Difference of activation processes and structure of activation peptides in human pepsinogens A and progastricsin

Journal of Biochemistry
T KageyamaK Takahashi

Abstract

The activation processes of two human pepsinogens A (pepsinogens 3 and 5) and progastricsin were compared with special attention to pepsinogens 3 and 5. Each zymogen was converted to pepsin in a stepwise manner through intermediate forms. In pepsinogens A, the major cleavage site was the Leu23-Lys24 bond and this cleavage was suggested to occur intramolecularly. When each of the pepsins A was added to the corresponding pepsinogen A exogenously, the latter was rapidly converted to pepsin, releasing the 47-residue intact activation segment. In this case, the Leu47-Val48 bond connecting the activation segment with the pepsin moiety was cleaved by an intermolecular reaction. On the other hand, when the pepsinogen A-pepstatin complex was attacked by each corresponding pepsin A added exogenously, significant cleavage by an intermolecular reaction occurred at the Asp25-Phe26 bond, generating the Phe26-intermediate form. These shifts of the cleavage sites in pepsinogens A depending on the activation conditions are likely to correlate with the conformation of the activation segment. These results can be explained consistently in terms of a proposed molecular model of activation.

Citations

Sep 20, 2005·Biomedical Papers of the Medical Faculty of the University Palacký, Olomouc, Czechoslovakia·Martin Fusek, Václav Vetvicka
Feb 1, 1995·Protein Science : a Publication of the Protein Society·X LinJ Tang
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Oct 7, 2005·Biological Chemistry·Matilde-Esther FuentesEdelmira Valero
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Apr 8, 2006·Protein Expression and Purification·Ajamaluddin MalikBrigitte Söhling
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