Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII

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dc.contributor.authorFarias, S L
dc.contributor.authorSabatini, R A
dc.contributor.authorSampaio, T C
dc.contributor.authorHirata, I Y
dc.contributor.authorCezari, M S
dc.contributor.authorJuliano, M A
dc.contributor.authorSturrock, E D
dc.contributor.authorCarmona, A K
dc.contributor.authorJuliano, L
dc.date.accessioned2016-09-05T19:23:00Z
dc.date.available2016-09-05T19:23:00Z
dc.date.issued2006
dc.date.updated2016-09-05T11:55:36Z
dc.description.abstractExtracellular matrix and soluble plasma proteins generate peptides that regulate biological activities such as cell growth, differentiation and migration. Bradykinin, a peptide released from kininogen by kallikreins, stimulates vasodilatation and endothelial cell proliferation. Various classes of substances can potentiate these biological actions of bradykinin. Among them, the best studied are bradykinin potentiating peptides (BPPs) derived from snake venom, which can also strongly inhibit angiotensin I-converting enzyme (ACE) activity. We identified and synthesized sequences resembling BPPs in the vicinity of potential proteolytic cleavage sites in the collagen XVIII molecule, close to endostatin. These peptides were screened as inhibitors of human recombinant wild-type ACE containing two intact functional domains; two full-length ACE mutants containing only a functional C- or N-domain catalytic site; and human testicular ACE, a natural form of the enzyme that only contains the C-domain. The BPP-like peptides inhibited ACE in the micromolar range and interacted preferentially with the C-domain. The proteolytic activity involved in the release of BPP-like peptides was studied in human serum and human umbilical-vein endothelial cells. The presence of enzymes able to release these peptides in blood led us to speculate on a physiological mechanism for the control of ACE activities.en_ZA
dc.identifierhttp://dx.doi.org/10.1515/BC.2006.078
dc.identifier.apacitationFarias, S. L., Sabatini, R. A., Sampaio, T. C., Hirata, I. Y., Cezari, M. S., Juliano, M. A., ... Juliano, L. (2006). Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII. <i>Biological Chemistry</i>, http://hdl.handle.net/11427/21679en_ZA
dc.identifier.chicagocitationFarias, S L, R A Sabatini, T C Sampaio, I Y Hirata, M S Cezari, M A Juliano, E D Sturrock, A K Carmona, and L Juliano "Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII." <i>Biological Chemistry</i> (2006) http://hdl.handle.net/11427/21679en_ZA
dc.identifier.citationFarias, S. L., Sabatini, R. A., Sampaio, T. C., Hirata, I. Y., Cezari, M. H. S., Juliano, M. A., ... & Juliano, L. (2006). Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII. Biological chemistry, 387(5), 611-616.en_ZA
dc.identifier.issn1431-6730en_ZA
dc.identifier.ris TY - Journal Article AU - Farias, S L AU - Sabatini, R A AU - Sampaio, T C AU - Hirata, I Y AU - Cezari, M S AU - Juliano, M A AU - Sturrock, E D AU - Carmona, A K AU - Juliano, L AB - Extracellular matrix and soluble plasma proteins generate peptides that regulate biological activities such as cell growth, differentiation and migration. Bradykinin, a peptide released from kininogen by kallikreins, stimulates vasodilatation and endothelial cell proliferation. Various classes of substances can potentiate these biological actions of bradykinin. Among them, the best studied are bradykinin potentiating peptides (BPPs) derived from snake venom, which can also strongly inhibit angiotensin I-converting enzyme (ACE) activity. We identified and synthesized sequences resembling BPPs in the vicinity of potential proteolytic cleavage sites in the collagen XVIII molecule, close to endostatin. These peptides were screened as inhibitors of human recombinant wild-type ACE containing two intact functional domains; two full-length ACE mutants containing only a functional C- or N-domain catalytic site; and human testicular ACE, a natural form of the enzyme that only contains the C-domain. The BPP-like peptides inhibited ACE in the micromolar range and interacted preferentially with the C-domain. The proteolytic activity involved in the release of BPP-like peptides was studied in human serum and human umbilical-vein endothelial cells. The presence of enzymes able to release these peptides in blood led us to speculate on a physiological mechanism for the control of ACE activities. DA - 2006 DB - OpenUCT DP - University of Cape Town J1 - Biological Chemistry LK - https://open.uct.ac.za PB - University of Cape Town PY - 2006 SM - 1431-6730 T1 - Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII TI - Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII UR - http://hdl.handle.net/11427/21679 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/21679
dc.identifier.vancouvercitationFarias SL, Sabatini RA, Sampaio TC, Hirata IY, Cezari MS, Juliano MA, et al. Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII. Biological Chemistry. 2006; http://hdl.handle.net/11427/21679.en_ZA
dc.languageengen_ZA
dc.publisherDe Gruyteren_ZA
dc.publisher.institutionUniversity of Cape Town
dc.sourceBiological Chemistryen_ZA
dc.source.urihttp://www.degruyter.com/view/j/bchm
dc.subject.otherACE inhibitors
dc.subject.otherangiogenesis
dc.subject.otherbradykinin potentiating peptides
dc.subject.otherendostatin
dc.titleAngiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIIIen_ZA
dc.typeJournal Articleen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceArticleen_ZA
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