receptors, identified as AM1 and AM2, which are formed by the combination of different subunits. The AM1 receptor is composed of the calcitonin receptor-like receptor (CLR) and receptor activity-modifying protein 2 (RAMP2), while the AM2 receptor is composed of CLR and RAMP3.

Adrenomedullin receptors play important roles in various physiological processes, including cardiovascular regulation, vasodilation, and inhibition of cell growth and proliferation. They are widely distributed throughout the body, particularly in the vascular system, kidneys, adrenal glands, and central nervous system. Activation of these receptors by adrenomedullin leads to a range of intracellular signaling events, including the activation of adenylyl cyclase, increased levels of cAMP, and activation of protein kinase A (PKA). These downstream effects contribute to the diverse biological activities of adrenomedullin.

In addition to adrenomedullin, related peptides such as adrenotensin and intermedin can also bind to and activate these receptors, albeit with lower affinity. Dysregulation of adrenomedullin receptor signaling has been implicated in several pathological conditions, including hypertension, heart failure, and cancer. As a result, targeting adrenomedullin receptors has emerged as a potential therapeutic strategy for the treatment of these diseases.

Calcitonin receptor-like protein (CRLR) is a gene that encodes for a protein involved in the regulation of various physiological functions, including cell proliferation, differentiation, and apoptosis. CRLR itself does not bind to calcitonin or any other ligands, but it serves as a necessary component for the formation of functional receptors for certain peptide hormones, such as calcitonin gene-related peptide (CGRP) and adrenomedullin.

These hormones play important roles in regulating blood pressure, inflammation, and nociception (the perception of pain). CRLR forms a complex with receptor activity-modifying proteins (RAMPs) to create functional receptors for CGRP and adrenomedullin. The specific combination of CRLR and RAMPs determines the type of receptor formed, which in turn dictates the ligand specificity and downstream signaling pathways activated.

Mutations in the CRLR gene have been associated with various diseases, including familial hypocalciuric hypercalcemia (FHH) type 3, a rare inherited disorder characterized by elevated serum calcium levels and decreased urinary calcium excretion. Additionally, dysregulation of CRLR-mediated signaling pathways has been implicated in the development and progression of several types of cancer, neurodegenerative disorders, and cardiovascular diseases.

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

Receptor Activity-Modifying Protein 2 (RAMP2) is a protein that plays a role in modulating the function of certain G protein-coupled receptors (GPCRs). RAMP2 combines with specific GPCRs to form complexes that alter their ligand binding, trafficking, and signaling properties.

These GPCRs include calcitonin receptor-like receptor (CALCRL) and calcitonin receptor (CTR), which bind to peptide hormones such as calcitonin gene-related peptide (CGRP) and adrenomedullin. RAMP2-containing complexes have been implicated in various physiological processes, including vasodilation, nociception, and neurotransmission.

Mutations in the RAMP2 gene can lead to several genetic disorders, such as familial migraine with aura and autosomal dominant osteoporosis type II. Additionally, RAMP2 has been targeted for drug development in conditions like migraine and cardiovascular diseases.

Receptor Activity-Modifying Proteins (RAMPs) are a family of single-pass transmembrane proteins that play a crucial role in modulating the function of certain G protein-coupled receptors (GPCRs). RAMPs were first identified in 1998, and since then, they have been shown to interact with and alter the pharmacological properties, ligand specificity, trafficking, and signal transduction of class II GPCRs, including calcitonin gene-related peptide (CGRP) receptors and adrenomedullin receptors.

There are three known isoforms of RAMPs: RAMP1, RAMP2, and RAMP3. These isoforms can form heterodimers with class II GPCRs, leading to the formation of distinct receptor complexes with unique functional properties. The interaction between RAMPs and GPCRs can result in the generation of novel signaling pathways, which may have implications for various physiological processes and diseases.

RAMPs are involved in several biological functions, such as regulating vasodilation, inflammation, nociception, and cell proliferation. Dysregulation of RAMP-mediated signaling has been implicated in the pathogenesis of various disorders, including migraine, cardiovascular diseases, and cancer. Therefore, understanding the molecular mechanisms underlying RAMP function is essential for developing novel therapeutic strategies targeting these diseases.

Receptor Activity-Modifying Protein 3 (RAMP3) is a protein that plays a role in modulating the activity of certain G protein-coupled receptors (GPCRs). RAMP3 combines with specific GPCRs to form complexes, which then alter the binding properties and signaling capabilities of those receptors.

RAMP3 is primarily associated with calcitonin gene-related peptide (CGRP) receptors and adrenomedullin receptors. By forming a complex with these GPCRs, RAMP3 helps to regulate their activity and plays a role in various physiological processes, including neurotransmission, vasodilation, and inflammation.

It is important to note that the study of RAMP3 and its functions is still an active area of research, and new findings may continue to expand our understanding of this protein and its role in health and disease.

Calcitonin receptors (CTRs) are a type of G protein-coupled receptor (GPCR) that bind and respond to the hormone calcitonin. Calcitonin is a peptide hormone secreted by the parafollicular cells (C cells) of the thyroid gland, and plays a crucial role in regulating calcium homeostasis in the body.

CTRs are widely expressed in various tissues and organs, including bone, kidney, intestine, and brain. In bone, CTR activation inhibits osteoclast-mediated bone resorption, thereby increasing bone density and reducing the risk of fractures. In the kidney, CTR activation promotes calcium reabsorption and phosphate excretion, helping to maintain normal serum calcium and phosphate levels.

CTRs are also involved in various physiological processes, such as nociception (pain perception), neuroprotection, and cell proliferation and differentiation. Dysregulation of CTR signaling has been implicated in several diseases, including osteoporosis, hypercalcemia, and cancer.

The medical definition of "Receptors, Calcitonin" refers to the specific proteins that bind calcitonin hormone and mediate its effects on target cells and tissues.

Calcitonin gene-related peptide (CGRP) is a neurotransmitter and vasodilator peptide that is widely distributed in the nervous system. It is encoded by the calcitonin gene, which also encodes calcitonin and catestatin. CGRP is produced and released by sensory nerves and plays important roles in pain transmission, modulation of inflammation, and regulation of blood flow.

CGRP exists as two forms, α-CGRP and β-CGRP, which differ slightly in their amino acid sequences but have similar biological activities. α-CGRP is found primarily in the central and peripheral nervous systems, while β-CGRP is expressed mainly in the gastrointestinal tract.

CGRP exerts its effects by binding to specific G protein-coupled receptors, which are widely distributed in various tissues, including blood vessels, smooth muscles, and sensory neurons. Activation of CGRP receptors leads to increased intracellular cyclic AMP levels, activation of protein kinase A, and subsequent relaxation of vascular smooth muscle, resulting in vasodilation.

CGRP has been implicated in several clinical conditions, including migraine, cluster headache, and inflammatory pain. Inhibition of CGRP signaling has emerged as a promising therapeutic strategy for the treatment of these disorders.

Calcitonin gene-related peptide (CGRP) receptors are a type of cell surface receptor found in various tissues and cells, including the nervous system and blood vessels. CGRP is a neuropeptide that plays a role in regulating vasodilation, inflammation, and nociception (the sensation of pain).

The CGRP receptor is a complex of two proteins: calcitonin receptor-like receptor (CLR) and receptor activity-modifying protein 1 (RAMP1). When CGRP binds to the CLR-RAMP1 complex, it activates a signaling pathway that leads to vasodilation and increased pain sensitivity.

CGRP receptors have been identified as important targets for the treatment of migraine headaches, as CGRP levels are known to increase during migraine attacks. Several drugs that target CGRP receptors have been developed and approved for the prevention and acute treatment of migraines.

Peptide receptors are a type of cell surface receptor that bind to peptide hormones and neurotransmitters. These receptors play crucial roles in various physiological processes, including regulation of appetite, pain perception, immune function, and cardiovascular homeostasis. Peptide receptors belong to the G protein-coupled receptor (GPCR) superfamily or the tyrosine kinase receptor family. Upon binding of a peptide ligand, these receptors activate intracellular signaling cascades that ultimately lead to changes in cell behavior and communication with other cells.

Peptide receptors can be classified into two main categories: metabotropic and ionotropic. Metabotropic peptide receptors are GPCRs, which activate intracellular signaling pathways through coupling with heterotrimeric G proteins. These receptors typically have seven transmembrane domains and undergo conformational changes upon ligand binding, leading to the activation of downstream effectors such as adenylyl cyclase, phospholipase C, or ion channels.

Ionotropic peptide receptors are ligand-gated ion channels that directly modulate ion fluxes across the cell membrane upon ligand binding. These receptors contain four or five subunits arranged around a central pore and undergo conformational changes to allow ion flow through the channel.

Examples of peptide receptors include:

1. Opioid receptors (μ, δ, κ) - bind endogenous opioid peptides such as enkephalins, endorphins, and dynorphins to modulate pain perception and reward processing.
2. Somatostatin receptors (SSTR1-5) - bind somatostatin and cortistatin to regulate hormone secretion, cell proliferation, and angiogenesis.
3. Neuropeptide Y receptors (Y1-Y5) - bind neuropeptide Y to modulate feeding behavior, energy metabolism, and cardiovascular function.
4. Calcitonin gene-related peptide receptor (CGRP-R) - binds calcitonin gene-related peptide to mediate vasodilation and neurogenic inflammation.
5. Bradykinin B2 receptor (B2R) - binds bradykinin to induce pain, inflammation, and vasodilation.
6. Vasoactive intestinal polypeptide receptors (VPAC1, VPAC2) - bind vasoactive intestinal peptide to regulate neurotransmission, hormone secretion, and smooth muscle contraction.
7. Oxytocin receptor (OXTR) - binds oxytocin to mediate social bonding, maternal behavior, and uterine contractions during childbirth.
8. Angiotensin II type 1 receptor (AT1R) - binds angiotensin II to regulate blood pressure, fluid balance, and cell growth.

Receptor Activity-Modifying Protein 1 (RAMP1) is not a medical term per se, but rather a scientific term used in the field of molecular biology and pharmacology. RAMP1 is a single-pass type I membrane protein that plays a crucial role in the function of certain G protein-coupled receptors (GPCRs), particularly the calcitonin gene-related peptide (CGRP) receptor and adrenomedullin receptors.

RAMP1 forms complexes with specific GPCRs, thereby modifying their ligand specificity, trafficking, and signaling properties. It is involved in the transportation of these receptors to the cell surface and influences their binding affinity for different ligands. RAMP1-containing receptors are implicated in various physiological processes, including vasodilation, nociception (pain perception), neurogenic inflammation, and bone homeostasis. Dysregulation of RAMP1 and its associated receptors has been linked to several diseases, such as migraine, hypertension, and cancer.

While not a medical definition, understanding the role of RAMP1 in modulating GPCR activity is essential for researchers working on drug development and therapeutic strategies targeting these receptor systems.

Vasodilator agents are pharmacological substances that cause the relaxation or widening of blood vessels by relaxing the smooth muscle in the vessel walls. This results in an increase in the diameter of the blood vessels, which decreases vascular resistance and ultimately reduces blood pressure. Vasodilators can be further classified based on their site of action:

1. Systemic vasodilators: These agents cause a generalized relaxation of the smooth muscle in the walls of both arteries and veins, resulting in a decrease in peripheral vascular resistance and preload (the volume of blood returning to the heart). Examples include nitroglycerin, hydralazine, and calcium channel blockers.
2. Arterial vasodilators: These agents primarily affect the smooth muscle in arterial vessel walls, leading to a reduction in afterload (the pressure against which the heart pumps blood). Examples include angiotensin-converting enzyme (ACE) inhibitors, angiotensin receptor blockers (ARBs), and direct vasodilators like sodium nitroprusside.
3. Venous vasodilators: These agents primarily affect the smooth muscle in venous vessel walls, increasing venous capacitance and reducing preload. Examples include nitroglycerin and other organic nitrates.

Vasodilator agents are used to treat various cardiovascular conditions such as hypertension, heart failure, angina, and pulmonary arterial hypertension. It is essential to monitor their use carefully, as excessive vasodilation can lead to orthostatic hypotension, reflex tachycardia, or fluid retention.

Miotics, also known as parasympathomimetics or cholinergic agents, are a class of medications that stimulate the parasympathetic nervous system. They work by activating muscarinic receptors, which are found in various organs throughout the body, including the eye. In the eye, miotics cause contraction of the circular muscle of the iris, resulting in pupillary constriction (miosis). This action can help to reduce intraocular pressure in patients with glaucoma.

Miotics may also have other effects on the eye, such as accommodation (focusing) and decreasing the production of aqueous humor. Some examples of miotics include pilocarpine, carbachol, and ecothiopate. It's important to note that the use of miotics can have side effects, including blurred vision, headache, and brow ache.

Cyclic adenosine monophosphate (cAMP) is a key secondary messenger in many biological processes, including the regulation of metabolism, gene expression, and cellular excitability. It is synthesized from adenosine triphosphate (ATP) by the enzyme adenylyl cyclase and is degraded by the enzyme phosphodiesterase.

In the body, cAMP plays a crucial role in mediating the effects of hormones and neurotransmitters on target cells. For example, when a hormone binds to its receptor on the surface of a cell, it can activate a G protein, which in turn activates adenylyl cyclase to produce cAMP. The increased levels of cAMP then activate various effector proteins, such as protein kinases, which go on to regulate various cellular processes.

Overall, the regulation of cAMP levels is critical for maintaining proper cellular function and homeostasis, and abnormalities in cAMP signaling have been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Radioimmunoassay (RIA) is a highly sensitive analytical technique used in clinical and research laboratories to measure concentrations of various substances, such as hormones, vitamins, drugs, or tumor markers, in biological samples like blood, urine, or tissues. The method relies on the specific interaction between an antibody and its corresponding antigen, combined with the use of radioisotopes to quantify the amount of bound antigen.

In a typical RIA procedure, a known quantity of a radiolabeled antigen (also called tracer) is added to a sample containing an unknown concentration of the same unlabeled antigen. The mixture is then incubated with a specific antibody that binds to the antigen. During the incubation period, the antibody forms complexes with both the radiolabeled and unlabeled antigens.

After the incubation, the unbound (free) radiolabeled antigen is separated from the antibody-antigen complexes, usually through a precipitation or separation step involving centrifugation, filtration, or chromatography. The amount of radioactivity in the pellet (containing the antibody-antigen complexes) is then measured using a gamma counter or other suitable radiation detection device.

The concentration of the unlabeled antigen in the sample can be determined by comparing the ratio of bound to free radiolabeled antigen in the sample to a standard curve generated from known concentrations of unlabeled antigen and their corresponding bound/free ratios. The higher the concentration of unlabeled antigen in the sample, the lower the amount of radiolabeled antigen that will bind to the antibody, resulting in a lower bound/free ratio.

Radioimmunoassays offer high sensitivity, specificity, and accuracy, making them valuable tools for detecting and quantifying low levels of various substances in biological samples. However, due to concerns about radiation safety and waste disposal, alternative non-isotopic immunoassay techniques like enzyme-linked immunosorbent assays (ELISAs) have become more popular in recent years.

Atrial natriuretic factor (ANF), also known as atrial natriuretic peptide (ANP), is a hormone that is primarily produced and secreted by the atria of the heart in response to stretching of the cardiac muscle cells due to increased blood volume. ANF plays a crucial role in regulating body fluid homeostasis, blood pressure, and cardiovascular function.

The main physiological action of ANF is to promote sodium and water excretion by the kidneys, which helps lower blood volume and reduce blood pressure. ANF also relaxes vascular smooth muscle, dilates blood vessels, and inhibits the renin-angiotensin-aldosterone system (RAAS), further contributing to its blood pressure-lowering effects.

Defects in ANF production or action have been implicated in several cardiovascular disorders, including heart failure, hypertension, and kidney disease. Therefore, ANF and its analogs are being investigated as potential therapeutic agents for the treatment of these conditions.

Antihypertensive agents are a class of medications used to treat high blood pressure (hypertension). They work by reducing the force and rate of heart contractions, dilating blood vessels, or altering neurohormonal activation to lower blood pressure. Examples include diuretics, beta blockers, ACE inhibitors, ARBs, calcium channel blockers, and direct vasodilators. These medications may be used alone or in combination to achieve optimal blood pressure control.

Islet amyloid polypeptide receptors (IAPRs) are a type of G protein-coupled receptor (GPCR) that play a role in the regulation of glucose homeostasis and energy balance. They are activated by the hormone islet amyloid polypeptide (IAPP), also known as amylin, which is co-secreted with insulin from pancreatic beta cells in response to meals.

There are two subtypes of IAPRs, named RCS3 (or IA PR1) andRAMP2 (or IA PR2). These receptors can form heterodimers with other GPCRs, such as the calcitonin receptor (CTR), to form functional complexes that bind IAPP with high affinity. Activation of IAPRs by IAPP has been shown to inhibit gastric emptying, reduce food intake, and lower blood glucose levels, suggesting a role in the regulation of satiety and glucose metabolism.

Mutations in the genes encoding IAPP and IAPRs have been associated with the development of type 2 diabetes, suggesting that dysfunction of the IAPP/IAPR system may contribute to the pathogenesis of this disease. Additionally, the accumulation of misfolded IAPP in pancreatic islets can lead to the formation of amyloid deposits, which are a characteristic feature of type 2 diabetes and have been implicated in the destruction of beta cells and the development of insulin resistance.

... at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Human ADM genome location and ADM gene ... Adrenomedullin (ADM or AM) is a vasodilator peptide hormone of uncertain significance in human health and disease. It was ... Adrenomedullin may function as a hormone in the circulation control because it is found in blood in a considerable ... The adrenomedullin knockout is an embryonic lethal phenotype and dies mid gestation from a condition known as hydrops fetalis. ...
"Entrez Gene: ADM2 adrenomedullin 2". Human ADM2 genome location and ADM2 gene details page in the UCSC Genome Browser. Kawai M ... Takei Y, Inoue K, Ogoshi M, Kawahara T, Bannai H, Miyano S (Jan 2004). "Identification of novel adrenomedullin in mammals: a ... 2006). "Immunocytochemical localization of adrenomedullin 2/intermedin-like immunoreactivity in human hypothalamus, heart and ...
Endogenous inducers include i) lipids such as lipoxin and epoxyeicosatrienoic acid; and ii) peptides such as adrenomedullin and ...
"Treatment of bone disorders with adrenomedullin or adrenomedullin agonists." U.S. Patent 6,440,421, issued 27 August 2002. Reid ...
In the presence of this (RAMP2) protein, CRLR functions as an adrenomedullin receptor. The RAMP2 protein is involved in core ... Fritz-Six KL, Dunworth WP, Li M, Caron KM (January 2008). "Adrenomedullin signaling is necessary for murine lymphatic vascular ... Kuwasako K, Kitamura K, Nagoshi Y, Eto T (2003). "Novel calcitonin-(8-32)-sensitive adrenomedullin receptors derived from co- ... 2008). "Lack of linkage and association of adrenomedullin and its receptor genes in French Caucasian rheumatoid arthritis trio ...
... adrenomedullin, adrenomedullin 2 (intermedin) and calcitonin‑receptor‑stimulating peptide. Calcitonin is mainly produced by ... The CGRP family includes calcitonin (CT), adrenomedullin (AM), and amylin (AMY). CGRP is produced in both peripheral and ... The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors". Pharmacological Reviews. 54 ... which is necessary for CGRP and adrenomedullin (AM receptors). For function CGRP, CALCRL must coincide with RAMP1 where the ...
2002). "Possible role of nitric oxide and adrenomedullin in bipolar affective disorder". Neuropsychobiology. 45 (2): 57-61. doi ...
Li Z, Takeuchi S, Ohara N, Maruo T (2003). "Paradoxically abundant expression of Bcl-2 and adrenomedullin in invasive cervical ...
1998). "Expression of the rat adrenomedullin receptor or a putative human adrenomedullin receptor does not correlate with ... 2004). "[Study of the expression and role of adrenomedullin and adrenomedullin receptor in patients with chronic obstructive ... of the rat adrenomedullin receptor or a putative human adrenomedullin receptor does not correlate with adrenomedullin binding ... 1997). "Expression of adrenomedullin and its receptor in normal and malignant human skin: a potential pluripotent role in the ...
2000). "CGRP-RCP, a novel protein required for signal transduction at calcitonin gene-related peptide and adrenomedullin ... in adrenomedullin receptor signal transduction". Peptides. 22 (11): 1773-81. doi:10.1016/S0196-9781(01)00517-4. PMID 11754963. ...
2005). "High plasma levels of human chromogranin A and adrenomedullin in patients with pheochromocytoma". Tumori. 91 (1): 53-8 ...
In the presence of this (RAMP3) protein, CRLR functions as an adrenomedullin receptor with low affinity for CGRP. GRCh38: ... Kuwasako K, Kitamura K, Nagoshi Y, Eto T (2003). "Novel calcitonin-(8-32)-sensitive adrenomedullin receptors derived from co- ... 2005). "Receptor activity-modifying protein (RAMP) isoform-specific regulation of adrenomedullin receptor trafficking by NHERF- ... receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. In humans and other ...
Kuwasako K, Kitamura K, Nagoshi Y, Eto T (2003). "Novel calcitonin-(8-32)-sensitive adrenomedullin receptors derived from co- ... 2004). "Tumor necrosis factor-alpha downregulates adrenomedullin receptors in human coronary artery smooth muscle cells". ... receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. In combination with the ... adrenomedullin, and amylin receptor function". Mol. Pharmacol. 74 (4): 1059-71. doi:10.1124/mol.108.047142. PMID 18593822. ...
Stress can cause high levels of the following hormones: norepinephrine, leptin, NPY, nitrite, ACTH and adrenomedullin. Elevated ...
The placenta normally produces the potent vasodilator adrenomedullin but it is reduced in pre-eclampsia and eclampsia. Other ... "Adrenomedullin is decreased in preeclampsia because of failed response to epidermal growth factor and impaired syncytialization ...
Born W, Muff R, Fischer JA (2002). "Functional interaction of G protein-coupled receptors of the adrenomedullin peptide family ... 1999). "The RAMP2/CRLR complex is a functional adrenomedullin receptor in human endothelial and vascular smooth muscle cells". ... 2000). "CGRP-RCP, a novel protein required for signal transduction at calcitonin gene-related peptide and adrenomedullin ... Hill H, Pioszak A (2013). "Bacterial expression and purification of a heterodimeric adrenomedullin receptor extracellular ...
The likelihood is that the phenotype of RAMP2 KO mice is more connected with the abolition of most adrenomedullin (AM) ... "The RAMP2/CRLR complex is a functional adrenomedullin receptor in human endothelial and vascular smooth muscle cells". FEBS ... to AM KO mice and mice lacking the Calcitonin-like receptor which are unable to form either AM1 or AM-2 adrenomedullin ...
... and physiological actions of factor H as an adrenomedullin binding protein present in human plasma". Microscopy Research and ...
Evans JJ, Youssef AH, Yandle TG, Lewis LK, Nicholls MG (October 2002). "Effects of endothelin-1 on release of adrenomedullin ...
"CL/RAMP2 and CL/RAMP3 produce pharmacologically distinct adrenomedullin receptors: a comparison of effects of adrenomedullin22- ...
"Mid-regional pro-adrenomedullin outperforms N-terminal pro-B-type natriuretic peptide for the diagnosis of acute heart failure ... Plasma N-terminal pro-brain natriuretic peptide and adrenomedullin: new neurohormonal predictors of left ventricular function ...
... and adrenomedullin. Neutral endopeptidase (NEP) also known as neprilysin is the enzyme that metabolizes natriuretic peptides. ...
... and the precursor of adrenomedullin. Secretion of calcitonin is stimulated by: an increase in serum [Ca2+] gastrin and ...
PHI PHM PHV Endogenous Adrenomedullin Apelin Asprosin Bombesin Calcitonin Carnosine CART CLIP DSIP Enteroglucagon Formyl ...
... and adrenomedullin. The physiology of their secretion and its regulation is incompletely understood. Regulatory cues might come ...
... the national authority managing Morocco's expressways Abductor digiti minimi muscle of hand Adrenomedullin, a vasodilator ...
... and adrenomedullin. Calcitonin is a 32 amino acid polypeptide hormone that causes a rapid but short-lived drop in the level of ...
Adrenomedullin receptor (GPR182) Duffy blood group, chemokine receptor (DARC, DUFF) G Protein-coupled Receptor 30 (GPER, CML2, ...
... adrenomedullin, and semaphorin 4D. Moreover, cytokines produced by TAMs induce tumor cells to produce pro-angiogenic factors, ...
Structure and dynamics of the adrenomedullin (AM) receptors, AM1 and AM2, reveals key mechanisms in the control of receptor ...
Adrenomedullin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Human ADM genome location and ADM gene ... Adrenomedullin (ADM or AM) is a vasodilator peptide hormone of uncertain significance in human health and disease. It was ... Adrenomedullin may function as a hormone in the circulation control because it is found in blood in a considerable ... The adrenomedullin knockout is an embryonic lethal phenotype and dies mid gestation from a condition known as hydrops fetalis. ...
Human adrenomedullin (hAM), a potent vasodilatory peptide originally identified in pheochromocytoma, has been shown to be ... Increased circulating adrenomedullin, a novel vasodilatory peptide, in sepsis J Clin Endocrinol Metab. 1996 Apr;81(4):1449-53. ... Human adrenomedullin (hAM), a potent vasodilatory peptide originally identified in pheochromocytoma, has been shown to be ...
Haemodynamic and hormonal effects of adrenomedullin in patients with pulmonary hypertension Message subject: (Your Name) has ...
Calcitonin gene-related peptide (CGRP), adrenomedullin (AM) and adrenomedullin 2 (AM2) are related peptides, which are potent ... N2 - Calcitonin gene-related peptide (CGRP), adrenomedullin (AM) and adrenomedullin 2 (AM2) are related peptides, which are ... AB - Calcitonin gene-related peptide (CGRP), adrenomedullin (AM) and adrenomedullin 2 (AM2) are related peptides, which are ... abstract = "Calcitonin gene-related peptide (CGRP), adrenomedullin (AM) and adrenomedullin 2 (AM2) are related peptides, which ...
Adrenomedullin peptides and precursor levels in relation to haemodynamics and prognosis after heart transplantation. *Mark ... Out of 18 plasma proteins, 11 proteins including adrenomedullin peptides and precursor levels (ADM) and protein suppression of ... Out of 18 plasma proteins, 11 proteins including adrenomedullin peptides and precursor levels (ADM) and protein suppression of ... Adrenomedullin peptides and precursor levels in relation to haemodynamics and prognosis after heart transplantation}}, url = {{ ...
Human AMR(Adrenomedullin Receptor) ELISA Kit. Human AMR(Adrenomedullin Receptor) ELISA Kit ... Description: A sandwich ELISA kit for detection of Adrenomedullin Receptor from Human in samples from blood, serum, plasma, ... Description: A sandwich quantitative ELISA assay kit for detection of Human Adrenomedullin (ADM) in samples from serum, plasma ... Description: A sandwich quantitative ELISA assay kit for detection of Human Adrenomedullin (ADM) in samples from serum, plasma ...
Description: A sandwich ELISA kit for detection of Adrenomedullin from Rat in samples from blood, serum, plasma, cell culture ... Description: A sandwich quantitative ELISA assay kit for detection of Rat Adrenomedullin (ADM) in samples from serum, plasma or ... Description: A sandwich quantitative ELISA assay kit for detection of Rat Adrenomedullin (ADM) in samples from serum, plasma or ... Description: A sandwich ELISA kit for quantitative measurement of Rat ADM (Adrenomedullin) in samples from Serum, Plasma, Cell ...
Home / Peptides / Adrenomedullin Peptides / Adrenomedullin (1-50), human. Adrenomedullin (1-50), human. $300.00. - $495.00. ... Rat adrenomedullin, rADM, (1-50) and its C-terminal rADM (11-50) induce a dose-dependent and endothelium-independent ...
Home › ELISA Kits › Bovine Adrenomedullin (ADM) ELISA Kit Bovine Adrenomedullin (ADM) ELISA Kit. ...
... rat is a peptide fragment of adrenomedullin that acts on calcitonin gene-related peptide-1 (CGRP1) receptors. ... Adrenomedullin (11-50) is the active C-terminal fragment of rat adrenomedullin. Adrenomedullin is thought to be a vasodilator ...
Human AMR(Adrenomedullin Receptor) ELISA Kit Human AMR(Adrenomedullin Receptor) ELISA Kit. To Order Contact us: [email protected] ... Description: A sandwich quantitative ELISA assay kit for detection of Rat Adrenomedullin (ADM) in samples from serum, plasma or ... Description: A sandwich quantitative ELISA assay kit for detection of Rat Adrenomedullin (ADM) in samples from serum, plasma or ... Description: A sandwich ELISA kit for detection of Adrenomedullin Receptor from Human in samples from blood, serum, plasma, ...
title = "Plasma adrenomedullin levels in patients on hemodialysis",. abstract = "Adrenomedullin (AM) is a hypotensive peptide ... Plasma adrenomedullin levels in patients on hemodialysis. / Yamasaki, Hiroko; Nagake, Yoshio; Akagi, Shigeru et al. In: Nephron ... Plasma adrenomedullin levels in patients on hemodialysis. Hiroko Yamasaki, Yoshio Nagake, Shigeru Akagi, Taro Sugimoto, Haruo ... Adrenomedullin (AM) is a hypotensive peptide that has recently been isolated from human pheochromocytoma. In this study, we ...
... Quantity: Order. ... Mid-regional pro-adrenomedullin as a novel predictor of mortality in patients with chronic heart failure. Eur J Heart Fail. ... Adrenomedullin (AM) is a 52 amino acid vasoactive peptide discovered in 1993. A member of the calcitonin family of peptides, it ... AIMS: Adrenomedullin (ADM) is a vasodilatory peptide. Its plasma levels or its precursors have not been evaluated in large ...
Central adrenomedullin augments the baroreceptor reflex in conscious rabbits. In: Hypertension. 1999 ; Vol. 33, No. 4. pp. 992- ... Central adrenomedullin augments the baroreceptor reflex in conscious rabbits. Kiyoshi Matsumura, Isao Abe, Takuya Tsuchihashi, ... title = "Central adrenomedullin augments the baroreceptor reflex in conscious rabbits",. abstract = "We examined the roles of ... Central adrenomedullin augments the baroreceptor reflex in conscious rabbits. / Matsumura, Kiyoshi; Abe, Isao; Tsuchihashi, ...
Keywords: Adrenomedullin, heart failure, antifibrotic effects, cardiovascular diseases, neurohumoral factors, cAMP response ... Keywords: Adrenomedullin, heart failure, antifibrotic effects, cardiovascular diseases, neurohumoral factors, cAMP response ... Adrenomedullin in Heart Failure: Molecular Mechanism and Therapeutic Implication. Author(s): Toshio Nishikimi, Kazuwa Nakao and ... Adrenomedullin (AM) is a potent long-lasting vasodilatory peptide that was discovered in acid extracts of human ...
Synthetic rat adrenomedullin (rADM) induces effective and durable antihypertensive activity in anesthetized rats. ...
A comparison of the actions of BIBN4096BS and CGRP 8-37 on CGRP and adrenomedullin receptors expressed on SK-N-MC, L6, Col 29 ... A comparison of the actions of BIBN4096BS and CGRP 8-37 on CGRP and adrenomedullin receptors expressed on SK-N-MC, L6, Col 29 ... A comparison of the actions of BIBN4096BS and CGRP 8-37 on CGRP and adrenomedullin receptors expressed on SK-N-MC, L6, Col 29 ... A comparison of the actions of BIBN4096BS and CGRP 8-37 on CGRP and adrenomedullin receptors expressed on SK-N-MC, L6, Col 29 ...
... Quantity: Order. ... These results suggest that IMD(1-53), like adrenomedullin, has cardioprotective effects against myocardial I/R injury.. Yang JH ... Interestingly, the above IMD effects were similar to those of adrenomedullin (10(-8)mol/L). These results suggest that IMD, ... Calcitonin, calcitonin gene-related peptide (CGRP), adrenomedullin (ADM), and amylin belong to a unique group of peptide ...
Rat adrenomedullin, rADM, (1-50) and its C-terminal rADM (11-50) induce a dose-dependent and endothelium-independent ...
Endothelin-1 receptor antagonist and adrenomedullin improve functional recovery after myocardial infarction. ...
Prognostic Value of Adrenomedullin and Natriuretic Peptides in Uroseptic Patients Induced by Ureteroscopy. Wei Hu , Pang-hu ...
... human-武汉科斯坦生物科技有限公司-Pro-Adrenomedullin (N-20), human ...
Scale bar: 500 μm (hypoxia, first and third images); 50 μm (hypoxia, second and fourth images); 100 μm (adrenomedullin). (C and ... Tumor-associated macrophages promote angiogenesis and melanoma growth via adrenomedullin in a paracrine and autocrine manner. ... Grk2fl/fl animals displayed higher infiltration of macrophages and a marked increase of hypoxia and adrenomedullin, known to ... GRK2 and adrenomedullin expression, hypoxic status, or macrophage infiltration. Human breast tissue samples were obtained from ...
Molecular forms of adrenomedullin in pericardial fluid and plasma in patients with ischaemic heart disease Toshio NISHIKIMI; ... Experimental studies have demonstrated that adrenomedullin (AM) has a positive inotropic action and exerts inhibitory effects ... Molecular forms of adrenomedullin in pericardial fluid and plasma in patients with ischaemic heart disease. Clin Sci (Lond) 1 ...
Adrenomedullin in sepsis. Hans Friberg (First/primary/lead supervisor), Olle Melander (Second supervisor), Attila Frigyesi ( ...
Adrenomedullin; Calcitonin gene-related peptide; GPCR; Receptor activity-modifying protein; Molecular modeling; Molecular ... Calcitonin gene-related peptide (CGRP) or adrenomedullin (AM) receptors are heteromers of the calcitonin receptor-like receptor ... protein dependent and independent activation mechanisms in the coupling of calcitonin gene-related peptide and adrenomedullin ... protein dependent and independent activation mechanisms in the coupling of calcitonin gene-related peptide and adrenomedullin ...
The study aimed to evaluate the transcriptional levels of the natriuretic peptides (NP), endothelin (ET)-1, adrenomedullin (ADM ... The study aimed to evaluate the transcriptional levels of the natriuretic peptides (NP), endothelin (ET)-1, adrenomedullin (ADM ... Evaluation of transcriptional levels of the natriuretic peptides, endothelin-1, adrenomedullin, their receptors and long non- ...
Keywords: urocortin 1, adrenomedullin, heart failure, pro-brain natriuretic peptide. Erkan Yıldırım, Mahir Cengiz, Nilgün ... The evaluation of the clinical utility of urocortin 1 and adrenomedullin versus proBNP in systolic heart failure. Erkan ... The evaluation of the clinical utility of urocortin 1 and adrenomedullin versus proBNP in systolic heart failure. Anatol J ... Adrenomedullin (ADM) increases cardiac output and lowers blood pressure in healthy men and in patients with heart failure. The ...

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