2‐D protein maps of rat gastrocnemius and soleus muscles: A tool for muscle plasticity assessment
- 9 January 2006
- journal article
- research article
- Published by Wiley in Proteomics
- Vol. 6 (1) , 321-340
- https://doi.org/10.1002/pmic.200501337
Abstract
Functional characterization of muscle fibers relies on ATPase activity and on differential measurements of metabolic proteins, including mitochondrial and glycolytic enzymes, glucose, lactate and lactic acid transporters, calcium cycling proteins and components of the contractile machinery. The recent introduction of microarray technology has enabled detailed gene expression studies under different physiological and pathological conditions, thus generating novel hypotheses on muscle function. However, microarray approaches are limited by the incomplete genome coverage of currently available chips, and by poor correlation between mRNA concentration and protein expression level. We have used 2‐DE and MS to build a reference map of proteins from rat mixed gastrocnemius and soleus muscle, and to assess qualitative and quantitative differences in protein distribution between these two functionally dissimilar muscles. More than 800 spots on each gel were detected by silver staining, of which 167 were excised, digested in‐gel with trypsin and analyzed by ESI‐MS/MS. One hundred and twenty eight distinct gene products were identified, including metabolic, transport and contractile proteins. Forty one spots displayed differences in relative expression level between mixed gastrocnemius and soleus samples. These data not only enable differentiation of functionally distinct slow‐twitch and fast‐twitch fiber types, but also provide tools for investigating muscle plasticity in response to physiological and environmental conditions such as aging or hypoxia.Keywords
This publication has 33 references indexed in Scilit:
- New aspects of altitude adaptation in Tibetans: a proteomic approachThe FASEB Journal, 2004
- Two‐dimensional protein map of human vastus lateralis muscleElectrophoresis, 2003
- Clenbuterol induces expression of multiple myosin heavy chain isoforms in rat soleus fibresActa Physiologica Scandinavica, 2002
- Probability-based protein identification by searching sequence databases using mass spectrometry dataElectrophoresis, 1999
- Phosphorylation of Myosin Regulatory Light Chain Eliminates Force-Dependent Changes in Relaxation Rates in Skeletal MuscleBiophysical Journal, 1998
- Biphasic expression of slow myosin light chains and slow tropomyosin isoforms during the development of the human quadriceps muscleFEBS Letters, 1991
- II. Morphological Adaptations of Human Skeletal Muscle to Chronic Hypoxia*International Journal of Sports Medicine, 1990
- Non‐linear pH courses with immobilized pH gradientsElectrophoresis, 1985
- Muscle fiber type composition of the rat hindlimbJournal of Anatomy, 1984
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970