Attenuation of renovascular damage in Zucker diabetic fatty rat by NWT-03, an egg protein hydrolysate with ACE- and DPP4-inhibitory Activity

PLoS One. 2012;7(10):e46781. doi: 10.1371/journal.pone.0046781. Epub 2012 Oct 10.

Abstract

Background: Dipeptidyl peptidase 4 (DPP4) and angiotensin-converting enzyme (ACE) are important target enzymes in glycemic control and renovascular protection. Here, we studied the effect of NWT-03, an egg protein hydrolysate with DPP4- and ACE-inhibitory activity, on renovascular damage in Zucker diabetic fatty (ZDF) rats. Comparisons were made to rats treated with vildagliptin (VIL), included as a positive control for the effect of DPP4 inhibition.

Methods: ZDF rats received NWT-03 (1 g/kg/day) or VIL (3 mg/kg/day) from 10 to 25 weeks of age. Metabolic and renal functions were assessed; the kidney was removed for histological analysis of glomerulosclerosis and expression of pro-inflammatory/fibrotic markers (RT-PCR and Western blotting); and the aorta was removed for studies of endothelium-dependent relaxation (EDR).

Findings: Hyperinsulinemic ZDF rats typically developed signs of type-2 diabetes and renovascular damage, as evidenced by albuminuria, glomerulosclerosis, and impaired EDR. Neither NWT-03 nor VIL improved metabolic parameters; for VIL, this was despite a 5-fold increase in glucagon-like peptide (GLP)-1 levels. NWT-03 and VIL both reduced renal interleukin (Il)-1β/Il-13 mRNA expression and glomerulosclerosis. However, only NWT-03 additionally decreased renal tumor necrosis factor (TNF)-α mRNA and P22(phox) protein expression, reduced albuminuria, and restored aortic EDR. Indomethacin added to the organ bath instantly improved aortic EDR, indicating a role for cyclooxygenase (COX)-derived contractile prostanoids in opposing relaxation in ZDF rats. This indomethacin effect was reduced by NWT-03, but not by VIL, and coincided with decreased renal COX-1/2 protein expression.

Conclusion and interpretation: Long-term supplementation with the egg protein hydrolysate NWT-03 attenuated renovascular damage in this preclinical rat model of type 2 diabetes. A comparison to the DPP4-inhibitor VIL suggests that the effects of NWT-03 were related to both ACE- and DPP4-inhibitory properties. The development of protein hydrolysates with a multiple-targeting strategy may be of benefit to functional food formulations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholine / pharmacology
  • Adamantane / analogs & derivatives
  • Adamantane / pharmacology
  • Angiotensin-Converting Enzyme Inhibitors / pharmacology*
  • Animals
  • Aorta / drug effects
  • Aorta / metabolism
  • Aorta / physiology
  • Blood Pressure / drug effects
  • Blotting, Western
  • Cell Adhesion Molecules / metabolism
  • Diabetes Mellitus, Type 2 / genetics
  • Diabetes Mellitus, Type 2 / metabolism
  • Diabetes Mellitus, Type 2 / prevention & control
  • Dipeptidyl Peptidase 4 / blood
  • Dipeptidyl Peptidase 4 / metabolism
  • Dipeptidyl-Peptidase IV Inhibitors / pharmacology*
  • E-Selectin / genetics
  • Egg Proteins / pharmacology*
  • Endothelium, Vascular / drug effects
  • Endothelium, Vascular / physiology
  • Immunohistochemistry
  • In Vitro Techniques
  • Kidney / drug effects
  • Kidney / metabolism
  • Nitriles / pharmacology
  • Peptidyl-Dipeptidase A / blood
  • Peptidyl-Dipeptidase A / metabolism
  • Prostaglandin-Endoperoxide Synthases / metabolism
  • Protein Hydrolysates / pharmacology*
  • Pyrrolidines / pharmacology
  • Rats
  • Rats, Inbred SHR
  • Rats, Zucker
  • Reverse Transcriptase Polymerase Chain Reaction
  • Vasodilation / drug effects
  • Vasodilator Agents / pharmacology
  • Vildagliptin

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Cell Adhesion Molecules
  • Dipeptidyl-Peptidase IV Inhibitors
  • E-Selectin
  • Egg Proteins
  • Havcr1protein, rat
  • NWT-03
  • Nitriles
  • Protein Hydrolysates
  • Pyrrolidines
  • Vasodilator Agents
  • Prostaglandin-Endoperoxide Synthases
  • Dipeptidyl Peptidase 4
  • Peptidyl-Dipeptidase A
  • Vildagliptin
  • Acetylcholine
  • Adamantane

Grants and funding

This study was supported by Stichting Food & Nutrition Delta and Dutch Ministry of Economic Affairs, and Newtricious BV, Oirlo, The Netherlands. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.