Historical Perspectives: Plasticity of mammalian skeletal muscle

2001 ◽  
Vol 90 (3) ◽  
pp. 1119-1124 ◽  
Author(s):  
Dirk Pette
Keyword(s):  
Skeletal Muscle ◽  
Fiber Type ◽  
Specific Impulse ◽  
Muscle Fibers ◽  
Experimental Models ◽  
Fiber Types ◽  
Mammalian Skeletal Muscle ◽  
Muscle Plasticity ◽  
Historical Perspectives ◽  
Quantitative Changes

More than 40 years ago, the nerve cross-union experiment of Buller, Eccles, and Eccles provided compelling evidence for the essential role of innervation in determining the properties of mammalian skeletal muscle fibers. Moreover, this experiment revealed that terminally differentiated muscle fibers are not inalterable but are highly versatile entities capable of changing their phenotype from fast to slow or slow to fast. With the use of various experimental models, numerous studies have since confirmed and extended the notion of muscle plasticity. Together, these studies demonstrated that motoneuron-specific impulse patterns, neuromuscular activity, and mechanical loading play important roles in both the maintenance and transition of muscle fiber phenotypes. Depending on the type, intensity, and duration of changes in any of these factors, muscle fibers adjust their phenotype to meet the altered functional demands. Fiber-type transitions resulting from multiple qualitative and quantitative changes in gene expression occur sequentially in a regular order within a spectrum of pure and hybrid fiber types.

The KATP channel Kir6.2 subunit content is higher in glycolytic than oxidative skeletal muscle fibers

2011 ◽  
Vol 301 (4) ◽  
pp. R916-R925 ◽  
Author(s):  
Krystyna Banas ◽  
Charlene Clow ◽  
Bernard J. Jasmin ◽  
Jean-Marc Renaud
Keyword(s):  
Skeletal Muscle ◽  
Cross Sections ◽  
Fiber Type ◽  
Energy Levels ◽  
Muscle Fibers ◽  
Metabolic Stress ◽  
Oxidative Capacity ◽  
Fiber Types ◽  
Fiber Damage ◽  
The Individual

It has long been suggested that in skeletal muscle, the ATP-sensitive K+ channel (KATP) channel is important in protecting energy levels and that abolishing its activity causes fiber damage and severely impairs function. The responses to a lack of KATP channel activity vary between muscles and fibers, with the severity of the impairment being the highest in the most glycolytic muscle fibers. Furthermore, glycolytic muscle fibers are also expected to face metabolic stress more often than oxidative ones. The objective of this study was to determine whether the t-tubular KATP channel content differs between muscles and fiber types. KATP channel content was estimated using a semiquantitative immunofluorescence approach by staining cross sections from soleus, extensor digitorum longus (EDL), and flexor digitorum brevis (FDB) muscles with anti-Kir6.2 antibody. Fiber types were determined using serial cross sections stained with specific antimyosin I, IIA, IIB, and IIX antibodies. Changes in Kir6.2 content were compared with changes in CaV1.1 content, as this Ca2+ channel is responsible for triggering Ca2+ release from sarcoplasmic reticulum. The Kir6.2 content was the lowest in the oxidative soleus and the highest in the glycolytic EDL and FDB. At the individual fiber level, the Kir6.2 content within a muscle was in the order of type IIB > IIX > IIA ≥ I. Interestingly, the Kir6.2 content for a given fiber type was significantly different between soleus, EDL, and FDB, and highest in FDB. Correlations of relative fluorescence intensities from the Kir6.2 and CaV1.1 antibodies were significant for all three muscles. However, the variability in content between the three muscles or individual fibers was much greater for Kir6.2 than for CaV1.1. It is suggested that the t-tubular KATP channel content increases as the glycolytic capacity increases and as the oxidative capacity decreases and that the expression of KATP channels may be linked to how often muscles/fibers face metabolic stress.

The Adaptive Potential of Skeletal Muscle Fibers

2002 ◽  
Vol 27 (4) ◽  
pp. 423-448 ◽  
Author(s):  
Dirk Pette
Keyword(s):  
Skeletal Muscle ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Protein Isoforms ◽  
Mammalian Skeletal Muscle ◽  
Adaptive Potential ◽  
Hybrid Fibers ◽  
Neuromuscular Activity ◽  
Skeletal Muscle Fibers ◽  
Initial Location

Mammalian skeletal muscle fibers display a great adaptive potential. This potential results from the ability of muscle fibers to adjust their molecular, functional, and metabolic properties in response to altered functional demands, such as changes in neuromuscular activity or mechanical loading. Adaptive changes in the expression of myofibrillar and other protein isoforms result in fiber type transitions. These transitions occur in a sequential order and encompass a spectrum of pure and hybrid fibers. Depending on the quality, intensity, and duration of the alterations in functional demand, muscle fibers may undergo functional transitions in the direction of slow or fast, as well as metabolic transitions in the direction of aerobic-oxidative or glycotytic. The maximum range of possible transitions in either direction depends on the fiber phenotype and is determined by its initial location in the fiber spectrum. Key words: Ca-sequestering proteins, energy metabolism, fiber type transition, myofibrillar protein isofonns, myosin, neuromuscular activity

scholarly journals Identification of sarcolemma-associated antigens with differential distributions on fast and slow skeletal muscle fibers

1987 ◽  
Vol 104 (4) ◽  
pp. 967-979 ◽  
Author(s):  
DA Schafer ◽  
FE Stockdale
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Cardiac Myocytes ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Fiber Types ◽  
In Ovo ◽  
Adult Chicken ◽  
Skeletal Muscle Fibers ◽  
Vascular Structures

We have identified three sarcolemma-associated antigens, including two antigens that are differentially distributed on skeletal muscle fibers of the fast, fast/slow, and slow types. Monoclonal antibodies were prepared using partially purified membranes of adult chicken skeletal muscles as immunogens and were used to characterize three antigens associated with the sarcolemma of muscle fibers. Immunofluorescence staining of cryosections of adult and embryonic chicken muscles showed that two of the three antigens differed in expression by fibers depending on developmental age and whether the fibers were of the fast, fast/slow, or slow type. Fiber type was assigned by determining the content of fast and slow myosin heavy chain. MSA-55 was expressed equally by fibers of all types. In contrast, MSA-slow and MSA-140 differed in their expression by muscle fibers depending on fiber type. MSA-slow was detected exclusively at the periphery of fast/slow and slow fibers, but was not detected on fast fibers. MSA-140 was detected on all fibers but fast/slow and slow fibers stained more intensely suggesting that these fiber types contain more MSA-140 than fast fibers. These sarcolemma-associated antigens were developmentally regulated in ovo and in vitro. MSA-55 and MSA-140 were detected on all primary muscle fibers by day 8 in ovo of embryonic development, whereas MSA-slow was first detected on muscle fibers just before hatching. Those antigens expressed by fast fibers (MSA-55 and MSA-140) were expressed only after myoblasts differentiated into myotubes, but were not expressed by fibroblasts in cell culture. Each antigen was also detected in one or more nonskeletal muscle cell types: MSA-55 and MSA-slow in cardiac myocytes and smooth muscle of gizzard (but not vascular structures) and MSA-140 in cardiac myocytes and smooth muscle of vascular structures. MSA-55 was identified as an Mr 55,000, nonglycosylated, detergent-soluble protein, and MSA-140 was an Mr 140,000, cell surface protein. The Mr of MSA-slow could not be determined by immunoblotting or immunoprecipitation techniques. These findings indicate that muscle fibers of different physiological function differ in the components associated with the sarcolemma. While the function of these sarcolemma-associated antigens is unknown, their regulated appearance during development in ovo and as myoblasts differentiate in culture suggests that they may be important in the formation, maturation, and function of fast, fast/slow, and slow muscle fibers.

scholarly journals Advanced Fiber Type-Specific Protein Profiles Derived from Adult Murine Skeletal Muscle

Proteomes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 28
Author(s):  
Britta Eggers ◽  
Karin Schork ◽  
Michael Turewicz ◽  
Katalin Barkovits ◽  
Martin Eisenacher ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Spectrometric Analysis ◽  
Type I ◽  
Fiber Types ◽  
Protein Profiles ◽  
Data Set ◽  
Public Data ◽  
Murine Skeletal Muscle

Skeletal muscle is a heterogeneous tissue consisting of blood vessels, connective tissue, and muscle fibers. The last are highly adaptive and can change their molecular composition depending on external and internal factors, such as exercise, age, and disease. Thus, examination of the skeletal muscles at the fiber type level is essential to detect potential alterations. Therefore, we established a protocol in which myosin heavy chain isoform immunolabeled muscle fibers were laser microdissected and separately investigated by mass spectrometry to develop advanced proteomic profiles of all murine skeletal muscle fiber types. All data are available via ProteomeXchange with the identifier PXD025359. Our in-depth mass spectrometric analysis revealed unique fiber type protein profiles, confirming fiber type-specific metabolic properties and revealing a more versatile function of type IIx fibers. Furthermore, we found that multiple myopathy-associated proteins were enriched in type I and IIa fibers. To further optimize the assignment of fiber types based on the protein profile, we developed a hypothesis-free machine-learning approach, identified a discriminative peptide panel, and confirmed our panel using a public data set.

scholarly journals Activity-Dependent Signaling Pathways Controlling Muscle Diversity and Plasticity

Physiology ◽  
2007 ◽  
Vol 22 (4) ◽  
pp. 269-278 ◽  
Author(s):  
Stefano Schiaffino ◽  
Marco Sandri ◽  
Marta Murgia
Keyword(s):  
Skeletal Muscle ◽  
Signaling Pathways ◽  
Fiber Type ◽  
Neuromuscular Diseases ◽  
Fiber Types ◽  
Mammalian Skeletal Muscle ◽  
Nerve Activity ◽  
Prevention And Treatment ◽  
Metabolic Properties ◽  
Activity Dependent

A variety of fiber types with different contractile and metabolic properties is present in mammalian skeletal muscle. The fiber-type profile is controlled by nerve activity via specific signaling pathways, whose identification may provide potential therapeutic targets for the prevention and treatment of metabolic and neuromuscular diseases.

scholarly journals LncRNA-FKBP1C regulates muscle fiber type switching by affecting the stability of MYH1B

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Jia-ao Yu ◽  
Zhijun Wang ◽  
Xin Yang ◽  
Manting Ma ◽  
Zhenhui Li ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Stability ◽  
Muscle Fiber ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Fast Muscle ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Regulatory Processes ◽  
Muscle Genes

AbstractLong non-coding RNAs (lncRNAs) are well-known to participate in a variety of important regulatory processes in myogenesis. In our previous RNA-seq study (accession number GSE58755), we found that lncRNA-FKBP1C was differentially expressed between White Recessive Rock (WRR) and Xinghua (XH) chicken. Here, we have further demonstrated that lncRNA-FKBP1C interacted directly with MYH1B by biotinylated RNA pull-down assay and RNA immunoprecipitation (RIP). Protein stability and degradation experiments identified that lncRNA-FKBP1C enhanced the protein stability of MYH1B. Overexpression of lncRNA-FKBP1C inhibited myoblasts proliferation, promoted myoblasts differentiation, and participated in the formation of skeletal muscle fibers. LncRNA-FKBP1C could downregulate the fast muscle genes and upregulate slow muscle genes. Conversely, its interference promoted cell proliferation, repressed cell differentiation, and drove the transformation of slow-twitch muscle fibers to fast-twitch muscle fibers. Similar results were observed after knockdown of the MYH1B gene, but the difference was that the MYH1B gene had no effects on fast muscle fibers. In short, these data demonstrate that lncRNA-FKBP1C could bound with MYH1B and enhance its protein stability, thus affecting proliferation, differentiation of myoblasts and conversion of skeletal muscle fiber types.

scholarly journals Deep muscle-proteomic analysis of freeze-dried human muscle biopsies reveals fiber type-specific adaptations to exercise training

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
A. S. Deshmukh ◽  
D. E. Steenberg ◽  
M. Hostrup ◽  
J. B. Birk ◽  
J. K. Larsen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Exercise Training ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Human Muscle ◽  
Fiber Types ◽  
Freeze Dried ◽  
Fast Twitch Muscle ◽  
Fast Twitch ◽  
Muscle Biopsies

AbstractSkeletal muscle conveys several of the health-promoting effects of exercise; yet the underlying mechanisms are not fully elucidated. Studying skeletal muscle is challenging due to its different fiber types and the presence of non-muscle cells. This can be circumvented by isolation of single muscle fibers. Here, we develop a workflow enabling proteomics analysis of pools of isolated muscle fibers from freeze-dried human muscle biopsies. We identify more than 4000 proteins in slow- and fast-twitch muscle fibers. Exercise training alters expression of 237 and 172 proteins in slow- and fast-twitch muscle fibers, respectively. Interestingly, expression levels of secreted proteins and proteins involved in transcription, mitochondrial metabolism, Ca2+ signaling, and fat and glucose metabolism adapts to training in a fiber type-specific manner. Our data provide a resource to elucidate molecular mechanisms underlying muscle function and health, and our workflow allows fiber type-specific proteomic analyses of snap-frozen non-embedded human muscle biopsies.

scholarly journals Comparison of the effects of inorganic phosphate on caffeine-induced Ca2+ release in fast- and slow-twitch mammalian skeletal muscle

2008 ◽  
Vol 294 (1) ◽  
pp. C97-C105 ◽  
Author(s):  
Giuseppe S. Posterino ◽  
Stacey L. Dunn
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Inorganic Phosphate ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Creatine Phosphate ◽  
Mammalian Skeletal Muscle ◽  
Time Integral ◽  
Slow Twitch ◽  
Fast Twitch

We compared the effects of 50 mM Pi on caffeine-induced Ca2+ release in mechanically skinned fast-twitch (FT) and slow-twitch (ST) skeletal muscle fibers of the rat. The time integral (area) of the caffeine response was reduced by ∼57% (FT) and ∼27% (ST) after 30 s of exposure to 50 mM Pi in either the presence or absence of creatine phosphate (to buffer ADP). Differences in the sarcoplasmic reticulum (SR) Ca2+ content between FT and ST fibers [∼40% vs. 100% SR Ca2+ content (pCa 6.7), respectively] did not contribute to the different effects of Pi observed; underloading the SR of ST fibers so that the SR Ca2+ content approximated that of FT fibers resulted in an even smaller (∼21%), but not significant, reduction in caffeine-induced Ca2+ release by Pi. These observed differences between FT and ST fibers could arise from fiber-type differences in the ability of the SR to accumulate Ca2+-Pi precipitate. To test this, fibers were Ca2+ loaded in the presence of 50 mM Pi. In FT fibers, the maximum SR Ca2+ content (pCa 6.7) was subsequently increased by up to 13 times of that achieved when loading for 2 min in the absence of Pi. In ST fibers, the SR Ca2+ content was only doubled. These data show that Ca2+ release in ST fibers was less affected by Pi than FT fibers, and this may be due to a reduced capacity of ST SR to accumulate Ca2+-Pi precipitate. This may account, in part, for the fatigue-resistant nature of ST fibers.

Coregulation of fast contractile protein transgene and glycolytic enzyme expression in mouse skeletal muscle

2002 ◽  
Vol 282 (1) ◽  
pp. C113-C124 ◽  
Author(s):  
Patricia L. Hallauer ◽  
Kenneth E. M. Hastings
Keyword(s):  
Skeletal Muscle ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Glycolytic Enzyme ◽  
Contractile Protein ◽  
Fiber Types ◽  
Enzyme Expression ◽  
Mouse Muscle ◽  
Fast Fiber ◽  
Gene Regulatory

Little is known of the gene regulatory mechanisms that coordinate the contractile and metabolic specializations of skeletal muscle fibers. Here we report a novel connection between fast isoform contractile protein transgene and glycolytic enzyme expression. In quantitative histochemical studies of transgenic mouse muscle fibers, we found extensive coregulation of the glycolytic enzyme glycerol-3-phosphate dehydrogenase (GPDH) and transgene constructs based on the fast skeletal muscle troponin I (TnIfast) gene. In addition to a common IIB > IIX > IIA fiber type pattern, TnIfast transgenes and GPDH showed correlated fiber-to-fiber variation within each fast fiber type, concerted emergence of high-level expression during early postnatal muscle maturation, and parallel responses to muscle under- or overloading. Regulatory information for GPDH-coregulated expression is carried by the TnIfast first-intron enhancer (IRE). These results identify an unexpected contractile/metabolic gene regulatory link that is amenable to further molecular characterization. They also raise the possibility that the equal expression in all fast fiber types observed for the endogenous TnIfast gene may be driven by different metabolically coordinated mechanisms in glycolytic (IIB) vs. oxidative (IIA) fast fibers.

Myosin isoforms in mammalian skeletal muscle

1994 ◽  
Vol 77 (2) ◽  
pp. 493-501 ◽  
Author(s):  
S. Schiaffino ◽  
C. Reggiani
Keyword(s):  
Skeletal Muscle ◽  
Fiber Type ◽  
Mammalian Species ◽  
Maximum Velocity ◽  
Fiber Types ◽  
Myosin Isoforms ◽  
Mammalian Skeletal Muscle ◽  
Differential Distribution ◽  
Specific Regulation

Skeletal muscles of different mammalian species contain four major myosin heavy-chain (MHC) isoforms: the “slow” or beta-MHC and the three “fast” IIa-, IIx-, and IIb-MHCs; and three major myosin light-chain (MLC) isoforms, the “slow” MLC1s and the two “fast” MLC1f and MLC3f. The differential distribution of the MHCs defines four major fiber types containing a single MHC isoform and a number of intermediate hybrid fiber populations containing both beta/slow- and IIa-MHC, IIa- and IIx-MHC, or IIx- and IIb-MHC. The IIa-, IIx-, and IIb-MHCs were first detected in neonatal muscles, and their expression in developing and adult muscle is regulated by neural, hormonal, and mechanical factors. The transcriptional mechanisms responsible for the fiber type-specific regulation of MHC and MLC gene expression are not known and are presently being explored by in vivo transfection experiments. The functional role of MHC isoforms has been in part clarified by correlated biochemical-physiological studies on single skinned fibers: these studies, in agreement with results from in vitro motility assays, indicate that both MHC and MLC isoforms determine the maximum velocity of shortening of skeletal muscle fibers.

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