Next Article in Journal / Special Issue
Role of Protein Carbonylation in Skeletal Muscle Mass Loss Associated with Chronic Conditions
Previous Article in Journal
Activity-Based Proteomics Reveals Heterogeneous Kinome and ATP-Binding Proteome Responses to MEK Inhibition in KRAS Mutant Lung Cancer
Previous Article in Special Issue
Age- and Activity-Related Differences in the Abundance of Myosin Essential and Regulatory Light Chains in Human Muscle
Open AccessArticle

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
Proteomes 2016, 4(2), 17;
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)
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
Show Figures

Figure 1

MDPI and ACS Style

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.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop