Processing of proendothelin‐1 by members of the subtilisin‐like pro‐protein convertase family

FEBS Letters

Leduc, Richard¹  Klarskov, Klaus¹  Day, Robert¹  Fugère, Martin¹  Blais, Véronique¹  Denault, Jean-Bernard¹ 

[1] Department of Pharmacology, Faculty of Medicine, Université de Sherbrooke, 3001 12th Ave North, Sherbrooke, QC, Canada J1H 5N4

关键词: Endothelin-1;    Precursor protein;    Proteolytic cleavage;    Furin;    PC7;    Endothelial cell;    amc;    7-amido-4-methylcoumarine;    EC;    endothelial cell;    ET-1;    endothelin-1;    HUVEC;    human umbilical vein endothelial cell;    SPC;    subtilisin-like pro-protein convertase;   

DOI  :  10.1016/S0014-5793(02)02998-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Endothelial cells (ECs) secrete numerous bioactive peptides that are initially synthesized as inactive precursor proteins. One of these, proendothelin-1 (proET-1), undergoes proteolysis at specific pairs of basic amino acids. Here, we wished to examine the role of mammalian convertases in this event. Northern blot analysis shows that only furin and PC7 are expressed in ECs. In vitro cleavage of proET-1 by furin or PC7 demonstrated that both enzymes efficiently and specifically process proET-1. These data reveal that furin and PC7 have similar specificities towards proET-1 and suggest that both enzymes may participate in the maturation of proET-1 in ECs.

【 授权许可】

Unknown