Abstract
Secreted polypeptides pass through a complex intracellular route before reaching the cell surface, and this route is used, to some extent, by plasma membrane proteins as well. Among the former, secreted peptides are of particular interest, as they originate from larger precursors from which they are liberated by different processing reactions in the course of this intracellular transport. In common with other secreted polypeptides, these precursors contain as nascent chains a prepeptide or signal peptide that is cleaved early, probably cotranslationally, as demonstrated for larger polypeptides. The resulting propeptides are then transported to the Golgi apparatus, where they apparently enter a special route by being packaged into secretory granules. Most, and possibly all, of the further processing takes place in these granules. The mature peptides are then stored and finally released in response to a variety of physiological stimuli. In recent years, it has been demonstrated that several biologically active peptides of diverse functions may be liberated from a given precursor. Morover, different processing routes may operate in different cell types. In spite of this complex picture, it still appears that only a few types of enzymatic reactions are involved in the liberation of most peptides serving as hormones, neurotransmitters, or in defensive secretions. Our current knowledge about the enzymes catalyzing these typical cleavages is summarized in this review. The maturation of prohormones has recently been reviewed by Docherty and Steiner (1), and I will thus concentrate on the findings made during the last years.
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Kreil, G. (1986). The Posttranslational Processing of the Precursors of Secreted Peptides. In: Strauss, A.W., Boime, I., Kreil, G. (eds) Protein Compartmentalization. Springer Series in Molecular Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4930-6_4
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DOI: https://doi.org/10.1007/978-1-4612-4930-6_4
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