Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L

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2004-10-15
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Puzer, L.
Cotrin, S. S.
Alves, MFM
Egborge, T.
Araujo, M. S.
Juliano, M. A.
Juliano, L.
Bromme, D.
Carmona, A. K.
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Cathepsins V and L have high identity and few structural differences. in this paper, we reported a comparative study of the hydrolytic activities of recombinant human cathepsins V and L using fluorescence resonance energy transfer peptides derived from Abz-KLRSSKQ-EDDnp (Abz = ortho-aminobenzoic acid and EDDnp = N-(2,4-dinitrophenyl)ethylenediamine). Five series of peptides were synthesized to map the S-3 to S'(2) subsites. the cathepsin V subsites S-1 and S-3 present a broad specificity while cathepsin L has preference for positively charged residues. the S-2 subsites of both enzymes require hydrophobic residues with preference for Phe and Leu. the S-1' and S-2' subsites of cathepsins V and L are less specific. Based on these data we designed substrates to explore the electrostatic potential differences of them. Finally, the kininogenase activities of these cathepsins were compared using synthetic human kininogen fragments. Cathepsin V preferentially released Lys-bradykinin while cathepsin L released bradykinin. This kininogenase activity by cathepsins V and L was also observed from human high and low molecular weight kininogens. (C) 2004 Elsevier Inc. All rights reserved.
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Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 430, n. 2, p. 274-283, 2004.