Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0031511 (pheochromocytoma)
 14,622 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adrenomedullin is a strong vasorelaxing peptide discovered in pheochromocytoma tissue. Monocrotaline, a pyrrolizidine alkaloid derived from Crotalaria spectabilis, is known to cause pulmonary hypertension. To test the hypothesis that adrenomedullin plays a role similar to that of atrial natriuretic peptide or brain natriuretic peptide in modulating right ventricular responses to pulmonary hypertension, we have compared concentrations of immunoreactive rat adrenomedullin and adrenomedullin messenger RNA levels in tissues of monocrotaline treated rats with those of control rats. We also measured the effect of pulmonary hypertension on plasma level of the peptide. The concentrations of adrenomedullin immunoreactivity in right ventricle and plasma were significantly higher in monocrotaline treated rats than in control rats. The messenger RNA level of adrenomedullin in right ventricle was also higher in monocrotaline treated rats than in control rats. These results suggest that adrenomedullin participates in the mechanism to counteract the high blood pressure in pulmonary circulation.
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PMID:Augmented adrenomedullin concentrations in right ventricle and plasma of experimental pulmonary hypertension. 747 19

Adrenomedullin (ADM) is a new endogenous hypotensive and vasorelaxing peptide that may play an important role in the regulation of cardiovascular function. Although ADM was originally isolated from pheochromocytoma, ADM-like immunoreactivity has also been widely detected in various tissues, including the cardiovascular system. Based upon the reports that ADM mRNA and ADM-like immunoreactivity are present in the heart, the present study was designed to investigate the immunohistochemical localization of ADM in the canine heart and aorta. In the canine heart, immunohistochemical examination revealed positive immunostaining within the myocardia in both atria and ventricles. ADM immunoreactivity was observed within the cytoplasm of myocardium, and was widely distributed in the peripheral cytoplasm. ADM immunoreactivity was more intense in the atria than in the ventricles. In the canine aorta, vascular smooth muscle cells of the aorta and vasa vasorum were also immunopositive for ADM. ADM immunoreactivity was mostly localized in the perinuclear position within the smooth muscle cells. There was no immunoreactivity in endothelium, endocardium, epicardium, adventitia, or connective tissues. The current study demonstrates for the first time that immunoreactive ADM by immunohistochemistry is present in the cardiovascular system. As ADM has hypotensive and vasorelaxing actions and circulates in the body, ADM is a cardiovascular peptide hormone that may play an important role in the regulation of cardiovascular system.
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PMID:Immunohistochemical localization of adrenomedullin in canine heart and aorta. 747 14

Adrenomedullin(AM) is a novel vasodilator peptide recently isolated from pheochromocytoma. Using a specific and sensitive radioimmunoassay for human AM, we have characterized immunoreactive AM in human plasma and urine. Patients with chronic renal failure had about five-fold higher plasma immunoreactive AM levels than normal subjects, which did not change before and after hemodialysis. Immunoreactive AM was present in normal human urine, whose concentrations were about six-fold greater than those in human plasma. Reverse-phase HPLC of human plasma and urine revealed that immunoreactive AM emerged as a single peak at a position identical to that of authentic human AM(1-52). These data suggest that circulating AM is cleared by the kidney and urinary excretion of AM may be derived from glomerular filtration and/or its renal production.
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PMID:Characterization of immunoreactive adrenomedullin in human plasma and urine. 760 98

Adrenomedullin (AM) is a potent hypotensive peptide recently discovered in extracts of human pheochromocytoma. In this report we present evidence, using reverse transcriptase-polymerase chain reaction, immunocytochemistry, and in situ reverse transcriptase-polymerase chain reaction, that AM is synthesized by several cell populations of the normal lung, tumor cell lines of pulmonary origin, and tumor specimens. Among the normal cell populations of the lung, we found AM expression in the columnar epithelium, some glands, neurons of the pulmonary parasympathetic nervous system, endothelial cells, chondrocytes, alveolar macrophages, and smooth muscle cells. In tumors, AM expression was located in most of the nonsmall cell lung carcinomas and in half of the small cell lung carcinomas studied. These findings suggest that AM may play a broad role in respiratory homeostasis and lung carcinogenesis.
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PMID:Expression of adrenomedullin in normal human lung and in pulmonary tumors. 764 18

Adrenomedullin is a novel hypotensive peptide recently isolated from human pheochromocytoma. Since a high concentration of immunoreactive adrenomedullin was found in pheochromocytoma tissue, the cDNA library of pheochromocytoma was constructed, and the cDNA clone encoding an adrenomedullin precursor was isolated and sequenced. The precursor for human adrenomedullin (human preproadrenomedullin) is 185 amino acids in length, including an adrenomedullin sequence. Proadrenomedullin (proAM) contains a unique twenty amino acid sequence followed by Gly-Lys-Arg in the N-terminal region. It is possible that a novel 20 residues peptide, termed "proadrenomedullin N-terminal 20 peptide" (proAM-N20) whose carboxy terminus may be Arg-NH2, is processed from proadrenomedullin. By RNA blot analysis, human adrenomedullin mRNA was found to be highly expressed in several tissues including adrenal medulla, ventricle, lung and kidney as well as pheochromocytoma.
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PMID:Cloning and characterization of cDNA encoding a precursor for human adrenomedullin. 768 24

Adrenomedullin is a new hypotensive peptide recently identified in human pheochromocytoma arising from adrenal medulla. We report here the cDNA encoding a rat adrenomedullin precursor. The precursor is 185 amino acids in length, including a 21 residue putative signal peptide at the N-terminus. Rat adrenomedullin consists of 50 amino acids similar to, but distinct from human adrenomedullin; 2 residues were deleted and 6 residues were substituted compared to those in the human peptide. In the proadrenomedullin N-terminal 20 peptide, whose amino acid sequence is present in adrenomedullin precursor, 3 amino acids were substituted. RNA blot analysis showed that rat adrenomedullin mRNA was expressed in adrenal glands, lung, kidney, heart, spleen, duodenum and submandibular glands. Synthetic rat adrenomedullin elicits a potent and long-lasting hypotensive activity in anesthetized rats.
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PMID:Molecular cloning and biological activities of rat adrenomedullin, a hypotensive peptide. 769 May 63

Responses to adrenomedullin, a newly discovered hypotensive peptide isolated from human pheochromocytoma cells, and the carboxy terminal 15-52 (adrenomedullin-(15-52)) and 22-52 (adrenomedullin-(22-52)) amino acid fragments of adrenomedullin were investigated in the mesenteric vascular bed of the cat. Under constant flow conditions, injections of adrenomedullin, adrenomedullin-(15-52), and calcitonin gene-related peptide (CGRP) in doses of 0.003-1 nmol into the perfused superior mesenteric artery caused significant dose-related decreases in mesenteric arterial perfusion pressure. Mesenteric vasodilator responses to adrenomedullin and adrenomedullin-(15-52) were similar in magnitude and duration, while vasodilator responses to CGRP were greater in magnitude and longer in duration than those produced by adrenomedullin or adrenomedullin-(15-52) when these agents were injected in doses of 0.1-1 nmol. Adrenomedullin-(22-52) caused no significant change in mesenteric arterial perfusion pressure when injected in doses up to 10 nmol. These results suggest that amino acids 15-52 and the six-membered ring structure of adrenomedullin are important for the expression of vasodilator activity in the mesenteric vascular bed of the cat.
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PMID:Comparison of responses to adrenomedullin and adrenomedullin analogs in the mesenteric vascular bed of the cat. 771 43

Adrenomedullin (ADM) is a newly described 52-amino acid peptide originally isolated from extracts of human pheochromocytoma and, more recently, detected in human plasma. Based on the report that ADM mRNA and immunoreactivity are present in the kidney, the current study was designed to determine the renal distribution of ADM by immunohistochemistry and the renal biological actions of ADM. In the immunohistochemical studies, the present investigation demonstrated the localization of ADM in glomeruli, cortical distal tubules, and medullary collecting duct cells of the normal canine kidney. In the in vivo studies, ADM was administered (0.25 ng.kg-1.min-1 in group I and 1, 5, and 25 ng.kg-1.min-1 in group II) intrarenally in normal mongrel dogs with the contralateral kidney receiving only saline vehicle. Intrarenal infusion of ADM resulted in a marked diuretic and natriuretic response, whereas the contralateral kidney showed no renal effects. These significant natriuresis and diuresis in the ADM kidney were associated with increases in glomerular filtration rate and fractional sodium excretion and with a decrease in distal tubular sodium reabsorption. Intrarenal infusion of ADM also caused an increase in mean arterial blood pressure and a decrease in heart rate. Plasma concentrations of atrial natriuretic peptide, renin activity, aldosterone, and guanosine 3',5'-cyclic monophosphate were not changed during the infusion of ADM. The current study demonstrates that ADM is present in renal glomerular and tubular cells and is a potent natriuretic peptide that may play an important role in the regulation of sodium excretion.
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PMID:Renal localization and actions of adrenomedullin: a natriuretic peptide. 773 22

Adrenomedullin is a potent vasodilator peptide that was isolated from human pheochromocytoma. But the presence of adrenomedullin in the brain has not been clarified. We studied the presence of adrenomedullin in the human brain obtained at autopsy from 6 subjects by radioimmunoassay, as well as in the human adrenal glands and tumor tissues of pheochromocytoma, ganglioneuroblastoma and neuroblastoma. Immunoreactive adrenomedullin was detected in every region of human brain examined (0.26-1.4 pmol/g wet weight) with the highest concentrations found in thalamus (1.40 +/- 0.39 pmol/g wet weight, mean +/- SEM) and hypothalamus (1.28 +/- 0.48 pmol/g wet weight). Reverse phase high performance liquid chromatography showed that the immunoreactive adrenomedullin in the human brain was eluted in the position of synthetic human adrenomedullin 1-52. High concentrations of immunoreactive adrenomedullin were found in human adrenal glands (12.6 +/- 1.0 pmol/g wet weight, n = 7), pheochromocytoma (4.5 +/- 1.5 pmol/g wet weight, n = 11), ganglioneuroblastoma (2.0 +/- 1.3 pmol/g wet weight, n = 4) and neuroblastoma (0.55 +/- 0.21 pmol/g wet weight, n = 3). The present study has shown that adrenomedullin is present in the human brain in high concentrations, suggesting that adrenomedullin acts as a neurotransmitter, neuromodulator or neurohormone in man.
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PMID:Adrenomedullin in human brain, adrenal glands and tumor tissues of pheochromocytoma, ganglioneuroblastoma and neuroblastoma. 774 31

Proadrenomedullin N-terminal 20 peptide (PAMP) is a novel hypotensive peptide found in adrenomedullin precursor. Using a radioimmunoassay for human PAMP, we purified immunoreactive PAMP (ir-PAMP) from human pheochromocytoma and determined its complete amino acid sequence. The major component of PAMP-like immunoreactivity was found to be PAMP [1-20] NH2 with an amino acid sequence identical to that of the deduced amino acid sequence by cDNA analysis. Both ir-PAMP and ir-adrenomedullin were found to be abundant in normal adrenal medulla as well as pheochromocytoma tissue arising from adrenal medulla, and there was a significantly (p < 0.05) positive correlation between ir-adrenomedullin and ir-PAMP concentrations in these tissues. However, the PAMP/adrenomedullin ratio in pheochromocytoma tissues (0.197 +/- 0.013) was significantly (p < 0.005) lower than that in adrenal medullae (0.384 +/- 0.041). The present data indicate that PAMP is biosynthesized from adrenomedullin precursor, but the biosynthesis or metabolism of PAMP in pheochromocytoma may be different from that of normal adrenal medulla.
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PMID:Human proadrenomedullin N-terminal 20 peptide in pheochromocytoma and normal adrenal medulla. 779 84


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