Role of the prohormone convertase PC2 in the processing of proglucagon to glucagon

FEBS Letters

Rouillé, Yves¹  Halban, Philippe A.¹  Irminger, Jean-Claude¹  Bianchi, Matteo¹ 

[1] Laboratoires de Recherche Louis Jeantet, Centre Médical Universitaire, 1 rue Michel Servet, 1211 Geneva 4, Switzerland

关键词: Proglucagon;    Prohormone processing;    Islet of Langerhans;    Adenovirus vector;    α-Cell;    GLP;    glucagon-like peptide;    IP;    intervening peptide;    GRPP;    glicentin-related polypeptide;    MPGF;    major proglucagon fragment;    tGLP-1;    truncated GLP-1 (GLP-1-(7-37) and/or GLP-1-(7-36amide));    DMEM;    Dulbecco's modified Eagle's medium;    FCS;    fetal calf serum;    SDS-PAGE;    sodium dodecylsulfate-polyacrylamide gel electrophoresis;    HPLC;    high performance liquid chromatography;    CPE;    carboxypeptidase E;    TPCK;    N-Tosyl-l-phenylalanine chloromethyl ketone;    TLCK;    Nα-p-Tosyl-l-lysine chloromethyl ketone;    SPC;    subtilisine-like proprotein convertase;    PG;    proglucagon;   

DOI  :  10.1016/S0014-5793(97)00892-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Proglucagon is alternatively processed to glucagon in pancreatic α-cells, or to glucagon-like peptide-1 in intestinal L cells. Here, the specificity of PC2, the major prohormone convertase of α-cells, was examined both in vivo and in vitro. Adenovirus-mediated co-expression of proglucagon and PC2 in GH₄C₁ cells resulted in a pattern of processing products very similar to that observed in α-cells. Oxyntomodulin, an intermediate in the processing of proglucagon, was quantitatively converted to glucagon in vitro by purified recombinant PC2, in combination with carboxypeptidase E. It is concluded that PC2 is able to act alone in the pancreatic pathway of proglucagon processing.

【 授权许可】

Unknown