肾上腺髓质素前体肽内不同片段间的相互作用

肾上腺髓质素(adrenomedullin,ADM)是1993年由Kitamura等1]发现的一种心血管活性肽.ADM除具有强大的舒张血管、降低血压、抑制血管平滑肌细胞(vascular smooth muscle cells,VSMC)迁移、增殖作用外,还有利钠、利尿和心脏保护等作用,在维持循环稳态和心血管疾病中具有重要意义1].随后人们发现ADM前体(preproADM,185个氨基酸残基)在体内经内源性肽酶降解后产生的另外3个片段也具有生物学效应:肾上腺髓质素原N末端20肽(preproADM22-41,proADM N terminal20 peptide,PAMP)具有弱的舒张血管、降低血压作用2];preproADM153-185具有升高血压、促进VSMC增殖的作用3];preproADM45-92亦具有弱的舒张血管、轻度降低血压的作用3,4 ].

Interaction among different fragments of the precursor peptide preproadrenomedullin

Adrenomedullin (ADM) is a vasodilator and hypotensive peptide. The precursor of ADM can be decomposed into four peptide fragments in vivo by endogenous aminopeptidase: pro adrenomedullin N terminal 20 peptide(PAMP), preproADM 45 92 , preproADM 95 146 (ADM) and preproADM 153 185 . Each peptide can exert various bioactive effects independently. However, there is an interaction among different fragments from common precursor (preproADM) in their bioactive effects, signal transduction and gene expression. The interaction among different fragments from common preproADM has physiological and pathophysiological significance and needs to be further investigated.