Intracellular proteolytic processing of proopiomelanocortin in heterologous COS-1 cells by the yeast KEX2 endoprotease |
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| Authors: | L Zollinger C Racine P Crine G Boileau D Germain D Y Thomas F Gossard |
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| Institution: | Département de Biochimie, Faculté de Médecine, Université de Montréal, Québec, Canada. |
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| Abstract: | We have transiently expressed the yeast KEX2 gene together with the proopiomelanocortin (POMC) cDNA in COS-1 cells. Characterization of the POMC-related immunoreactive peptides by gel permeation and reversed-phase high pressure liquid chromatography showed that the KEX2 enzyme was active and capable of carrying out cleavage of POMC to release the authentic maturation product beta-endorphin(1-31). Peptides resembling beta-lipotropin, the amino terminal glycopeptide, and ACTH(1-39) were also detected as major products in the cell extracts. Our results indicate that the KEX2 enzyme can proteolytically release from POMC a set of peptides similar to that normally found in interior pituitary. |
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