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A Novel Disulfide Pattern in Laminin-Type Epidermal Growth Factor-like (LE) Modules of Laminin β1 and γ1 Chains

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Stefan Kalkhof‡^#, Konstanze Witte‡^#, Christian H. Ihling‡, Mathias Q. Müller‡, Manuel V. Keller§

, Sebastian Haehn§, Neil Smyth

, Mats Paulsson§

, and Andrea Sinz*‡

^‡ Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, D-06120 Halle (Saale), Germany

^§ Center for Biochemistry and Center for Molecular Medicine, Faculty of Medicine, University of Cologne, D-50931 Cologne, Germany

Cologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases (CECAD), D-50931 Cologne, Germany

School of Biological Sciences, University of Southampton, East Southampton SO16 7PX, United Kingdom

Biochemistry, 2010, 49 (38), pp 8359–8366

DOI: 10.1021/bi101187f

Publication Date (Web): August 23, 2010

*Address correspondence to this author. Tel: +49-345-5525170. Fax: +49-345-5527026. E-mail: andrea.sinz@pharmazie.uni-halle.de.,

Present address: Department of Proteomics, Helmholtz Center for Environmental Research—UFZ, D-04318 Leipzig, Germany

, #

Both authors contributed equally to this work

† Funding Statement

This work was funded by grants SI 867/7-1 and SM 65/1-3 from the DFG (Deutsche Forschungsgemeinschaft). S.K. acknowledges support by the International Postgraduate Programme (IPP) at the University of Leipzig and the DFG-funded Graduiertenkolleg 1026 “Conformational Transitions in Macromolecular Interactions” at the Martin Luther University Halle-Wittenberg.

Abstract

In-depth mass spectrometric analysis of disulfide bond patterns in recombinant mouse laminin β1 and γ1 chain N-terminal fragments comprising the laminin N-terminal (LN) domain and the first four laminin epidermal growth factor-like (LE) domains revealed a novel disulfide pattern for LE domains. This showed a (2−3, 4−5, 6−7, 8−1) connectivity with the last cysteine of one LE domain being connected to the first cysteine of the following LE domain. The same pattern was also found in E4, the N-terminal β1 chain fragment derived by elastase digestion of mouse EHS tumor laminin-111, showing that this pattern occurs in native laminin. The strictly linear pattern with an interdomain disulfide has not been described previously for EGF domains. The N-terminal portions of laminin short arms, consisting of the LN domain and LE domains 1−4, are essential for laminin−laminin self-interactions, whereas the internal LE domains 7−9 in the laminin γ1 chain harbor the nidogen binding site and have a conventional disulfide pattern. This suggests that LE domains differing in function also differ in their disulfide patterns.

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