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2008 | 55 | 2 | 297-305
Article title

Specific inhibition of procollagen C-endopeptidase activity by synthetic peptide with conservative sequence found in chordin

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EN
Abstracts
EN
Procollagen C-endopeptidase (BMP-1) and N-endopeptidase (ADAMTS-2) are key enzymes for correct and efficient conversion of fibrillar procollagens to their self assembling monomers. Thus, they have an essential role in building and controlling the quality of extracellular matrices (ECMs). Here, we tested inhibition of activity of the largest variant of BMP-1, a recombinant mammalian tolloid (mTld), in vitro by three synthetic peptides with conservative amino-acid sequences found in chordin using procollagen type I as a substrate. We also verified the specific action of best inhibitory 16 amino-acid peptide in the procollagen type I cleavage assay with the use of ADAMTS-2 (procollagen N-endopeptidase). Subsequently, we determined the critical residues and minimal sequence of six amino acids in the original 16 amino-acid peptide required to maintain the inhibitory potential. Studies on the interactions of 6 and 16 amino acid long peptides with the enzyme revealed their binding to non-catalytic, regulatory domains of mTld; the inhibitory activity was not due to the competition of peptides with the substrate for the enzyme active center, because mTld did not cleave the peptides. However, in the presence of mTld both peptides underwent cyclization by disulfide bond formation. Concluding, we have shown that procollagen C-endopeptidase may be specifically blocked via its non-catalytic domains by synthetic peptide consisting of 6 amino acids in the sequence found in highly conservative region of chordin. Thus, we hypothesize that the 6 amino-acid peptide could be a good candidate for anti-fibrotic drug development.
Publisher

Year
Volume
55
Issue
2
Pages
297-305
Physical description
Dates
published
2008
received
2008-02-22
revised
2008-04-22
accepted
2008-04-30
(unknown)
2008-06-07
Contributors
author
  • Department of General and Molecular Biology and Genetics, Center of Excellence for Research and Teaching of Molecular Biology of Matrix and Nanotechnology, Silesian Medical University in Katowice, Katowice, Poland
  • Department of General and Molecular Biology and Genetics, Center of Excellence for Research and Teaching of Molecular Biology of Matrix and Nanotechnology, Silesian Medical University in Katowice, Katowice, Poland
author
  • Department of General and Molecular Biology and Genetics, Center of Excellence for Research and Teaching of Molecular Biology of Matrix and Nanotechnology, Silesian Medical University in Katowice, Katowice, Poland
  • Department of General and Molecular Biology and Genetics, Center of Excellence for Research and Teaching of Molecular Biology of Matrix and Nanotechnology, Silesian Medical University in Katowice, Katowice, Poland
  • Department of General and Molecular Biology and Genetics, Center of Excellence for Research and Teaching of Molecular Biology of Matrix and Nanotechnology, Silesian Medical University in Katowice, Katowice, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv55p297kz
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