Jump to ContentJump to Main Navigation

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR increased in 2014: 3.268
Rank 106 out of 289 in category Biochemistry & Molecular Biology in the 2014 Thomson Reuters Journal Citation Report/Science Edition

SCImago Journal Rank (SJR) 2014: 1.596
Source Normalized Impact per Paper (SNIP) 2014: 0.845
Impact per Publication (IPP) 2014: 2.992

VolumeIssuePage

Issues

Interaction of the cellular prion protein with raft-like lipid membranes

Kerstin Elfrink1 / Luitgard Nagel-Steger2 / Detlev Riesner3

1.

2.

3.

Corresponding author

Citation Information: Biological Chemistry. Volume 388, Issue 1, Pages 79–89, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2007.010, January 2007

Publication History

Received:
May 9, 2006
Accepted:
September 19, 2006
Published Online:
2007-01-10

Abstract

Conversion of the cellular isoform of the prion protein (PrPC) into the disease-associated isoform (PrPSc) plays a key role in the development of prion diseases. Within its cellular pathway, PrPC undergoes several posttranslational modifications, i.e., the attachment of two N-linked glycans and a glycosyl phosphatidyl inositol (GPI) anchor, by which it is linked to the plasma membrane on the exterior cell surface. To study the interaction of PrPC with model membranes, we purified posttranslationally modified PrPC from transgenic Chinese hamster ovary (CHO) cells. The mono-, di- and oligomeric states of PrPC free in solution were analyzed by analytical ultracentrifugation. The interaction of PrPC with model membranes was studied using both lipid vesicles in solution and lipid bilayers bound to a chip surface. The equilibrium and mechanism of PrPC association with the model membranes were analyzed by surface plasmon resonance. Depending on the degree of saturation of binding sites, the concentration of PrPC released from the membrane into aqueous solution was estimated at between 10-9 and 10-7 M. This corresponds to a free energy of the insertion reaction of -48 kJ/mol. Consequences for the conversion of PrPC to PrPSc are discussed.

Keywords: Biacore; GPI anchor; prion; PrPC; surface plasmon resonance

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Anita Alvarez‑Laviada, Ivan Kadurin, Assunta Senatore, Roberto Chiesa, and Annette C. Dolphin
Biochemical Journal, 2014, Volume 458, Number 2, Page 365
[2]
K. Elfrink, J. Ollesch, J. Stohr, D. Willbold, D. Riesner, and K. Gerwert
Proceedings of the National Academy of Sciences, 2008, Volume 105, Number 31, Page 10815
[3]
Thomas Schubert, Michael Bärmann, Monika Rusp, Walter Gränzer, and Motomu Tanaka
Journal of Membrane Science, 2008, Volume 321, Number 1, Page 61
[4]
Jan Stöhr, Kerstin Elfrink, Nicole Weinmann, Holger Wille, Dieter Willbold, Eva Birkmann, and Detlev Riesner
Biological Chemistry, 2011, Volume 392, Number 5
[5]
Stéphanie Steunou, Jean-François Chich, Human Rezaei, and Jasmina Vidic
Biosensors and Bioelectronics, 2010, Volume 26, Number 4, Page 1399
[6]
Giannantonio Panza, Christian Dumpitak, and Eva Birkmann
Rejuvenation Research, 2010, Volume 13, Number 2-3, Page 220
[7]
Adriano Aguzzi, Frank Baumann, and Juliane Bremer
Annual Review of Neuroscience, 2008, Volume 31, Number 1, Page 439
[8]
Rebecca L. Rich and David G. Myszka
Journal of Molecular Recognition, 2008, Volume 21, Number 6, Page 355

Comments (0)

Please log in or register to comment.