scholarly journals Z- and M-band appearance in different histochemically defined types of human skeletal muscle fibers.

1982 ◽  
Vol 30 (1) ◽  
pp. 1-11 ◽  
Author(s):  
M Sjöström ◽  
S Kidman ◽  
K H Larsén ◽  
K A Angquist

In order to define ultrastructural features, which alone or in combination with other features could be used to identify different types of fibers in human skeletal muscle, frozen biopsy specimens of m. tibialis anterior were serially sectioned. The thawed sections were prepared either for enzyme histochemistry or for electron microscopy. The same fiber was then identified in all serial sections and its ultrastructure examined under the electron microscope. A total of 75 fibers were included in this investigation. Specimens were also conventionally prepared for electron microscopy. Special interest was devoted to the appearance of the sarcomeric Z- and M-bands. In the same fiber, all myofibrils showed the same Z- as well as M-band structure. On the other hand, it was evident that these structures varied from one type of fiber to another in the same muscle and that their appearance were covariant to a great extent. Low level resolution of Type 1 fibers usually showed broad Z- and M-bands with five strong M-bridge lines. In Type 2A fibers intermediate Z-bands were observed. In the middle portion of the M-bands, three strong M-bridge lines were distinct while the two outer lines were relatively weak. Finally, Type 2B fibers usually appeared with narrow Z-bands. The three M-bridge lines in the middle were strong while the two outer ones were very weak, if seen at all. Discriminant analysis showed that about 70% of the fibers should have been correctly allocated on the basis of the Z-band width alone. When two independent observers classified the fibers on the basis of M-band appearance, more than 95% of the fibers were correctly classified. Thus, both the Z- and M-bands, alone or in combination, can be used as fiber type discriminators. However, the M-band structure proved to be more reliable than the Z-band width, and should therefore be used as the fiber type indicator when only one of these parameters is considered.

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Marta Murgia ◽  
Leonardo Nogara ◽  
Martina Baraldo ◽  
Carlo Reggiani ◽  
Matthias Mann ◽  
...  

Abstract Background Human skeletal muscle is composed of three major fiber types, referred to as type 1, 2A, and 2X fibers. This heterogeneous cellular composition complicates the interpretation of studies based on whole skeletal muscle lysate. A single-fiber proteomics approach is required to obtain a fiber-type resolved quantitative information on skeletal muscle pathophysiology. Methods Single fibers were dissected from vastus lateralis muscle biopsies of young adult males and processed for mass spectrometry-based single-fiber proteomics. We provide and analyze a resource dataset based on relatively pure fibers, containing at least 80% of either MYH7 (marker of slow type 1 fibers), MYH2 (marker of fast 2A fibers), or MYH1 (marker of fast 2X fibers). Results In a dataset of more than 3800 proteins detected by single-fiber proteomics, we selected 404 proteins showing a statistically significant difference among fiber types. We identified numerous type 1 or 2X fiber type–specific protein markers, defined as proteins present at 3-fold or higher levels in these compared to other fiber types. In contrast, we could detect only two 2A-specific protein markers in addition to MYH2. We observed three other major patterns: proteins showing a differential distribution according to the sequence 1 > 2A > 2X or 2X > 2A > 1 and type 2–specific proteins expressed in 2A and 2X fibers at levels 3 times greater than in type 1 fibers. In addition to precisely quantifying known fiber type–specific protein patterns, our study revealed several novel features of fiber type specificity, including the selective enrichment of components of the dystrophin and integrin complexes, as well as microtubular proteins, in type 2X fibers. The fiber type–specific distribution of some selected proteins revealed by proteomics was validated by immunofluorescence analyses with specific antibodies. Conclusion We here show that numerous muscle proteins, including proteins whose function is unknown, are selectively enriched in specific fiber types, pointing to potential implications in muscle pathophysiology. This reinforces the notion that single-fiber proteomics, together with recently developed approaches to single-cell proteomics, will be instrumental to explore and quantify muscle cell heterogeneity.


2020 ◽  
Vol 134 ◽  
pp. 110880 ◽  
Author(s):  
V.L. Wyckelsma ◽  
W. Lindkvist ◽  
T. Venckunas ◽  
M. Brazaitis ◽  
S. Kamandulis ◽  
...  

2018 ◽  
Vol 56 (2) ◽  
pp. 322-331
Author(s):  
Rani S. Sellers ◽  
S. Radma Mahmood ◽  
Geoffrey S. Perumal ◽  
Frank P. Macaluso ◽  
Irwin J. Kurland

Lipin-1 ( Lpin1)–deficient lipodystrophic mice have scant and immature adipocytes and develop transient fatty liver early in life. Unlike normal mice, these mice cannot rely on stored triglycerides to generate adenosine triphosphate (ATP) from the β-oxidation of fatty acids during periods of fasting. To compensate, these mice store much higher amounts of glycogen in skeletal muscle and liver than wild-type mice in order to support energy needs during periods of fasting. Our studies demonstrated that there are phenotypic changes in skeletal muscle fibers that reflect an adaptation to this unique metabolic situation. The phenotype of skeletal muscle (soleus, gastrocnemius, plantaris, and extensor digitorum longus [EDL]) from Lpin1-/- was evaluated using various methods including immunohistochemistry for myosin heavy chains (Myh) 1, 2, 2a, 2b, and 2x; enzyme histochemistry for myosin ATPase, cytochrome-c oxidase (COX), and succinyl dehydrogenase (SDH); periodic acid–Schiff; and transmission electron microscopy. Fiber-type changes in the soleus muscle of Lpin1-/- mice were prominent and included decreased Myh1 expression with concomitant increases in Myh2 expression and myosin-ATPase activity; this change was associated with an increase in the presence of Myh1/2a or Myh1/2x hybrid fibers. Alterations in mitochondrial enzyme activity (COX and SDH) were apparent in the myofibers in the soleus, gastrocnemius, plantaris, and EDL muscles. Electron microscopy revealed increases in the subsarcolemmal mitochondrial mass in the muscles of Lpin1-/- mice. These data demonstrate that lipin-1 deficiency results in phenotypic fiber-specific modulation of skeletal muscle necessary for compensatory fuel utilization adaptations in lipodystrophy.


1995 ◽  
Vol 9 (11) ◽  
pp. 1091-1095 ◽  
Author(s):  
Jean‐Aimé Simoneau ◽  
Claude Bouchard

1997 ◽  
Vol 22 (4) ◽  
pp. 307-327 ◽  
Author(s):  
Robert S. Staron

This brief review attempts to summarize a number of studies on the delineation, development, and distribution of human skeletal muscle fiber types. A total of seven fiber types can be identified in human limb and trunk musculature based on the pH stability/ability of myofibrillar adenosine triphosphatase (mATPase). For most human muscles, mATPase-based fiber types correlate with the myosin heavy chain (MHC) content. Thus, each histochemically identified fiber has a specific MHC profile. Although this categorization is useful, it must be realized that muscle fibers are highly adaptable and that innumerable fiber type transients exist. Also, some muscles contain specific MHC isoforms and/or combinations that do not permit routine mATPase-based fiber typing. Although the major populations of fast and slow are, for the most part, established shortly after birth, subtle alterations take place throughout life. These changes appear to relate to alterations in activity and/or hormonal levels, and perhaps later in life, total fiber number. Because large variations in fiber type distribution can be found within a muscle and between individuals, interpretation of data gathered from human muscle is often difficult. Key words: aging, myosin heavy chains, myogenesis, myofibrillar adenosine triphosphate


2012 ◽  
Vol 22 (4) ◽  
pp. 292-303 ◽  
Author(s):  
Ildus I. Ahmetov ◽  
Olga L. Vinogradova ◽  
Alun G. Williams

The ability to perform aerobic or anaerobic exercise varies widely among individuals, partially depending on their muscle-fiber composition. Variability in the proportion of skeletal-muscle fiber types may also explain marked differences in aspects of certain chronic disease states including obesity, insulin resistance, and hypertension. In untrained individuals, the proportion of slow-twitch (Type I) fibers in the vastus lateralis muscle is typically around 50% (range 5–90%), and it is unusual for them to undergo conversion to fast-twitch fibers. It has been suggested that the genetic component for the observed variability in the proportion of Type I fibers in human muscles is on the order of 40–50%, indicating that muscle fiber-type composition is determined by both genotype and environment. This article briefly reviews current progress in the understanding of genetic determinism of fiber-type proportion in human skeletal muscle. Several polymorphisms of genes involved in the calcineurin–NFAT pathway, mitochondrial biogenesis, glucose and lipid metabolism, cytoskeletal function, hypoxia and angiogenesis, and circulatory homeostasis have been associated with fiber-type composition. As muscle is a major contributor to metabolism and physical strength and can readily adapt, it is not surprising that many of these gene variants have been associated with physical performance and athlete status, as well as metabolic and cardiovascular diseases. Genetic variants associated with fiber-type proportions have important implications for our understanding of muscle function in both health and disease.


Author(s):  
Athan G. Dial ◽  
Grace K. Grafham ◽  
Cynthia MF. Monaco ◽  
Jennifer Voth ◽  
Linda Brandt ◽  
...  

Though preclinical models of type 1 diabetes (T1D) exhibit impaired muscle regeneration, this has yet to be investigated in humans with T1D. Here we investigated the impact of damaging exercise (eccentric quadriceps contractions) in eighteen physically-active young adults with and without T1D. Pre- and post-exercise (48h and 96h), participants provided blood samples, vastus lateralis biopsies and performed maximal voluntary quadriceps contractions (MVC). Skeletal muscle sarcolemmal integrity, extracellular matrix content (ECM), and satellite cell (SC) content/proliferation were assessed by immunofluorescence. Transmission electron microscopy was used to quantify ultrastructural damage. MVC was comparable between T1D and controls before exercise. Post-exercise, MVC was decreased in both groups, but T1D subjects exhibited moderately lower strength recovery at both 48h and 96h. Serum creatine kinase, an indicator of muscle damage, was moderately higher in T1D participants at rest, and exhibited a small elevation 96h post-exercise. T1D participants showed lower SC content at all timepoints and demonstrated a moderate delay in SC proliferation after exercise. A greater number of myofibers exhibited sarcolemmal damage (disrupted dystrophin) and increased ECM (laminin) content in participants with T1D despite no differences between groups in ultrastructural damage as assessed by electron microscopy. Finally, transcriptomic analyses revealed dysregulated gene networks involving RNA translation and mitochondrial respiration, providing potential explanations for previous observations of mitochondrial dysfunction in similar T1D cohorts. Our findings indicate that skeletal muscle in young adults with moderately-controlled T1D is altered after damaging exercise; suggesting that longer recovery times following intense exercise may be necessary.


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