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The angiotensin converting enzyme inhibitory tripeptides Ile-Pro-Pro and Val-Pro-Pro show increasing permeabilities with increasing physiological relevance of absorption models.
Peptides. 2008 Aug; 29(8):1312-20.P

Abstract

Transepithelial transport of the ACE inhibitory peptides Ile-Pro-Pro and Val-Pro-Pro was studied in different models of absorption. Apparent permeability (P(app)) values for absorptive transport across Caco-2 monolayers were 1.0+/-0.9 x 10(-8) (Ile-Pro-Pro) and 0.5+/-0.1 x 10(-8)cms(-1) (Val-Pro-Pro). Ex vivo transport across jejunal segments in the Ussing chamber was 5-times (Ile-Pro-Pro) to 10-times (Val-Pro-Pro) higher with no significant differences (p>0.05) observed between both peptides. The peptidase inhibitor bestatin increased permeability for the absorptive direction for Ile-Pro-Pro by twofold. Neither a transepithelial pH gradient nor increased apical tripeptide concentration nor longitudinal localization of the intestinal segment influenced P(app) in the ex vivo experiments. Val-Pro-Pro transport across Peyer's patches, however, was 4-times higher (P(app)=21.0+/-9.3 x10(-8)cms(-1)) as compared to duodenum (P(app)=4.8+/-1.4 x 10(-8)cms(-1)). In the in situ perfusion experiments P(app) values varied greatly among different animals ranging from 0.5 to 24.0 x10(-8)cms(-1) (Ile-Pro-Pro) and from 1.0 to 15.6 x 10(-8)cms(-1) (Val-Pro-Pro). In summary, Caco-2 and ex vivo absorption models differ considerably regarding their peptide permeability. The in situ model seems to be less appropriate because of the observed large variability in peptide permeability. The results of this study demonstrate that the ACE inhibitory peptides Ile-Pro-Pro and Val-Pro-Pro are absorbed partially undegraded.

Authors+Show Affiliations

Unilever Food and Health Research Institute, 3133 AT Vlaardingen, The Netherlands. martin.foltz@unilever.comNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

18490081

Citation

Foltz, Martin, et al. "The Angiotensin Converting Enzyme Inhibitory Tripeptides Ile-Pro-Pro and Val-Pro-Pro Show Increasing Permeabilities With Increasing Physiological Relevance of Absorption Models." Peptides, vol. 29, no. 8, 2008, pp. 1312-20.
Foltz M, Cerstiaens A, van Meensel A, et al. The angiotensin converting enzyme inhibitory tripeptides Ile-Pro-Pro and Val-Pro-Pro show increasing permeabilities with increasing physiological relevance of absorption models. Peptides. 2008;29(8):1312-20.
Foltz, M., Cerstiaens, A., van Meensel, A., Mols, R., van der Pijl, P. C., Duchateau, G. S., & Augustijns, P. (2008). The angiotensin converting enzyme inhibitory tripeptides Ile-Pro-Pro and Val-Pro-Pro show increasing permeabilities with increasing physiological relevance of absorption models. Peptides, 29(8), 1312-20. https://doi.org/10.1016/j.peptides.2008.03.021
Foltz M, et al. The Angiotensin Converting Enzyme Inhibitory Tripeptides Ile-Pro-Pro and Val-Pro-Pro Show Increasing Permeabilities With Increasing Physiological Relevance of Absorption Models. Peptides. 2008;29(8):1312-20. PubMed PMID: 18490081.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The angiotensin converting enzyme inhibitory tripeptides Ile-Pro-Pro and Val-Pro-Pro show increasing permeabilities with increasing physiological relevance of absorption models. AU - Foltz,Martin, AU - Cerstiaens,Anja, AU - van Meensel,Ans, AU - Mols,Raf, AU - van der Pijl,Pieter C, AU - Duchateau,Guus S M J E, AU - Augustijns,Patrick, Y1 - 2008/04/08/ PY - 2008/01/25/received PY - 2008/03/27/revised PY - 2008/03/28/accepted PY - 2008/5/21/pubmed PY - 2008/12/17/medline PY - 2008/5/21/entrez SP - 1312 EP - 20 JF - Peptides JO - Peptides VL - 29 IS - 8 N2 - Transepithelial transport of the ACE inhibitory peptides Ile-Pro-Pro and Val-Pro-Pro was studied in different models of absorption. Apparent permeability (P(app)) values for absorptive transport across Caco-2 monolayers were 1.0+/-0.9 x 10(-8) (Ile-Pro-Pro) and 0.5+/-0.1 x 10(-8)cms(-1) (Val-Pro-Pro). Ex vivo transport across jejunal segments in the Ussing chamber was 5-times (Ile-Pro-Pro) to 10-times (Val-Pro-Pro) higher with no significant differences (p>0.05) observed between both peptides. The peptidase inhibitor bestatin increased permeability for the absorptive direction for Ile-Pro-Pro by twofold. Neither a transepithelial pH gradient nor increased apical tripeptide concentration nor longitudinal localization of the intestinal segment influenced P(app) in the ex vivo experiments. Val-Pro-Pro transport across Peyer's patches, however, was 4-times higher (P(app)=21.0+/-9.3 x10(-8)cms(-1)) as compared to duodenum (P(app)=4.8+/-1.4 x 10(-8)cms(-1)). In the in situ perfusion experiments P(app) values varied greatly among different animals ranging from 0.5 to 24.0 x10(-8)cms(-1) (Ile-Pro-Pro) and from 1.0 to 15.6 x 10(-8)cms(-1) (Val-Pro-Pro). In summary, Caco-2 and ex vivo absorption models differ considerably regarding their peptide permeability. The in situ model seems to be less appropriate because of the observed large variability in peptide permeability. The results of this study demonstrate that the ACE inhibitory peptides Ile-Pro-Pro and Val-Pro-Pro are absorbed partially undegraded. SN - 0196-9781 UR - https://www.unboundmedicine.com/medline/citation/18490081/The_angiotensin_converting_enzyme_inhibitory_tripeptides_Ile_Pro_Pro_and_Val_Pro_Pro_show_increasing_permeabilities_with_increasing_physiological_relevance_of_absorption_models_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0196-9781(08)00140-X DB - PRIME DP - Unbound Medicine ER -