Session 39 I. Politis Agricultural University of Athens
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1 Session 39 I. Politis Agricultural University of Athens
2 Opioid Antihypertensive Antithrombotic Immunoregulatory Enhancement or Suppression?
3
4 Origin of immunoregulatory peptides derived from caseins in bovine milk Protein Peptide Immune effect αs1-casein f( ) antibody formation, phagocytosis f(1-23) f(90-96) f(90-95) f(23-34 phagocytic response lymphocyte proliferation, NK cell activity, neutrophil chemotaxis ACE inhibitor, phagocytosis, protective response to Klebsiella pneumoniae infection β-casein f( ) proliferating responses in lymphocytes f(63-68) f( ) antibody formation, phagocytosis antibody formation, phagocytosis, antigen dependent T cell proliferation κ-casein f( ) lymphocyte proliferation f(17-21) f(38-39) antibody formation and phagocytosis in vitro lymphocyte proliferation
5 The β casein story (I) Hydrolytic products Inhibit proliferation of splenic lymphocytes Inhibit proliferation of Peyer s patch cells Inhibit proliferation of human lymphocytes
6 The β casein story (II) Two critical peptides Pro Gly Pro Ile Pro Asn (63-68) Leu Leu Tyr ( ) Promote antibody production Enhance phagocytosis and T-cell proliferation
7 Effect of bovine milk protein peptides on the function of T-cells
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9 Peptides tested Low molecular weight peptide fraction Leu Leu Tyr (tripeptide) Target cells T-cells Parameters IL-2 IFN-γ IL-4
10 1.2 Peptide concentration (mg/ml) Elution time (min)
11 250 CI A214 (mau) CII CIII Elution time (min)
12 In vitro effect of various milk protein peptides on IL-2 secretion by stimulated porcine T-cells. Data are expressed as pgx1000/ml/10 6 cells (six independent experiments) IL-2 (pg x 1000/ml/10 6 cells) Treatment Weaning (w) w + 8 weeks Control 30.2 ± ± 9.7 Fraction III 12.4 ± 4.7* 39.3 ± 6.8 Tripeptide 25.2 ± ± 6.5
13 In vitro effect of various milk protein peptides on IFN-γ secretion by stimulated porcine T-cells. Data are expressed as pg/ml/10 6 cells (six independent experiments) IFN-γ (pg/ml/10 6 cells) Treatment Weaning (w) w + 8 weeks Control 21.8 ± ± 7.8 Fraction III 10.3 ± 4.7* 34.3 ± 5.8* Tripeptide 18.3 ± ± 4.7
14 In vitro effect of various milk protein peptides on IL-4 secretion by stimulated porcine T-cells. Data are expressed as pg/ml/10 6 cells (six independent experiments) IL-4 (pg/ml/10 6 cells) Treatment Weaning (w) w + 8 weeks Control 40.3 ± ± 7.6 Fraction III 18.5 ± 5.6* 45.3 ± 8.4 Tripeptide 35.2 ± ± 7.6
15 Conclusions Low molecular weight (LMW) peptide fraction down-regulated IL-2, IL-4 and IFN-γ production by T-cells at WEANING LMW peptide fraction showed a tendency to upregulate IL-2, IL- 4 and IFN-γ production by T-cells at 8 weeks after weaning Leu Leu Tyr had no effect on cytokine production by T-cells
16 Effects of two milk peptides on the function of porcine macrophages and neutrophils
17 Peptides tested Pro Gly Pro Ile Pro Asn (hexapeptide) Leu Leu Tyr (tripeptide) Target cells Macrophages, Neutrophils Parameters Chemotaxic index U-PA system Superoxide anion
18 Chemotactic Index Treatment Weaning (w) w + 4 weeks Control 2.4 ± ± 0.5 Tripeptide 1.5* ± ± 0.6 Hexapeptide 1.4* ± ± 0.7
19 u-pa (ΔΑ/h) Treatment Weaning (w) w + 4 weeks Control 0.32 ± ± 0.05 Tripeptide 0.16* ± ± 0.07 Hexapeptide 0.22* ± ± 0.07
20 Effect of two peptides (10μΜ) on membranebound u-pa by porcine neutrophiles u-pa (ΔΑ/h) Treatment Weaning (w) w + 4 weeks Control 0.47 ± ± 0.07 Tripeptide 0.23* ± ± 0.08 Hexapeptide 0.34* ± ± 0.09
21 Effect of two peptides (10μΜ) on superoxide anion (SA) production by porcine neutrophils SA (nm/10 6 cells) Treatment Weaning (w) w + 4 weeks Control 2.0 ± ± 0.05 Tripeptide 1.5* ± * ± 0.04 Hexapeptide 1.9 ± * ± 0.05
22 Effect of two peptides (10μΜ) on superoxide anion (SA) production by porcine macrophages SA (nm/10 6 cells) Treatment Weaning (w) w + 4 weeks Control 2.5 ± ± 0.03 Tripeptide 1.2* ± * ± 0.04 Hexapeptide 1.6* ± * ± 0.04
23 Tripeptide and Hexapeptide down-regulated various immune functions at WEANING Chemotactic activity, u-pa production Superoxide production
24 Tripeptide and Hexapeptide increased superoxide production and had no effect on various immune functions at FOUR WEEKS AFTER WEANING
25
26 extracellular signaling molecule αctivated phospholipase C-β PIP2 diacyglycerol activated receptor activated C-kinase endoplasmic reticulum
27 A C T I V A T I O N Cyclic nucleotide gated channels Guaninine exchange protein (Epac-1, Epac-2)
28 u-pa (ΔΑ/h) Treatment Macrophages Neutrophils Control a ± a ± PKA/Epac-1 activator (10μΜ) PKA activator (10 μμ) Εpac-1 activator (10 μμ) b ± b ± b ± b ± a ± a ± 0.030
29 Effect of various camp analogues (10μΜ) on superoxide anion (SA) production SA (nm/10 6 cells) Treatment Macrophages Neutrophils Control a ± a ± PKA/Epac-1 activator (10μΜ) PKA activator (10 μμ) Εpac-1 activator (10 μμ) d ± b ± b ± b ± c ± b ± 0.156
30 Effect of PKA inhibitors on membranebound u-pa u-pa (ΔΑ/h) Treatment Macrophages Neutrophils PMA a ± a ± PMA+tripeptide b ± b ± PMA+tripeptide+H89 (10μΜ) PMA+tripeptide+ΚΤ5720 (10μΜ) PMA+tripeptide +PKI (10μM) PMA+tripeptide+ΗΑ1004 (10μΜ) a ± a ± a ± a ± a ± a ± a ± a ± 0.039
31 Effect of PKA inhibitors on superoxide anion (SA) production SA (nm/10 6 cells) Treatment Macrophages Neutrophils PMA a ± a ± PMA+tripeptide c ± c ± PMA+tripeptide+H89 (10μΜ) PMA+tripeptide+ΚΤ5720 (10μΜ) PMA+tripeptide +PKI (10μM) PMA+tripeptide+ΗΑ1004 (10μΜ) b ± b ± b ± b ± b ± b ± b ± b ± 0.188
32 Conclusions 1. Activation of PKA, but not Epac-1, is responsible for the downregulation of the u- PA system 2. Activation of PKA and/or Epac-1 is responsible for the downregulation of the SA system
33 Effect of two protein kinases on IL-2, IL-4 and IFN-γ production by stimulated T-cells. Data are expressed as pg/ml/10 6 cells (six independent experiments) Treatment IL-2 (x1000) IL-4 IFN-γ Control 32.2 ± 8.3 a 43.3 ± 7.9 a 24.7 ± 5.6 a Fraction III 14.7 ± 5.2 b 20.0 ± 4.7 b 9.8 ± 4.3 b Fraction III +H7 0.8 ± 0.8 c 1 ± 0.8 c 0.6 ± 0.7 c Fraction III +HA ± 6.3 b 23.5 ± 5.7 b 9.6 ± 4.4 b
34 Conclusions Suppresion of T-cell activation is related to inhibition of PKC rather than of PKA
35
36 Affects 25% of the population 22 billion $ per annum (US alone) Increase of 5 mmhg in BP 16% increase in the risk of CVD
37 SBP (mmhg) DBP (mmhg) Normal < 120 < 80 Pre-hypertension < 139 < 90 Stage 1 hypertension < 159 < 99 Stage 2 hypertension
38 Renin- Angiotensin system Kinin-bradykinin system
39 Angiotensin Renin Angiotensin I ACE Angiotensin II Aminopeptidase A Aminopeptidase N Angiotensin III Angiotensin IV
40 Kininogen Kallidin Bradykinin ACE Inactive Fragments
41 Potent casokinin and lactokinin sequences Protein Casokinins Peptide fragment Primary sequence ACE IC 50 (μmol/l) αs1-casein f(25-27) VAP 2.0 αs2-casein f( ) FALPQY 4.3 β-casein f(74-76) IPP 5.0 κ-kasein f( ) VTSTAV 52.0 Lactokinins α-lactoglobulin f( ) WLAHK 77.0 β-lactoglobulin f( ) ALPMHIR 42.6 BSA f( ) ALKAWSVAR 3.0 FitzGerald et al. (2004)
42 Bovine casein-derived peptides displaying hypotensive effects in spontaneously hypertensive rats (I) Peptide Sequence IC 50 (μmol/l) αs1-casein Maximum decrease in SBP (mmhg) f(1-9) RPKHPIKHQ f(23-34) FFVAPFPEVFGK f( ) YVKVPQL f( ) YP f( ) TTMPLW αs2-casein f( ) AMPKPW f( ) MKPWIQPK f( ) TKVIP FitzGerald et al. (2004)
43 Bovine casein-derived peptides displaying hypotensive effects in spontaneously hypertensive rats (II) Peptide Sequence IC 50 (μmol/l) β-casein Maximum decrease in SBP (mmhg) f(59-61) VYP f(59-64) VYPFPG f(60-68) YPFPGPIPN f(74-76) IPP f(80-90) TPVVVPPFLQP f(84-86) VPP f( ) LQSW f( ) KVLPVP f( ) KVLPVPQ f( ) AVPYPQR FitzGerald et al. (2004)
44 mmhg n = 39, Inoue n = 80, Aihara n = 144, Misuno n = 36, Hata n = 20, Kawase JAPAN n = 56, Sano n = 46, Mizushima n = 162, van Mierlo n = 166, de Leeuw n = 275, van der Zander n = 54, Lee n = 134, Engberink NETHERLANDS GERMANY Summary of human studies FINLAND n = 39, Seppo n = 94, Jauhiainen n = 60, Tuomilehto
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46 EFSA conclusions Evidence is insufficient to establish a cause-effect relationship between consumptions of tripeptides VPP and IPP and: Maintenance of normal blood pressure Elastic properties of arteries
47 CONCLUSIONS Antihypertensive effect of milk peptides is still debatable Results concerning bioavailability are not convincing Mechanism of action unknown
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