RESEARCH ARTICLE


Calcium-Induced Conformational Transition of Trout Ependymins Monitored by Tryptophan Fluorescence



Bernhard Ganss1, 2, Werner Hoffmann*, 1, 3
1 Max-Planck-Institute for Psychiatry, Department of Neurochemistry, D-82152 Martinsried, Germany
2 CIHR Group in Matrix Dynamics, University of Toronto, Toronto, Ontario M5S 3E2, Canada
3 Institute of Molecular Biology and Medical Chemistry, Otto-von-Guericke-University, D-39120 Magdeburg, Germany

Article Information


Identifiers and Pagination:

Year: 2009
Volume: 3
First Page: 14
Last Page: 17
Publisher ID: TOBIOCJ-3-14
DOI: 10.2174/1874091X00903010014

Article History:

Received Date: 20/11/2008
Revision Received Date: 05/12/2008
Acceptance Date: 20/1/2009
Electronic publication date: 24/2/2009
Collection year: 2009

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Creative Commons License
© Ganss and Hoffmann; Licensee Bentham Open.

open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

* Address correspondence to this author at the Institut für Molekularbiologie und Medizinische Chemie, Universitätsklinikum, Leipziger Str. 44, D-39120 Magdeburg, Germany; Tel: +49-(391)-67-15 895; Fax: +49-(391)-67-13 096; E-mail: werner.hoffmann@med.ovgu.de


Abstract

Ependymins are secretory, calcium-binding sialoproteins which are the predominant constituents of the cerebrospinal fluid of many teleost fish. A bound form of these regeneration-responsive glycoproteins is associated with collagen fibrils of the extracellular matrix. Here, the tryptophan fluorescence of ependymins was monitored at various Ca2+ concentrations. Two distinct states were identified with a relatively sharp transition at about 1 mM Ca2+. In agreement with previous circular dichroism measurements, this strongly supports the hypothesis that a calcium-induced conformational change is important for the interaction of ependymins with components of the extracellular matrix. Such interactions with constituents of various basal laminae would also explain the important roles of piscine ependymins as well as invertebrate and mammalian ependymin-related proteins for cell adhesion processes and cell migration.

Keywords: Ependymins, MERP, calcium binding, extracellular matrix, tryptophan fluorescence, cell adhesion molecule, learning and memory.