Cytoskeletal Alterations and Biomechanical Properties of parkin-Mutant Human Primary Fibroblasts.
Identifieur interne : 000778 ( Main/Exploration ); précédent : 000777; suivant : 000779Cytoskeletal Alterations and Biomechanical Properties of parkin-Mutant Human Primary Fibroblasts.
Auteurs : Daniele Vergara [Italie] ; Marzia M. Ferraro [Italie] ; Mariafrancesca Cascione [Italie] ; Loretta L. Del Mercato [Italie] ; Stefano Leporatti [Italie] ; Anna Ferretta [Italie] ; Paola Tanzarella [Italie] ; Consiglia Pacelli [Canada] ; Angelo Santino [Italie] ; Michele Maffia [Italie] ; Tiziana Cocco [Italie] ; Ross Rinaldi [Italie] ; Antonio Gaballo [Italie]Source :
- Cell biochemistry and biophysics [ 1559-0283 ] ; 2015.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Ubiquitin-Protein Ligases.
- chemical , metabolism : Cytoskeletal Proteins.
- genetics : Parkinson Disease.
- metabolism : Cytoskeleton.
- pathology : Fibroblasts, Parkinson Disease.
- Biomechanical Phenomena, Cell Shape, Elasticity, Humans, Mechanical Phenomena, Mutation.
Abstract
Parkinson's disease (PD) is one of the most common neurodegenerative diseases. Genes which have been implicated in autosomal-recessive PD include PARK2 which codes for parkin, an E3 ubiquitin ligase that participates in a variety of cellular activities. In this study, we compared parkin-mutant primary fibroblasts, from a patient with parkin compound heterozygous mutations, to healthy control cells. Western blot analysis of proteins obtained from patient's fibroblasts showed quantitative differences of many proteins involved in the cytoskeleton organization with respect to control cells. These molecular alterations are accompanied by changes in the organization of actin stress fibers and biomechanical properties, as revealed by confocal laser scanning microscopy and atomic force microscopy. In particular, parkin deficiency is associated with a significant increase of Young's modulus of null-cells in comparison to normal fibroblasts. The current study proposes that parkin influences the spatial organization of actin filaments, the shape of human fibroblasts, and their elastic response to an external applied force.
DOI: 10.1007/s12013-014-0362-1
PubMed: 25399302
Affiliations:
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Le document en format XML
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<term>Elasticity</term>
<term>Fibroblasts (pathology)</term>
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<front><div type="abstract" xml:lang="en">Parkinson's disease (PD) is one of the most common neurodegenerative diseases. Genes which have been implicated in autosomal-recessive PD include PARK2 which codes for parkin, an E3 ubiquitin ligase that participates in a variety of cellular activities. In this study, we compared parkin-mutant primary fibroblasts, from a patient with parkin compound heterozygous mutations, to healthy control cells. Western blot analysis of proteins obtained from patient's fibroblasts showed quantitative differences of many proteins involved in the cytoskeleton organization with respect to control cells. These molecular alterations are accompanied by changes in the organization of actin stress fibers and biomechanical properties, as revealed by confocal laser scanning microscopy and atomic force microscopy. In particular, parkin deficiency is associated with a significant increase of Young's modulus of null-cells in comparison to normal fibroblasts. The current study proposes that parkin influences the spatial organization of actin filaments, the shape of human fibroblasts, and their elastic response to an external applied force.</div>
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