Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

Online
ISSN
1437-4315
See all formats and pricing
More options …
Volume 387, Issue 5

Issues

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

Shirley L. Farias
  • Departamento de Biofísica, Escola Paulista de Medicina, Universidade Federal de São Paulo, 04044-020 São Paulo SP, Brazil
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Regiane A. Sabatini
  • Departamento de Biofísica, Escola Paulista de Medicina, Universidade Federal de São Paulo, 04044-020 São Paulo SP, Brazil
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Tatiana C. Sampaio
  • Department of Histology and Embryology, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, 21940-590 Rio de Janeiro RJ, Brazil
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Izaura Y. Hirata
  • Departamento de Biofísica, Escola Paulista de Medicina, Universidade Federal de São Paulo, 04044-020 São Paulo SP, Brazil
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Maria Helena S. Cezari
  • Departamento de Biofísica, Escola Paulista de Medicina, Universidade Federal de São Paulo, 04044-020 São Paulo SP, Brazil
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Maria A. Juliano
  • Departamento de Biofísica, Escola Paulista de Medicina, Universidade Federal de São Paulo, 04044-020 São Paulo SP, Brazil
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Edward D. Sturrock
  • Division of Medical Biochemistry, Faculty of Health Sciences, University of Cape Town, 7925 Cape Town, South Africa
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Adriana K. Carmona
  • Departamento de Biofísica, Escola Paulista de Medicina, Universidade Federal de São Paulo, 04044-020 São Paulo SP, Brazil
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Luiz Juliano
  • Departamento de Biofísica, Escola Paulista de Medicina, Universidade Federal de São Paulo, 04044-020 São Paulo SP, Brazil
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-06-01 | DOI: https://doi.org/10.1515/BC.2006.078

Abstract

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.

Keywords: ACE inhibitors; angiogenesis; bradykinin potentiating peptides; endostatin

About the article

Corresponding author


Received: December 19, 2005

Accepted: March 9, 2006

Published Online: 2006-06-01

Published in Print: 2006-05-01


Citation Information: Biological Chemistry, Volume 387, Issue 5, Pages 611–616, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.078.

Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Muneyoshi Okada, Keisuke Imoto, Akira Sugiyama, Jumpei Yasuda, and Hideyuki Yamawaki
Biological & Pharmaceutical Bulletin, 2017, Volume 40, Number 12, Page 2050
[2]
Florian Veillard, Ahlame Saidi, Roberta E. Burden, Christopher J. Scott, Ludovic Gillet, Fabien Lecaille, and Gilles Lalmanach
Journal of Biological Chemistry, 2011, Volume 286, Number 43, Page 37158
[3]
Carlos Alberto-Silva, Joyce M. Gilio, Fernanda C. V. Portaro, Samyr M. Querobino, and Antonio C. M. Camargo
Journal of Venomous Animals and Toxins including Tropical Diseases, 2015, Volume 21, Number 1
[4]
Carlos A. Silva, Danielle A. Ianzer, Fernanda C.V. Portaro, Katsuhiro Konno, Marcella Faria, Beatriz L. Fernandes, and Antonio C.M. Camargo
Toxicon, 2008, Volume 52, Number 3, Page 501
[5]
Fang Hong, Luo Ming, Sheng Yi, Li Zhanxia, Wu Yongquan, and Liu Chi
Peptides, 2008, Volume 29, Number 6, Page 1062

Comments (0)

Please log in or register to comment.
Log in