A pinboard by
Faezeh Shekari

Researcher, Royan institute


Cell membrane acts like a country toll, give entry/exit permission or receive/send messages to the surrounding environment. The tools of cell membrane to accomplish its responsibilities are proteins. These proteins can be regarded as biomarker so one of the mission of membrane proteomics is finding new biomarkers can be used in clinics. However, as noted by Thierry Rabilloud, Love is possible but so difficult. I have worked on membrane proteomics for more than 9 years since I was MSc student. Moreover, I have been involved in two international Human Proteome Organization initiatives on membrane proteomics. In one of these initiatives, I have prepared standard membrane samples for other countries including Australia, South Korea, China, Japan and Singapore in collaboration with Academia Sinica (Taiwan) and Royan institute (Iran). My PhD thesis was also about organellar proteomics.
In recent years, it has been shown that cells communicate each other by sending some kind of packages name vesicles surrounded by membrane. These packages can be easily find in blood, urine, etc. and providing attractive sources for membrane proteomics specially people loving biomarker discovery. After completion of my PhD, Prof. Baharvand (director of Royan Institute for Stem Cell Biology and Technology) asked me to focus on these vesicles because my previous experiences on membrane isolation and proteomic characterizations. Now, I am trying to establish extracellular vesicle group in Royan institute working on both therapeutic applications and biomarker discovery of extracellular vesicles.


Identification of cytoplasmic and membrane-associated complexes in human embryonic stem cells using blue native PAGE.

Abstract: Human embryonic stem cells (hESCs) have great potential for use in developmental biology studies, functional genomics applications, drug screening, and regenerative medicine. A detailed understanding of the molecular mechanisms that are responsible for maintaining the undifferentiated and pluripotent nature of hESCs is essential for their effective therapeutic application. It has become evident that many complex cellular processes are carried out by assemblies of protein molecules (protein complexes). Blue native polyacrylamide gel electrophoresis (BN-PAGE) has been used to separate protein complexes from whole cell lysates. Using BN-PAGE, we resolved cytoplasmic and membrane-associated complexes from hESCs and characterised their composition, stoichiometry, and dynamics by denaturing SDS-PAGE. The reliability of the fractionation was examined by western blot analysis of membrane and cytosolic markers. MALDI TOF/TOF mass spectrometry identified 119 cytosolic and 69 membrane proteins from the BN-PAGE proteome maps. Potential protein complexes were validated by computational prediction of possible protein-protein interactions using the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) database. Based on BN-PAGE gels and validation by databases, 82 heteromultimeric and 47 homomultimeric protein complexes have been found in hESCs. Resolving some of the protein complexes provided insight into the function of previously uncharacterised complexes in hESCs.

Pub.: 06 Jul '11, Pinned: 29 Jul '17