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Adrenomedullin: a novel hypotensive peptide isolated from human pheochromocytoma 1993

Natl Cardiovasc Ctr, Res Inst, Suita, Osaka 565, Japan and Miyazaki Med Coll, Biochem Rech Inst, Miyazaki 88916, Japan
Biochemical and Biophysical Research Communications (Impact Factor: 2.28). 08/2012; 425(3):548-55. DOI: 10.1016/j.bbrc.2012.08.022
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    • "Since the discovery of AM in human , a 52 - amino acid peptide ( Kitamura et al . , 1993a ) , sequences from other species have then been elucidated . For instance , the rat AM contains 50 amino acids with 2 residues deleted and 6 residues substituted when compared to the human peptide ( Sakata et al . , 1993 ) ; the porcine AM , is found to be nearly identical to the human peptide , except with one residue substitution at p"
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    • "S ince the discovery of adrenomedullin (AM) in 1993 (Kitamura et al. 1993), an increasing number of studies have detected its expression in almost every tissue of the body but most remarkably in heart, kidney, pancreas, intestines, and lung (Martínez et al. 1995; Richards et al. 1996; Cameron and Fleming 1998; Asada et al. 1999; Hinson et al. 2000; López and Cuesta 2002). As expected from a peptide with such a wide distribution, a broad range of biological actions is attributed to AM, including vasodilatation, regulation of hormone secretion, cell growth, and antimicrobial effects, among others (López and Martínez 2002). "
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    ABSTRACT: Adrenomedullin (AM) is a potent vasodilator peptide present in the lung of mammals where it is expressed mainly in the columnar epithelium and alveolar macrophages. AM increases the secretion of phosphatidylcholine by type II pneumocytes, which suggests a role as an autocrine modulator of surfactant secretion. In this study we show the expression of an AM-like protein in the lung of the pigeon, Columba livia. Using an antibody against its human ortholog, AM-like immunoreactivity was found to be associated with membranous structures of the multivesicular bodies of type II pneumocytes. We also studied the differential expression of AM-like peptide in the lung of pigeons exposed to polluted city air vs cleaner countryside conditions and found that AM-like expression was higher in city animals. Similar results were obtained in an experimental study in which pigeons were exposed to increasing concentrations of a single pollutant, ozone. Taken together, our findings support the implication of AM in the response of type II pneumocytes to air pollutants.
    Journal of Histochemistry and Cytochemistry 07/2005; 53(6):773-80. DOI:10.1369/jhc.4A6498.2005 · 2.40 Impact Factor
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    • "lfide bridge between cysteine residues in positions 16 and 21 forming a six - amino acid ring ( Figure 1 . 1 ) ( Kitamura et al . , 1993a ; Beltowski and Jamroz , 2004 ) . These structural features are common to AM , amylin and calcitonin gene - related peptide ( CGRP ) , which all belong to the calcitonin family of peptides including calcitonin ( Kitamura et al . , 1993a ) . Recently , Roh et al . ( 2004 ) have identified intermedin as a new member of the calcitonin / CGRP peptide family on the basis of phylogenetic analysis ."
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