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Proteomes 2016, 4(2), 17;

Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice

International Institute of Agronomical Research (INRA)-Vetagro Sup, UMR1213, Saint-Genès-Champanelle F-63122, France
INRA-Metabolism Exploration Plateform (PFEM), Saint-Genès-Champanelle F-63122, France
Author to whom correspondence should be addressed.
Academic Editors: Jatin G. Burniston and Jacek R. Wisniewski
Received: 14 March 2016 / Revised: 12 April 2016 / Accepted: 18 April 2016 / Published: 4 May 2016
(This article belongs to the Special Issue Striated Muscle Proteomics)
PDF [5588 KB, uploaded 4 May 2016]


Hsp27—encoded by HspB1—is a member of the small heat shock proteins (sHsp, 12–43 kDa (kilodalton)) family. This protein is constitutively present in a wide variety of tissues and in many cell lines. The abundance of Hsp27 is highest in skeletal muscle, indicating a crucial role for muscle physiology. The protein identified as a beef tenderness biomarker was found at a crucial hub in a functional network involved in beef tenderness. The aim of this study was to analyze the proteins impacted by the targeted invalidation of HspB1 in the Tibialis anterior muscle of the mouse. Comparative proteomics using two-dimensional gel electrophoresis revealed 22 spots that were differentially abundant between HspB1-null mice and their controls that could be identified by mass spectrometry. Eighteen spots were more abundant in the muscle of the mutant mice, and four were less abundant. The proteins impacted by the absence of Hsp27 belonged mainly to calcium homeostasis (Srl and Calsq1), contraction (TnnT3), energy metabolism (Tpi1, Mdh1, PdhB, Ckm, Pygm, ApoA1) and the Hsp proteins family (HspA9). These data suggest a crucial role for these proteins in meat tenderization. The information gained by this study could also be helpful to predict the side effects of Hsp27 depletion in muscle development and pathologies linked to small Hsps. View Full-Text
Keywords: 2D-electrophoresis; MS-MS; skeletal muscle; HspB1-null mouse 2D-electrophoresis; MS-MS; skeletal muscle; HspB1-null mouse

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Picard, B.; Kammoun, M.; Gagaoua, M.; Barboiron, C.; Meunier, B.; Chambon, C.; Cassar-Malek, I. Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice. Proteomes 2016, 4, 17.

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