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Biochem Biophys Res Commun. 1998 May 29;246(3):719-24.

Cathepsin D is a good candidate for the specific release of a stable hemorphin from hemoglobin in vivo: VV-hemorphin-7.

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Laboratoire de Génie Protéique et Cellulaire, Pôle Sciences et Technique, La Rochelle, France.


Hemorphin peptides, issued from hemoglobin, are emerging as endogenous bioactive peptides derived from in vivo tissular degradation of hemoglobin. In order to find the enzymes which could be implicated in the in vivo release of these peptides, the major lysosomal enzyme cathepsin D was selected, and a study of its activity towards hemoglobin and hemorphins was performed. In this paper, it is shown that according to the primary specificity of cathepsin D towards hemoglobin, this enzyme could constitute a good candidate for the in vivo release of two hemorphins: LVV-hemorphin-7 and VV-hemorphin-7. Moreover, these products, especially VV-hemorphin-7, are resistant to an extended cleavage by the enzyme. Although LVV-hemorphin-7 exhibits a lower resistance, an extended incubation with cathepsin D led to the release of the stable peptide VV-hemorphin-7.

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