Key result
A synthetic 11-amino acid peptide spanning the human prorenin processing site was specifically cleaved by trypsin at the authentic processing site, while other enzymes cleaved at alternate sites.
A synthetic 11-amino acid peptide can be used as a specific assay to study human prorenin activation by different proteases.
This peptide assay may enable targeted prorenin research; leaves open translation to human hypertension or clinical use.
Human renin is synthesized as an inactive zymogen (prorenin) which is processed to the active form. We synthesized an 11-amino acid peptide which spans the human prorenin processing site in order to develop a simple assay to study human prorenin activation. Six enzymes which are capable of activating recombinant prorenin in vitro were studied. Four of these enzymes digested the synthetic peptide in a specific fashion, as analyzed by reverse-phase high-performance liquid chromatography. Amino acid analysis of the purified digestion products revealed that trypsin cleaves between Arg-Leu, the authentic processing site, while kallikrein, plasmin and elastase all cleaved at alternate sites. On the other hand, pepsin and cathepsin D did not cleave this substrate, suggesting that the activation of prorenin by these proteases might occur at a site distinct from the authentic processing site. Our data suggest that this synthetic peptide may be used as a simple and specific assay for prorenin activation.
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Dubin et al. (1991) studied this question. Synthetic 11-amino acid peptide substrate was evaluated on Cleavage of synthetic peptide by various enzymes. A synthetic 11-amino acid peptide spanning the human prorenin processing site was specifically cleaved by trypsin at the authentic processing site, while other enzymes cleaved at alternate sites.
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