Patterns of prohormone processing. Order revealed by a new procholecystokinin-derived peptide
| Autor: | R. Williams, D. Grandt, J Moessner, W. Niebel, Viktor E. Eysselein, Terry D. Lee, M. T. Davis, G. A. Eberlein, J. Zeeh, John E. Shively |
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| Rok vydání: | 1992 |
| Předmět: |
Tyrosine sulfation
chemistry.chemical_classification Signal peptidase biology Chemistry digestive oral and skin physiology Peptide Cell Biology Cleavage (embryo) digestive system Biochemistry Carboxypeptidase Preprohormone Intestinal mucosa biology.protein Molecular Biology Peptide sequence hormones hormone substitutes and hormone antagonists |
| Zdroj: | Journal of Biological Chemistry. 267:1517-1521 |
| ISSN: | 0021-9258 |
| Popis: | An 83-amino acid cholecystokinin peptide with a sulfated tyrosine and an amidated carboxyl terminus (CCK-83) was purified from human intestinal mucosa. The purified peptide was chemically characterized, and its bioactivity was compared to CCK-8. Several post-translational processing steps such as cleavage at basic residues, sulfation, and amidation are necessary to form biologically active cholecystokinin from its nascent prepropeptide. The discovery of CCK-83 gives new insight into the order of preprohormone processing. The processing of prepro-CCK appears to be in the order of: 1) signal peptidase cleavage, 2) tyrosine sulfation, 3) cleavage after a carboxyl-terminal pair of basic residues, 4) carboxypeptidase B-like cleavage of these basic residues, 5) amidation (which results in the formation of CCK-83), and 6) cleavage at monobasic residues by endopeptidases (which results in the smaller molecular forms of cholecystokinin). The characterization of biologically active CCK-83 with a sulfated tyrosine and an amidated carboxyl terminus establishes the site of signal peptidase action and suggests an order of post-translational modifications that give rise to the various molecular forms of cholecystokinin. |
| Databáze: | OpenAIRE |
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