In:
Annals of Clinical Biochemistry: International Journal of Laboratory Medicine, SAGE Publications, Vol. 36, No. 5 ( 1999-09), p. 622-628
Abstract:
The novel hypotensive peptide, proadrenomedullin N-terminal 20 peptide (PAMP), is processed from the adrenomedullin precursor. Recently, we identified PAMP-12 [PAMP(9-20)] from the porcine adrenal medulla as a major endogenous and biologically active peptide. Using a new, sensitive radioimmunoassay which recognizes the C-terminal region of PAMP-20 [PAMP(1-20)] , we investigated the role of PAMP in patients with essential hypertension who had normal renal function, and whether PAMP-12 is present in humans. The mean PAMP plasma concentration, like that of adrenomedullin, was significantly higher in hypertensive [1·51 fmol/mL, standard error of the mean (SEM) 0·09 fmol/mL] than normotensive participants (1·08 fmol/mL, SEM 0·05). The increase in plasma PAMP concentration in patients with organ damage accompanied by hypertension was significantly higher than that in patients without organ damage. The PAMP concentration had a significant positive correlation with mean blood pressure and adrenomedullin concentration. The immunoreactive PAMP in human tissue and plasma was characterized by reverse-phase high-performance liquid chromatography. PAMP-12, as well as PAMP-20, was abundant in the phaeochromocytoma tissue. These findings suggest that PAMP plays some pathophysiological role against the development of essential hypertension.
Type of Medium:
Online Resource
ISSN:
0004-5632
,
1758-1001
DOI:
10.1177/000456329903600510
Language:
English
Publisher:
SAGE Publications
Publication Date:
1999
detail.hit.zdb_id:
2041298-8
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