These authors contributed equally to this work.
Functional proteomics reveals the protective effects of saffron ethanolic extract on hepatic ischemia-reperfusion injury
Article first published online: 8 JUL 2013
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Volume 13, Issue 15, pages 2297–2311, August 2013
How to Cite
Pan, T.-L., Wu, T.-H., Wang, P.-W., Leu, Y.-L., Sintupisut, N., Huang, C.-H., Chang, F.-R. and Wu, Y.-C. (2013), Functional proteomics reveals the protective effects of saffron ethanolic extract on hepatic ischemia-reperfusion injury. Proteomics, 13: 2297–2311. doi: 10.1002/pmic.201200551
Colour Online: See the article online to view Figs. 1–7 in colour.
- Issue published online: 2 AUG 2013
- Article first published online: 8 JUL 2013
- Accepted manuscript online: 21 MAY 2013 04:06AM EST
- Manuscript Accepted: 10 APR 2013
- Manuscript Revised: 31 MAR 2013
- Manuscript Received: 4 DEC 2012
- National Science Research Grant of Taiwan. Grant Number: NSC-99-2320-B-182-015-MY3
- Chang Gung University. Grant Number: EMRPD1B0361
- Chang Gung Memorial Hospital. Grant Number: CMRPD1B0401
As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors.
Figure S1. LC-UV chromatogram of saffron. Mobile phase of buffer A: 1% acetic acid-water and buffer B: 1% acetic acid-acetonitrile. The initial condition was set at 10% of B, grading up to 20% in 15 min, up to 20% at 20 min and up to 40% at 50 min. Detection wavelength was 310 nm. Oven temperature was 30°C and flow rate was 0.5 mL/min. The chemical structures of marked peaks are illustrated.
Figure S2. Validation of p47 translocation via immunohistochemical study. The positive signal was presented as brown color and indicated by arrows. Original magnification: 400x
Figure S3. MALDI-TOF spectra of spot 5 was matched the rat SOD1 protein from the Swiss-Prot database (2012_05). The parent ions m/z 1367.7710 was selected for further analysis by an Ultraflex™ MS/MS operated in the LIFT mode using FlexControl™ software. A sequence was confirmed from the labeled b- and y-ions in the spectrum.
Figure S4. Biological network analyses of differentially expressed proteins using MetaCore™ mapping tools. Nodes represent proteins and lines between the nodes indicate direct protein–protein interactions. The related biologic processes in this network are mainly involved in ER stress and the ubiquitin-proteasome system. The various proteins on this map are indicated by different symbols representing the functional class of the proteins.