Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice
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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2016-05-01
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| Series: | Proteomes |
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| Online Access: | http://www.mdpi.com/2227-7382/4/2/17 |
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| author | Brigitte Picard Malek Kammoun Mohammed Gagaoua Christiane Barboiron Bruno Meunier Christophe Chambon Isabelle Cassar-Malek |
| author_facet | Brigitte Picard Malek Kammoun Mohammed Gagaoua Christiane Barboiron Bruno Meunier Christophe Chambon Isabelle Cassar-Malek |
| author_sort | Brigitte Picard |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-11T13:18:13Z |
| format | Article |
| id | doaj.art-8c27743f6f124b6381e6a1618fbbc651 |
| institution | Directory Open Access Journal |
| issn | 2227-7382 |
| language | English |
| last_indexed | 2024-04-11T13:18:13Z |
| publishDate | 2016-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Proteomes |
| spelling | doaj.art-8c27743f6f124b6381e6a1618fbbc6512022-12-22T04:22:18ZengMDPI AGProteomes2227-73822016-05-01421710.3390/proteomes4020017proteomes4020017Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null MiceBrigitte Picard0Malek Kammoun1Mohammed Gagaoua2Christiane Barboiron3Bruno Meunier4Christophe Chambon5Isabelle Cassar-Malek6International Institute of Agronomical Research (INRA)-Vetagro Sup, UMR1213, Saint-Genès-Champanelle F-63122, FranceInternational Institute of Agronomical Research (INRA)-Vetagro Sup, UMR1213, Saint-Genès-Champanelle F-63122, FranceInternational Institute of Agronomical Research (INRA)-Vetagro Sup, UMR1213, Saint-Genès-Champanelle F-63122, FranceInternational Institute of Agronomical Research (INRA)-Vetagro Sup, UMR1213, Saint-Genès-Champanelle F-63122, FranceInternational Institute of Agronomical Research (INRA)-Vetagro Sup, UMR1213, Saint-Genès-Champanelle F-63122, FranceINRA-Metabolism Exploration Plateform (PFEM), Saint-Genès-Champanelle F-63122, FranceInternational Institute of Agronomical Research (INRA)-Vetagro Sup, UMR1213, Saint-Genès-Champanelle F-63122, FranceHsp27—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.http://www.mdpi.com/2227-7382/4/2/172D-electrophoresisMS-MSskeletal muscleHspB1-null mouse |
| spellingShingle | Brigitte Picard Malek Kammoun Mohammed Gagaoua Christiane Barboiron Bruno Meunier Christophe Chambon Isabelle Cassar-Malek Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice Proteomes 2D-electrophoresis MS-MS skeletal muscle HspB1-null mouse |
| title | Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice |
| title_full | Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice |
| title_fullStr | Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice |
| title_full_unstemmed | Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice |
| title_short | Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice |
| title_sort | calcium homeostasis and muscle energy metabolism are modified in hspb1 null mice |
| topic | 2D-electrophoresis MS-MS skeletal muscle HspB1-null mouse |
| url | http://www.mdpi.com/2227-7382/4/2/17 |
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