Biochemical and Biophysical Research Communications
Regular ArticleImmunoreactive Proadrenomedullin N-Terminal 20 Peptide in Human Tissue, Plasma and Urine
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Proadrenomedullin N-terminal 20 peptide (PAMP) and its C-terminal 12-residue peptide, PAMP(9–20): Cell selectivity and antimicrobial mechanism
2020, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Although AM and PAMP both have hypotensive effects in the cardiovascular system, they also exert diverse and distinct effects on endocrine physiology, innate immunity, cytoskeletal biology, and receptor signaling pathways [2]. Similar to AM, PAMP is potently expressed and secreted by adrenal chromaffin cells but is also widely found throughout the body, including the plasma and urine [3]. Kuwasako et al. identified the C-terminal 12-residues of PAMP [PAMP(9–20)] in porcine adrenal medulla as a major endogenous active peptide of the AM precursor and demonstrated that its hypotensive activity is comparable to that of PAMP [4].
Genetic loss of proadrenomedullin N-terminal 20 peptide (PAMP) in mice is compatible with survival
2019, PeptidesCitation Excerpt :Far fewer studies have addressed the role of PAMP in physiology and pathophysiology. Like AM, PAMP is potently expressed and secreted by adrenal chromaffin cells but is also found widely throughout the body, including in plasma and urine [5]. PAMP is hydrolyzed by neprilysin, and like other neprilysin targets, exerts a hypotensive effect [6].
Expression of the adrenomedullin gene in adipose tissue
2005, Regulatory PeptidesIdentification of MrgX2 as a human G-protein-coupled receptor for proadrenomedullin N-terminal peptides
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Our data showed that MrgX2 responded to PAMP-12 with an EC50 value of 20–50 nM (Figs. 1 and 2). Under physiological conditions, immunoreactive-PAMP was reported to be present at 222.3 ± 27.2 fmol/mg in the wet tissue of the porcine adrenal medulla [4] and 18.4 fmol/mg in the wet tissue of the human adrenal medulla [6], which indicates that a 10–100 nM order of PAMP would exist in the tissue. The expression of MrgX2 in the adrenal chromaffin cells (Fig. 4B) suggests that PAMP would act in the adrenal medulla locally and that MrgX2 would be a previously proposed receptor that regulates catecholamine secretion and production from the adrenal medulla by PAMP in an autocrine or paracrine fashion under physiological conditions.