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Publikationsserver der RWTH Aachen University

Mechanismen des vermittelten und nicht-vermittelten Transportes einer amphiphilen Phosphonat-Sonde (NDP2) in der Erythrozytenmembran

Abstract

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This dissertation concerns itself with the transversal (re-)orientation of the long-chained anionic amphiphile NDP2 [10-(Naphth-1yl)-1-decane phosphonic acid]as a probe within the two leaves of the erythrocyte membrane. The overwhelming – mediated – part of this translocation takes place via the membrane protein AE1(Band 3), which was originally known as a transport protein for small hydrophilic anions (e.g. chloride -ions) and the characteristics of which as a transport agent for long-chain amphiphiles is at the centre of these investigations. The starting point was problems that had occurred in the context of studies carried out with the previous probe NDP1 [10-(Naphth-1yl)-1-decane phosphoric acid]. This is subject to an intracellular hydrolysis due to its phosphatester group. The difficulties arising from this when measuring the inwards and outwards translocation (flip and flop) within the erythrocyte membrane were overcome using the newly synthesised phosphonate probe NDP2 developed by Dr. E. Bremen, as this is not subject to any hydrolysis. Additionally, interest was focussed upon the comparison between the two different phospho-probes NDP1 und NDP2, in order to gain further information regarding the natural laws governing the translocation of long-chain amphiphiles in the erythrocyte membrane. The results testify to a far-reaching agreement of the translocation characteristics of the two probes NDP2 and NDP1. It can be demonstrated that the flip of NDP2 is inhibited by certain substances (e.g. 4,4´-diisothiocyanostilben-2,2´-disulfonic acid; DIDS) which are known as adverse substances of the AE1-mediated transport of small anions and the inhibiting effects of which upon the flip of other long-chain amphiphiles via AE1 for other probes (e.g. NDP1) have already been proven. Moreover, amongst other things, the influence of the stationary distribution and the kinetics of the inwards translocation of NDP2 through the incorporation of other substances – so-called membrane modifiers – into the membrane, through the alteration of the electrolyte composition and the pH-value of the incubation medium, as well as the addition of bivalent metal ions have also been investigated. Additionally the till now unknown inhibiting effect of DIDS (cf. above) upon an intrinsic transport protein, the so-called scramblase, was proven.

Degree

thesis:*
Grantor dc:publisher
Publikationsserver der RWTH Aachen University
Year dc:date
2007

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Sieberg, Thorsten Oliver
Contributors dc:contributor
  • Deuticke, Bernhard

Subjects

dc:subject × 9

Rights

dc:rights
Statement dc:rights
  • info:eu-repo/semantics/openAccess
Language dc:language
ger

Identifiers

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Chain of custody

source
Harvested from
RWTH Aachen University
Base URL
publications.rwth-aachen.de/oai2d
Last updated
2026-07-30
Source record
OAI-PMH GetRecord
citation

Sieberg, Thorsten Oliver. Mechanismen des vermittelten und nicht-vermittelten Transportes einer amphiphilen Phosphonat-Sonde (NDP2) in der Erythrozytenmembran. Publikationsserver der RWTH Aachen University, 2007. https://publications.rwth-aachen.de/record/52332