Identification and hypotensive activity of proadrenomedullin N‐terminal 20 peptide (PAMP)

Kïtamura, Kazuo; Kangawa, Kenji; Ishiyama, Yuichiro; Washimine, Hisanori; Ichiki, Yoshinari; Kawamoto, Mari; Minamino, Naoto; Matsuo, Hisayuki; Eto, Tanenao

doi:10.1016/0014-5793(94)00810-8

Cited by 136 publications

(86 citation statements)

References 6 publications

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“…Since the previous RIA for the entire PAMP-20 molecule showed only 19% cross-reactivity with PAMP-12 [6], the existence of PAMP-12 in vivo was not identified in previous studies [7,8]. In the present study, the immunoreactive peak of PAMP-12 was demonstrated to be reproducibly higher than that of PAMP-20 by the RP-HPLC analyses, indicating that this peptide exists in vivo as an endogenous peptide.…”

Section: Discussioncontrasting

confidence: 61%

“…With the use of this RIA, the existence of PAMP-20 in vivo was demonstrated by the isolation and characterization of the peptide from both human pheochromocytoma and porcine adrenal medulla [7,8]. PAMP-20 elicited a potent hypotensive effect when injected intravenously in anesthetized rats [8]. PAMP-20 also inhibited carbachol-induced catecholamine synthesis and secretion in cultured bovine adrenal medullary cells [9,10].…”

Section: *Corresponding Author Fax: (81) (985) 85-6596mentioning

confidence: 99%

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Purification and characterization of PAMP‐12 (PAMP[9–20]) in porcine adrenal medulla as a major endogenous biologically active peptide

et al. 1997

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Proadrenomedullin N-terminal 20 peptide (PAMP-20) is a potent hypotensive peptide processed from the adrenomedullin (AM) precursor. We developed a specific radioimmunoassay which recognizes the C-terminal region of PAMP-20. Using this radioimmunoassay, the distribution of immunoreactive (ir-) PAMP was determined in porcine tissues. High concentrations of ir-PAMP were observed in the adrenal medulla and in the atrium, and these values were comparable to the corresponding concentrations of ir-AM. The concentration of ir-PAMP was almost the same as that of ir-AM in the kidney, while ir-PAMP was significantly lower than ir-AM in the ventricle, lung, and aorta. Reversed-phase high performance liquid chromatography in each porcine tissue sample revealed that two major peaks of ir-PAMP existed: one emerged at a position identical to that of authentic porcine PAMP-20; the other unknown peak was eluted earlier. The unknown peptide was purified to homogeneity from porcine adrenal medulla, and its complete amino acid sequence was determined. This peptide was found to be PAMP[9-20] with a C-terminal amide structure, and was named PAMP-12. Intravenous injections of PAMP-12 in anesthetized rats showed a significant hypotensive effect in a dose-dependent fashion, and the effect was comparable to that of PAMP-20. These data indicate that PAMP-12, a major component of ir-PAMP, is processed from the AM precursor, as is PAMP-20, and may participate in cardiovascular control.

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Section: Discussioncontrasting

confidence: 61%

Section: *Corresponding Author Fax: (81) (985) 85-6596mentioning

confidence: 99%

Purification and characterization of PAMP‐12 (PAMP[9–20]) in porcine adrenal medulla as a major endogenous biologically active peptide

et al. 1997

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“…9,10 PAMP, but not AM, was specifically expressed by some NE cells of the human normal prostate. 11 NE expression in other tissues has also been associated with PAMP production.…”

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confidence: 93%

“…12 However, this peptide was first described in the vascular wall and in endocrine organs in normal and pathologic situations. 13 PAMP is a pluripotent peptide initially identified as a vasodilator, 9 but it can additionally act as a neural transmission inhibitor, 14 an endocrine secretion inhibitor 15 or a cell growth suppressor. 16 Some of these roles could contribute to the regulation of prostatic homeostasis or functioning.…”

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confidence: 99%

Peptidylglycine ?-amidating monooxygenase- and proadrenomedullin-derived peptide-associated neuroendocrine differentiation are induced by androgen deprivation in the neoplastic prostate

Jiménez¹,

Jongsma²,

Calvo³

et al. 2001

Int. J. Cancer

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Most PCs show NE differentiation. Several studies have tried to correlate NE expression with disease status, but the reported findings have been contradictory. Prostatic NE cells synthesize peptides with a wide spectrum of potential functions. Some of these active peptides, such as PAMP, are amidated. PAM is the only carboxy-terminal peptide-amidating enzyme identified. We studied expression of PAMP and PAM in normal prostate and prostatic tumors (clinical specimens and human xenograft models) with or without prior androgen-deprivation therapy and found a wide distribution of both molecules in NE subpopulations of all kinds. Although the correlation of either marker to tumor grade, clinical progression or disease prognosis did not reach statistical significance, PAMP-or PAM-immunoreactive cells were induced after androgen-blockade therapy. In the PC-310 and PC-295 androgen-dependent models, PAMP or PAM NE differentiation was induced after castration in different ways, being higher in PC-310, which might explain its long-term survival after androgen deprivation. We show induction of expression of 2 new NE markers in clinical specimens and xenografted PC after endocrine therapy.

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“…ADM inhibits ACTH secretion from the pituitary, insulin secretion from the pancreas, and catecholamine secretion from the adrenal gland [28]. PAMP is biologically active and it is a hypotensive agent [4,15] that decreases catecholamine secretion [13,29,36].…”

Section: Introductionmentioning

confidence: 99%

Proadrenomedullin NH2-terminal 20 peptide (PAMP) and adrenomedullin bind to teratocarcinoma cells☆

et al. 2000

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Proadrenomedullin NH 2-terminal 20 peptide (PAMP) and adrenomedullin (ADM) bind to teratocarcinoma cells. The effects of PAMP and ADM on teratocarcinoma cells were investigated. 125 I-PAMP bound to PA1 cells with moderate affinity (K d ϭ 110 nM) to a single class of sites (B max ϭ 110 000/cell). Specific 125 I-PAMP binding was inhibited by PAMP (IC 50 of 100 nM) but not ADM, calcitonin gene-related peptide (CGRP), or amylin. Specific 125 I-ADM binding was inhibited with high affinity by ADM, CGRP, and CGRP(8 -37) (IC 50 values of 10, 10, and 15 nM respectively) but not PAMP or amylin. ADM elevated cAMP (ED 50 value of 100 nM), whereas PAMP had no effect on basal cAMP but inhibited the increase in cAMP caused by 10 nM ADM. Also, the increase in cAMP caused by ADM was inhibited CGRP(8 -37), suggesting that ADM is binding to CGRP receptors. ADM (100 nM) stimulated transiently c-fos mRNA, whereas PAMP (1000 nM) had little effect; however, PAMP inhibited the increase in c-fos mRNA caused by ADM. ADM stimulated [ 3 H]thymidine uptake into PA1 cells, whereas PAMP inhibited the increase in thymidine uptake caused by ADM. These results indicate that ADM and PAMP are both biologically active in teratocarcinoma cells. Published by Elsevier Science Inc.

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Identification and hypotensive activity of proadrenomedullin N‐terminal 20 peptide (PAMP)

Cited by 136 publications

References 6 publications

Purification and characterization of PAMP‐12 (PAMP[9–20]) in porcine adrenal medulla as a major endogenous biologically active peptide

Purification and characterization of PAMP‐12 (PAMP[9–20]) in porcine adrenal medulla as a major endogenous biologically active peptide

Peptidylglycine ?-amidating monooxygenase- and proadrenomedullin-derived peptide-associated neuroendocrine differentiation are induced by androgen deprivation in the neoplastic prostate

Proadrenomedullin NH2-terminal 20 peptide (PAMP) and adrenomedullin bind to teratocarcinoma cells☆

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