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Post-translational modifications of heterologously expressed cholecystokinin in Saccharomyces cerevisiae.

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  • 1Department of Clinical Biochemistry, Rigshospitalet, University of Copenhagen, Denmark.


The vertebrate neuroendocrine peptide cholecystokinin (CCK) is subjected to numerous post-translational modifications upon maturation to bioactive CCK. However, the current knowledge of the proteolytic processing of proCCK, as reviewed here, is not complete. We have chosen Saccharomyces cerevisiae as a model to study these endoproteolytic processing events. Expression of proCCK as a fusion protein to the prepro leader peptide of alpha-mating factor directed the protein through the secretory pathway and resulted in nanomolar concentrations of secreted glycine-extended CCK. The CCK peptides showed many correlations to the known endoproteolytic processing products of proCCK in endocrine cells. Especially the processing to the abundant form, CCK-22, was investigated and it is suggested that a novel enzyme is responsible for its production. Thus, yeast may be used to study the proteolysis of proCCK with the aim to identify mammalian homologues involved in maturation of CCK.

[PubMed - indexed for MEDLINE]
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