In vitro ACE-inhibitory peptide KGYGGVSLPEW facilitates noradrenaline release from sympathetic nerve terminals: relationship with the lack of antihypertensive effect on spontaneous hypertensive rats

Cláudia Marques, Maria Manuela Amorim, Joana Odila Pereira, Luísa Guardão, Maria João Martins, Manuela Estevez Pintado, Daniel Moura, Conceição Calhau, Hélder Pinheiro*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

This study aimed to validate the antihypertensive activity of the angiotensin-converting enzyme (ACE)-inhibitor whey protein hydrolysate (WPH) obtained through the action of proteolytic enzymes from Cynara Cardunculus. The antihypertensive activity of WPH fractions containing peptides with molecular weight below 3 kDa (Whey < 3 kDa) and 1 kDa (Whey < 1 kDa) along with the antihypertensive activity of three potent ACE-inhibitory peptide sequences (DKVGINYW, DAQSAPLRVY and KGYGGVSLPEW), previously identified in WPH, were also investigated. In parallel, the influence of KGYGGVSLPEW (the most potent ACE-inhibitory peptide sequence) on AT1 receptors (a common pharmacological target of antihypertensive therapies beyond ACE), was evaluated. The effect of WPH and fractions (300 mg/kg) and peptide sequences (5 mg/kg) on systolic, diastolic and mean blood pressure was evaluated by telemetry on spontaneously hypertensive rats (SHR), after single oral administration. Despite their ACE-inhibitory effect in vitro, neither WPH, Whey <3 kDa, Whey <1 kDa or peptide sequences exhibited antihypertensive activity. In addition, KGYGGVSLPEW was not only devoid of AT1 receptor antagonism but, on the contrary, had a similar effect to that of Ang II by facilitating the noradrenaline release from sympathetic nerve terminals. In vitro ACE blockade does not always correlate with antihypertensive activity and food-derived peptides cannot be classified as antihypertensive agents based exclusively on in vitro assays. The absence of an antihypertensive effect may also be a result of the interaction of these compounds with other components of the systems involved in the blood pressure control.
Original languageEnglish
Article number69495
Pages (from-to)72-76
Number of pages5
JournalPeptides
Volume71
DOIs
Publication statusPublished - 17 Jul 2015

Keywords

  • Angiotensin-converting enzyme
  • Antihypertensive
  • Bioactive peptides
  • Hypertension
  • Mechanisms of action
  • Whey

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