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Open Access Correction

Correction: A smallest 6 kda metalloprotease, mini-matrilysin, in living world: a revolutionary conserved zinc-dependent proteolytic domain- helix-loop-helix catalytic zinc binding domain (ZBD)

Wei-Hsuan Yu1*, Po-Tsang Huang12, Kuo-Long Lou1234, Shuan-Su C Yu1 and Chen Lin1

Author Affiliations

1 Institute of Biochemistry and Molecular Biology, National Taiwan University, College of Medicine, Ren-Ai Road, Taipei, Taiwan

2 Graduate Institute of Oral Biology, National Taiwan University, College of Medicine, Ren-Ai Road, Taipei, Taiwan

3 NTU-DRCP Lectures and Core for Membrane Proteins, Center for Biotechnology, National Taiwan University, Chang Sing Street, Taipei, Taiwan

4 Institute of Biotechnology, National Taiwan University, Chang Sing Street, Taipei, Taiwan

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Journal of Biomedical Science 2012, 19:87  doi:10.1186/1423-0127-19-87


The electronic version of this article is the complete one and can be found online at: http://www.jbiomedsci.com/content/19/1/87


Received:17 September 2012
Accepted:24 September 2012
Published:6 October 2012

© 2012 Yu et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Correction

There is a major mistake in the order of Figure 5 to Figure 7 in [1]. We replce the Figure 5 and Figure 6 in [1] with new corrected Figures of Figure 1 and Figure 2. We also replace the correct original order of Figure 6 and Figure 7 in [1] with Figure 2 and Figure 3 in this correction. Sorry for the inconveniences!

thumbnailFigure 1. Combination of 0.05% Triton and 0.2 mg/ml heparin give the optimal refolding activities to cleave the synthetic coumarin-labelled peptide substrate, Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2. Panel A: Shows the refolded ZBD activities increased in dose-dependent manner. In the absence of the refolding accessory factors, Triton X-100 and heparin. The significant reduced activities in the high-concentration (> 100 μg/ml) was observed which could be due to autolysis. Panel B: Under 37°C incubation for 18 hours, Triton X-100 and heparin can prevent the activity loss. (All experiments were repeated at two batch of purification and refolding preparation and data collected from a representative experiments)

thumbnailFigure 2. The polymerization of the 6 kDa ZBD of MMP-7 in pentomer and Octmer demonstrate the significant proteolytic activities towards to the CM-transferrin substrate in CM-transferrin zymographic assay. 300 μg of craboxylmethylated transferrin (CM-transferrin) was co-polymerized with SDS-PAGE as a substrate gel for analyzing the MMP-7 activities in situ

thumbnailFigure 3. Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 assay for characterization of refolded ZBD. Panel A: Under the optimized conditions, the refolded ZBD shows increasing enzymatic activity in dose-dependent manner. No significant activity loss was found in the high concentration situation. Panel B: approximately 6 ng/ml refolded ZBD shows the increasing activity during the time course study and no significant activity loss during overnight incubation. Panel C: Recombinant ZBD can be inhibited by 10 nM EDTA, 1 mM CoCl2 and synthetic inhibitors, 50 nM BB94 & SC44463 and CoCl2, but not b6 250 nM Phosphoramidon. (All experiments were repeated at two batch of purification and refolding preparation and data collected from a representative experiments)

References

  1. Yu WH, Huang PT, Lou KL, Yu SS, Lin C: A Smallest 6 kDa Metalloprotease, Mini-matrilysin, in Living World: a Revolutionary Conserved Zinc-Dependent Proteolytic Domain- Helix-Loop-Helix Catalytic Zinc Binding Domain (ZBD).

    J Biomed Sci 2012, 19:54. PubMed Abstract | BioMed Central Full Text | PubMed Central Full Text OpenURL