Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 521, Issue 3, Pages 693-698Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2019.10.154
Keywords
Parkinson's disease; Human skin fibroblasts; Two-dimensional gel electrophoresis; Mass spectrometry; Proteomics
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Funding
- University of Bari
- Sanofi-Aventis Deutschland GmbH, Frankfurt am Main, Germany
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Vimentin, a member of cytoskeleton intermediate filaments proteins, plays a critical role in cell structure and dynamics. The present proteomic study reveals reduced amount of six different lengths, N-terminal truncated proteolytic products of vimentin, in the primary skin fibroblasts from two unrelated PD patients, as compared to control fibroblasts. The decreased amount of N-terminal truncated forms of vimentin in parkin-mutant fibroblasts, could contribute to impairment of cellular function, potentially contributing to the pathogenesis of Parkinson disease. (C) 2019 Elsevier Inc. All rights reserved.
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