BRADYKININ-POTENTIANTING PEPTIDES PRECURSOR FROM Crotalus durissus terrificus VENOM GLAND

Lameu, C., Baptista, G.R., Barbosa, S.R., Yamane, T., Camargo, A.C.M., Hayashi, M.A.F.

The bradykinin-potentiating peptides (BPPs) were the first naturally occurring ACE inhibitors described. Characteristically in Bothrops jararaca, they contain 5 to 13 amino acid residues that have a pyroglutamyl residue at the N-terminal and a proline at the C-terminal. Six BPPs isoforms were identified in a single precursor isolated from a Bothrops jararaca venom gland. This precursor encodes, not only seven BPPs isoforms aligned in tandem but, surprisingly, it also contains the sequence of a 22 amino acid residues C-type natriuretic peptide (CNP) at the C-terminus of the molecule (Murayama et al., PNAS, 1997). Except for one, the pentapeptide BPP-Va, all the other BPPs identified share similar features including a high content of proline residues and the tripeptideIle-Pro-Pro at the C-terminus. Several BPPs precursors isolated from the venom gland of other members belonging to Crotalinae subfamily has been described. Despite the differences observed in the BPPs coding region, all isolated precursors contain tandemly repeated BPPs at the N-terminus and a CNP at the C-terminus. The present study reports the isolation of a cDNA encoding a BPP precursor from the venom gland of another serpent belonging to Crotalinae subfamily Crotalus durissus terrificus. Northern blot and primary sequence analysis allowed us to observe unique features of the BPP-CNP precursor expressed in this specimen.

Financial supported by: FAPESP.

CORRESPONDENCE TO:

Claudiana Lameu, Rua Alberto Cortez, 180, Km 18, Osasco, SP, CEP: 06114-100, Brasil, Email: claulameu@hotmail.com