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Antihypertensive effects of lactoferrin hydrolyzates: Inhibition of angiotensin- and endothelin-converting enzymes

AutorFernández-Musoles, Ricardo ; Salom, Juan B.; Martínez-Maqueda, D. ; López Díez, José Javier ; Recio, Isidra ; Manzanares, Paloma
Palabras claveLactoferrin hydrolyzates
ECE-dependent vasoconstriction
ACE-dependent vasoconstriction
Renin–angiotensin system
Endothelin system
Vasopeptidase inhibitors
Fecha de publicación2013
CitaciónFood Chemistry 139(1-4): 994-1000 (2013)
ResumenThe potential of bovine lactoferrin (LF) as a source of antihypertensive peptides acting on the renin-angiotensin system (RAS) and the endothelin (ET) system as dual vasopeptidase inhibitors has been examined. For this purpose enzymatic LF hydrolyzates (LFHs) were generated by trypsin and proteinase K digestions. Permeate fractions with molecular masses lower than 3 kDa (LFH <3 kDa) were orally administered to spontaneously hypertensive rats (SHRs). Although both LFHs <3 kDa showed in vitro angiotensin I-converting enzyme (ACE)-inhibitory activity, only proteinase K LFH <3 kDa exerted an in vivo antihypertensive effect. The proteinase K LFH <3 kDa and a previously characterized pepsin LFH <3 kDa with ACE-inhibitory and antihypertensive effects were tested in ex vivo functional assays as inhibitors of ACE-dependent vasoconstriction. Pepsin LFH <3 kDa but not proteinase K LFH <3 kDa inhibited ACE-dependent vasoconstriction. When tested as inhibitors towards endothelin-converting enzyme (ECE), both LFHs <3 kDa exerted in vitro inhibitory effects on ECE activity and inhibited ECE-dependent vasoconstriction. Most abundant peptides in proteinase K LFH <3 kDa were identified by using an ion trap mass spectrometer. Based on peptide abundance, two peptides (GILRPY and REPYFGY) were chemically synthesized and their ECE-inhibitory activity was tested. Both exerted in vitro inhibitory effects on ECE activity. In conclusion, orally effective antihypertensive LFHs <3 kDa may act as dual vasopeptidase (ACE/ECE) or as single ECE inhibitors with different antivasoconstrictor effects depending on the protease used to release bioactive peptide sequences. © 2013 Elsevier Ltd. All rights reserved.
URIhttp://hdl.handle.net/10261/99738
DOI10.1016/j.foodchem.2012.12.049
Identificadoresdoi: 10.1016/j.foodchem.2012.12.049
issn: 0308-8146
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