Since August 2013:

 

 

 

Prof. Dr. rer. nat.
Salah Amasheh
Institute of Veterinary Physiology
Freie Universitšt Berlin
Oertzenweg 19b, Hs. 11
14163 Berlin, Germany
 
e-mail
phone
FAX
 
 salah.amasheh@fu-berlin.de 
 (030) 838-62602
 (030) 838-62610
 Personal Website
 
Research topics

Publications

Grants German Research Foundation (DFG)

2005 - 2007 Fromm, Amasheh DFG Research Grant (FR 652/4-3) "Regulation and function of tight junction und channel proteins in the colon"
2006 - 2009 Amasheh,
Fromm

Project 1 "Characterization of tight junction proteins as barrier or channel formers", in:
DFG Research Unit 721 (FOR 721/1) "Molecular structure and function of the tight junction"

2009 - 2012 Aust, Amasheh,
Fromm

DFG Research Grant (AU 132/7-1 and AM 141/4-1) "Meaning of CD97 in experimental colitis and ulcerative colitis: functional characterization of the molecule in intestinal epithelial cells"

2010 - 2012 Fromm, Amasheh

Project 1 "Characterization of tight junction proteins as barrier or channel formers", in:
DFG Research Unit 721 (FOR 721/2) "Molecular structure and function of the tight junction"

 2011 - 2012 Amasheh DFG Grant (AM 141/5-1), program Initiation and enhancement of bilateral cooperation. Joint project and mutual research stays of Prof. A. Markov, St. Peterburg, Russia, in Berlin and of S. Amasheh in St. Petersburg

CV

1990 - 1996 Study of Biology, Justus-Liebig-Universitšt Giessen
1995 - 1996 Diploma thesis, Institute of Animal Physiology, Justus-Liebig-Universitšt Giessen: "Studies on endogenous and expressed transporters in oocytes of Xenopus laevis"
06.1996 - 08.1998 Doctoral fellow, H. Wilhelm Schaumann-Stiftung
1998 PhD doctoral thesis, supervision Prof. Dr. Wolfgang Clauss, Institute of Animal Physiology, Justus-Liebig-Universitšt Giessen.
"Studies on the endogenous Cl- channel CaIC and the expressed H+/peptide transporters PepT1 and PepT2 in Xenopus laevis oocytes"
10.1998 - 10.2002  Postdoc Fellow, DFG, Inst. of Clinical Physiology, Fromm group
2001 Research award of the Medical Faculty of the FU Berlin, 1st prize, non-clinical institutions: 
"Claudin-2 determines cation permeability of epithelial tight junctions"
since 11.2002 Senior Researcher, Inst. of Clinical Physiology, Charitť, Campus Benjamin Franklin, Berlin
since 2004 Coordinating Teaching Officer of the Institute of Clinical Physiology
2007 Elected for "Personal research boost 2007", 100 T$ for 2 y
21.04.08  Habilitation for "Privatdozent"
since 2012 Member of the permanent MD/PhD examination panel of the Charitť
01.08.13 Tenured Professor, Institute of Veterinary Physiology, FU Berlin

Other research topics

In previous work, the cloned mammalian H+/peptide transporters, PepT1 and PepT2, and the Ca2+-inactivated Cl- channel CaIC were analysed electrophysiologically employing the voltage clamp technique on oocytes of the African clawed toad Xenopus laevis:

Peptide transporters PepT1 and PepT2

@ Prof. Hannelore Daniel, Dept. Physiology of Nutrition, TU Munich, Weihenstephan

Primarily, PepT1 and PepT2 were characterized functionally. These experiments focused on transport of differently charged dipeptides in order to represent the vast number of possible substrates. Major differences of substrate affinities, pH- and potential dependence of transport were detected electrophysiologically.

Based on the results of the comparative electrophysiological characterisation of PepT1 and PepT2, structure-function relationships were investigated using the chimeric approach. In this series of experiments, the first 90 amino acids of the N-terminal region have been shown to be responsible for substrate recognition. Furthermore, an uncoupling of transport characteristics was achieved.

Both transporters displayed electrogenic transport of delta-aminolevulinic acid. This porphyrin precursor is used in the photodynamic therapy of tumors and does not contain a peptide bond. In further experiments, the minimal structural requirements of substrate molecules were investigated. Experiments perfusing a series of different fatty acid molecules showed that amino-fatty acids of a molecular length between 500 and 630 pm satisfy the structural requirements of peptide transporters.

The Ca2+-inactivated Cl- channel CalC

@ Prof. Dr. Wolf-Michael Weber, present address: Institute of Animal Physiology, Electrophysiology and Molecular Biology Lab, University Muenster 

Basic requirement for the use of Xenopus laevis oocytes as an expression system is the knowledge of transport systems already present in the oocyte membrane. The Ca2+-inactivated Cl- channel CaIC endogenous to the oocyte membrane possesses characteristics unique among Xenopus laevis channel proteins. The following publications in part focus on inhibitors potentially important during expression experiments. Furthermore pH dependence and signal transduction was analysed.