scholarly journals Microbiopsy Sampling for Examining Age-Related Differences in Skeletal Muscle Fiber Morphology and Composition

2022 ◽  
Vol 12 ◽  
Author(s):  
Garrett M. Hester ◽  
Trisha A. VanDusseldorp ◽  
Phuong L. Ha ◽  
Kaveh Kiani ◽  
Alex A. Olmos ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Vastus Lateralis ◽  
Peak Torque ◽  
Type I ◽  
Type Ii ◽  
Fiber Morphology ◽  
Specific Strength ◽  
Age Related ◽  
Whole Muscle

Introduction: The increasingly popular microbiopsy is an appealing alternative to the more invasive Bergström biopsy given the challenges associated with harvesting skeletal muscle in older populations. Parameters of muscle fiber morphology and composition derived from the microbiopsy have not been compared between young and older adults.Purpose: The purpose of this study was to examine muscle fiber morphology and composition in young (YM) and older (OM) males using the microbiopsy sampling technique. A secondary aim was to determine if specific strength is associated with serum levels of C-terminal agrin fragment [CAF; an indicator of neuromuscular junction (NMJ) degradation].Methods: Thirty healthy, YM (n = 15, age = 20.7 ± 2.2 years) and OM (n = 15, age = 71.6 ± 3.9 years) underwent ultrasound imaging to determine whole-muscle cross-sectional area (CSA) of the vastus lateralis and rectus femoris as well as isometric and isokinetic (60°⋅s–1 and 180°⋅s–1) peak torque testing of the knee extensors. Microbiopsy samples of the vastus lateralis were collected from 13 YM and 11 OM, and immunofluorescence was used to calculate CSA and proportion of type I and type II fibers.Results: Peak torque was lower in OM at all velocities (p ≤ 0.001; d = 1.39–1.86) but only lower at 180°⋅s–1 (p = 0.003; d = 1.23) when normalized to whole-muscle CSA. Whole-muscle CSA was smaller in OM (p = 0.001; d = 1.34), but atrophy was not present at the single fiber level (p > 0.05). Per individual, ∼900 fibers were analyzed, and type I fiber CSA was larger (p = 0.05; d = 0.94) in OM which resulted in a smaller type II/I fiber CSA ratio (p = 0.015; d = 0.95). CAF levels were not sensitive to age (p = 0.159; d = 0.53) nor associated with specific strength or whole-muscle CSA in OM.Conclusion: The microbiopsy appears to be a viable alternative to the Bergström biopsy for histological analyses of skeletal muscle in older adults. NMJ integrity was not influential for age-related differences in specific strength in our healthy, non-sarcopenic older sample.

Compensatory muscle fiber hypertrophy in elderly men

1992 ◽  
Vol 73 (3) ◽  
pp. 812-816 ◽  
Author(s):  
A. Aniansson ◽  
G. Grimby ◽  
M. Hedberg
Keyword(s):  
Muscle Strength ◽  
Muscle Fiber ◽  
Citrate Synthase ◽  
Biceps Brachii ◽  
Vastus Lateralis ◽  
Cell Mass ◽  
Knee Extension ◽  
Type I ◽  
Type Ii ◽  
Elderly Men

Muscle strength and muscle morphology have been studied three times during a period of 11 yr in nine elderly men. On the last occasion the average age was 80.4 (range 79–82) yr. Body cell mass decreased by 6% and muscle strength for knee extension, measured by means of isometric and concentric isokinetic (30–60 degrees/s) recordings, declined by 25–35% over the 11-yr period. Between 76 and 80 yr of age only the isokinetic strength for 30 degrees/s decreased significantly. Muscle fiber composition in the vastus lateralis did not change between 69 and 76 yr of age, but there was a significant reduction in the proportion of type IIb fibers from 76 to 80 yr. The decrease in type II fiber areas was not significant between 69 and 76 yr of age (as in a larger sample from the same population), but a significant increase in both type I and type II fiber areas was recorded from 76 to 80 yr of age and biceps brachii showed similar tendencies. In the same period, the enzymatic activities of myokinase and lactate dehydrogenase subsided in the vastus lateralis, but there was no change for triose phosphate dehydrogenase, 3-hydroxy-CoA-dehydrogenase, and citrate synthase. The muscle fiber hypertrophy in this group of elderly men with maintained physical activity between 76 and 80 yr of age is interpreted as a compensatory adaptation for the loss of motor units. In addition, the adaptation with respect to oxidative capacities seems to be maintained at this age.

scholarly journals Satellite cell content is specifically reduced in type II skeletal muscle fibers in the elderly

2007 ◽  
Vol 292 (1) ◽  
pp. E151-E157 ◽  
Author(s):  
Lex B. Verdijk ◽  
René Koopman ◽  
Gert Schaart ◽  
Kenneth Meijer ◽  
Hans H. C. M. Savelberg ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Fiber Type ◽  
The Elderly ◽  
Type I ◽  
Type Ii ◽  
Fiber Area ◽  
Muscle Fiber Atrophy ◽  
Fiber Atrophy ◽  
Type Ii Fibers

Satellite cells (SC) are essential for skeletal muscle growth and repair. Because sarcopenia is associated with type II muscle fiber atrophy, we hypothesized that SC content is specifically reduced in the type II fibers in the elderly. A total of eight elderly (E; 76 ± 1 yr) and eight young (Y; 20 ± 1 yr) healthy males were selected. Muscle biopsies were collected from the vastus lateralis in both legs. ATPase staining and a pax7-antibody were used to determine fiber type-specific SC content (i.e., pax7-positive SC) on serial muscle cross sections. In contrast to the type I fibers, the proportion and mean cross-sectional area of the type II fibers were substantially reduced in E vs. Y. The number of SC per type I fiber was similar in E and Y. However, the number of SC per type II fiber was substantially lower in E vs. Y (0.044 ± 0.003 vs. 0.080 ± 0.007; P < 0.01). In addition, in the type II fibers, the number of SC relative to the total number of nuclei and the number of SC per fiber area were also significantly lower in E. This study is the first to show type II fiber atrophy in the elderly to be associated with a fiber type-specific decline in SC content. The latter is evident when SC content is expressed per fiber or per fiber area. The decline in SC content might be an important factor in the etiology of type II muscle fiber atrophy, which accompanies the loss of skeletal muscle with aging.

Histochemical and Morphometric Evaluation of Skeletal Muscle of Cachectic Sheep

1981 ◽  
Vol 18 (3) ◽  
pp. 279-298 ◽  
Author(s):  
T. J. Hulland
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Succinic Dehydrogenase ◽  
Adult Life ◽  
Biological Behavior ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Atrophy And Hypertrophy ◽  
Type I Fibers

Skeletal muscle of sheep was examined histochemically in an attempt to define muscle fiber populations capable of distinctive biological behavior. ATPase at alkaline and acid pH, NADH-TR, and succinic dehydrogenase showed at least 12 fiber types, but only three often enough to be considered biologically important muscle fiber populations. The proportions of the three major types altered during early life, but not perceptibly during adult life. Proportions of Type I and Type II fibers were different, sometimes significantly, from breed to breed. Histochemical techniques and morphometric analyses of fiber cross-sectional area were used to study muscle fiber changes in moderate to marked cachectic atrophy. Progressive reduction of gross muscle volume was attended by complex interrelationships between the two major muscle fiber types, including alternate episodes of atrophy and hypertrophy, resulting in marked inequality of mean fiber size between the fiber types. The patterns appeared to be different but characteristic for each muscle. The usual pattern of cachectic atrophy shows atrophy resistance of Type I fibers, but here a Type II-dominant atrophy also was seen. It is concluded that the large muscle fibers often seen in advanced cachectic atrophy are those Type I fibers that are more labile in both atrophy and hypertrophy than most.

The Effects of Non-Weight Bearing on Skeletal Muscle in Older Rats: an Interrupted Bout versus an Uninterrupted Bout

2004 ◽  
Vol 5 (3) ◽  
pp. 195-202 ◽  
Author(s):  
Alissa Guildner Gehrke ◽  
Margaret Sheie Krull ◽  
Robin Shotwell McDonald ◽  
Tracy Sparby ◽  
Jessica Thoele ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Fiber Type ◽  
Weight Bearing ◽  
Cross Sectional Area ◽  
Type I ◽  
Type Ii ◽  
Sectional Area ◽  
Cross Sectional ◽  
Age Related ◽  
Type Ii Fibers

Age-related changes in skeletal muscle, in combination with bed rest, may result in a poorer rehabilitation potential for an elderly patient. The purpose of this study was to determine the effects of non-weight bearing (hind limb unweighting [HU]) on the soleus and extensor digitorum longus (EDL) in older rats. Two non-weight bearing conditions were used: an uninterrupted bout of HU and an interrupted bout of HU. Twenty-one rats were randomly placed into 1 of 3 groups: control, interrupted HU (2 phases of 7 days of HU, separated by a 4-day weight-bearing phase) and an uninterrupted HU (18 uninterrupted days of HU). Following non-weight bearing, the soleus and EDL muscles were removed. Fiber type identification was performed by myofibrillar ATPase and cross-sectional area was determined. The findings suggest that any period of non-weight bearing leads to a decrease in muscle wet weight (19%-45%). Both type I and type II fibers of the soleus showed atrophy (decrease in cross-sectional area, 35%-44%) with an uninterrupted bout of non-weight bearing. Only the type II fibers of the soleus showed recovery with an interrupted bout of weight bearing. In the EDL, type II fibers were more affected by an uninterrupted bout of non-weight bearing (15% decrease in fiber size) compared to the type I fibers. EDL type II fibers showed more atrophy with interrupted bouts of non-weight bearing than with a single bout (a 40% compared to a 15% decrease). This study shows that initial weight bearing after an episode of non-weight bearing may be damaging to type II fibers of the EDL.

scholarly journals Prostaglandin E2/cyclooxygenase pathway in human skeletal muscle: influence of muscle fiber type and age

2016 ◽  
Vol 120 (5) ◽  
pp. 546-551 ◽  
Author(s):  
Sophia Z. Liu ◽  
Bozena Jemiolo ◽  
Kaleen M. Lavin ◽  
Bridget E. Lester ◽  
Scott W. Trappe ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Human Skeletal Muscle ◽  
Muscle Protein ◽  
Vastus Lateralis ◽  
Production Capacity ◽  
Prostaglandin E ◽  
Type I ◽  
Men And Women ◽  
Cox 1

Prostaglandin E2 (PGE2) produced by the cyclooxygenase (COX) pathway regulates skeletal muscle protein turnover and exercise training adaptations. The purpose of this study was twofold: 1) define the PGE2/COX pathway enzymes and receptors in human skeletal muscle, with a focus on type I and II muscle fibers; and 2) examine the influence of aging on this pathway. Muscle biopsies were obtained from the soleus (primarily type I fibers) and vastus lateralis (proportionally more type II fibers than soleus) of young men and women ( n = 8; 26 ± 2 yr), and from the vastus lateralis of young ( n = 8; 25 ± 1 yr) and old ( n = 12; 79 ± 2 yr) men and women. PGE2/COX pathway proteins [COX enzymes (COX-1 and COX-2), PGE2 synthases (cPGES, mPGES-1, and mPGES-2), and PGE2 receptors (EP1, EP2, EP3, and EP4)] were quantified via Western blot. COX-1, cPGES, mPGES-2, and all four PGE2 receptors were detected in all skeletal muscle samples examined. COX-1 ( P < 0.1) and mPGES-2 were ∼20% higher, while EP3 was 99% higher and EP4 57% lower in soleus compared with vastus lateralis ( P < 0.05). Aging did not change the level of skeletal muscle COX-1, while cPGES increased 45% and EP1 ( P < 0.1), EP3, and EP4 decreased ∼33% ( P < 0.05). In summary, PGE2 production capacity and receptor levels are different in human skeletal muscles with markedly different type I and II muscle fiber composition. In aging skeletal muscle, PGE2 production capacity is elevated and receptor levels are downregulated. These findings have implications for understanding the regulation of skeletal muscle adaptations to exercise and aging by the PGE2/COX pathway and related inhibitors.

scholarly journals Cytoskeletal structure of skeletal muscle: identification of an intricate exosarcomeric microtubule lattice in slow- and fast-twitch muscle fibers.

1993 ◽  
Vol 41 (7) ◽  
pp. 1013-1021 ◽  
Author(s):  
S Boudriau ◽  
M Vincent ◽  
C H Côté ◽  
P A Rogers
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Vastus Lateralis ◽  
Muscle Fiber Types ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Fiber Types ◽  
Mammalian Skeletal Muscle ◽  
Microtubule Network ◽  
Fast Twitch

We used immunochemical quantification and indirect immunofluorescence to investigate the cell content, distribution, and organization of microtubules in adult rat slow-twitch soleus and fast-twitch vastus lateralis muscles. An immunoblotting assay demonstrated that the soleus muscle (primarily Type I fibers) was found to have a 1.7-fold higher relative content of alpha-tubulin compared with the superficial portion of the vastus lateralis muscle (primarily Type IIb fibers). Both physiological muscle types revealed a complex arrangement of microtubules which displayed oblique, longitudinal, and transverse orientations within the sarcoplasmic space. The predominance of any one particular orientation varied significantly from one muscle tissue section to another. Nuclei were completely surrounded by a dense net-like structure of microtubules. Both muscle fiber types were found to possess a higher density of microtubules in the subsarcolemmal region. These microtubules followed the contour of the sarcolemma in slightly contracted fibers and showed a fine punctate appearance indicative of a restricted distribution. The immunofluorescence results indicate that microtubules are associated with the sarcolemma and therefore may form a part of the membrane cytoskeletal domain of the muscle fiber. We conclude that the microtubule network of the adult mammalian skeletal muscle fiber constitutes a bone fide component of the exosarcomeric cytoskeletal lattice domain along with the intermediate filaments, and as such could therefore participate in the mechanical integration of the various organelles of the myofibers during the contraction-relaxation cycle.

scholarly journals Evidence for Three Fast Myosin Heavy Chain Isoforms in Type II Skeletal Muscle Fibers in the Adult Llama (Lama glama)

2001 ◽  
Vol 49 (8) ◽  
pp. 1033-1044 ◽  
Author(s):  
Guillermo H. Graziotti ◽  
Clara M. Ríos ◽  
José-Luis L. Rivero
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Rank Order ◽  
Muscle Fiber Types ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Lama Glama ◽  
Fast Twitch ◽  
Matpase Histochemistry

Skeletal muscle fiber types classified on the basis of their content of different myosin heavy chain (MHC) isoforms were analyzed in samples from hindlimb muscles of adult sedentary llamas ( Lama glama) by correlating immunohistochemistry with specific anti-MHC monoclonal antibodies, myofibrillar ATPase (mATPase) histochemistry, and quantitative histochemistry of fiber metabolic and size properties. The immunohistochemical technique allowed the separation of four pure (i.e., expressing a unique MHC isoform) muscle fiber types: one slow-twitch (Type I) and three fast-twitch (Type II) phenotypes. The same four major fiber types could be objectively discriminated with two serial sections stained for mATPase after acid (pH 4.5) and alkaline (pH 10.5) preincubations. The three fast-twitch fiber types were tentatively designated as IIA, IIX, and IIB on the basis of the homologies of their immunoreactivities, acid denaturation of their mATPase activity, size, and metabolic properties expressed at the cellular level with the corresponding isoforms of rat and horse muscles. Acid stability of their mATPase activity increased in the rank order IIA>IIX>IIB. The same was true for size and glycolytic capacity, whereas oxidative capacity decreased in the same rank order IIA>IIX>IIB. In addition to these four pure fibers (I, IIA, IIX, and IIB), four other fiber types with hybrid phenotypes containing two (I + IIA, IIAX, and IIXB) or three (IIAXB) MHCs were immunohistochemically delineated. These frequent phenotypes (40% of the semitendinosus muscle fiber composition) had overlapped mATPase staining intensities with their corresponding pure fiber types, so they could not be delineated by mATPase histochemistry. Expression of the three fast adult MHC isoforms was spatially regulated around islets of Type I fibers, with concentric circles of fibers expressing MHC-IIA, then MHC-IIX, and peripherally MHC-IIB. This study demonstrates that three adult fast Type II MHC isoproteins are expressed in skeletal muscle fibers of the llama. The general assumption that the very fast MHC-IIB isoform is expressed only in small mammals can be rejected. (J Histochem Cytochem 49:1033–1044, 2001)

Operation Everest II: adaptations in human skeletal muscle

1989 ◽  
Vol 66 (5) ◽  
pp. 2454-2461 ◽  
Author(s):  
H. J. Green ◽  
J. R. Sutton ◽  
A. Cymerman ◽  
P. M. Young ◽  
C. S. Houston
Keyword(s):  
Skeletal Muscle ◽  
Fiber Type ◽  
Vastus Lateralis ◽  
Succinic Dehydrogenase ◽  
High Energy ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Type Ii ◽  
Cross Sectional ◽  
Distribution Type

Adaptations in skeletal muscle in response to progressive hypobaria were investigated in eight male subjects [maximal O2 uptake = 51.2 +/- 3.0 (SE) ml.kg-1.min-1] over 40 days of progressive decompression to the stimulated altitude of the summit of Mt. Everest. Samples of the vastus lateralis muscle extracted before decompression (SL-1), at 380 and 282 Torr, and on return to sea level (SL-2) indicated that maximal activities of enzymes representative of the citric acid cycle, beta-oxidation, glycogenolysis, glycolysis, glucose phosphorylation, and high-energy phosphate transfer were unchanged (P greater than 0.05) at 380 and 282 Torr over initial SL-1 values. After exposure to 282 Torr, however, representing an additional period of approximately 7 days, reductions (P less than 0.05) were noted in succinic dehydrogenase (21%), citrate synthetase (37%), and hexokinase (53%) between SL-2 and 380 Torr. No changes were found in the other enzymes. Capillarization as measured by the number of capillaries per cross-sectional area (CC/FA) was increased (P less than 0.05) in both type I (0.94 +/- 0.8 vs. 1.16 +/- 0.05) and type II (0.84 +/- 0.07 vs. 1.05 +/- 0.08) fibers between SL-1 and SL-2. This increase was mediated by a reduction in fiber area. No changes were found in fiber-type distribution (type I vs. type II). These findings do not support the hypothesis, at least in humans, that, at the level of the muscle cell, extreme hypobaric hypoxia elicits adaptations directed toward maximizing oxidative function.

scholarly journals Dissociation between short-term unloading and resistance training effects on skeletal muscle Na+,K+-ATPase, muscle function, and fatigue in humans

2016 ◽  
Vol 121 (5) ◽  
pp. 1074-1086 ◽  
Author(s):  
Ben D. Perry ◽  
Victoria L. Wyckelsma ◽  
Robyn M. Murphy ◽  
Collene H. Steward ◽  
Mitchell Anderson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Resistance Training ◽  
Muscle Function ◽  
Fiber Type ◽  
Peak Torque ◽  
Quadriceps Muscle ◽  
Type I ◽  
Type Ii ◽  
Type I Fibers ◽  
Type Ii Fibers

Physical training increases skeletal muscle Na+,K+-ATPase content (NKA) and improves exercise performance, but the effects of inactivity per se on NKA content and isoform abundance in human muscle are unknown. We investigated the effects of 23-day unilateral lower limb suspension (ULLS) and subsequent 4-wk resistance training (RT) on muscle function and NKA in 6 healthy adults, measuring quadriceps muscle peak torque; fatigue and venous [K+] during intense one-legged cycling exercise; and skeletal muscle NKA content ([3H]ouabain binding) and NKA isoform abundances (immunoblotting) in muscle homogenates (α1-3, β1–2) and in single fibers (α1–3, β1). In the unloaded leg after ULLS, quadriceps peak torque and cycling time to fatigue declined by 22 and 23%, respectively, which were restored with RT. Whole muscle NKA content and homogenate NKA α1–3 and β1–2 isoform abundances were unchanged with ULLS or RT. However, in single muscle fibers, NKA α3 in type I (−66%, P = 0.006) and β1 in type II fibers (−40%, P = 0.016) decreased after ULLS, with other NKA isoforms unchanged. After RT, NKA α1 (79%, P = 0.004) and β1 (35%, P = 0.01) increased in type II fibers, while α2 (76%, P = 0.028) and α3 (142%, P = 0.004) increased in type I fibers compared with post-ULLS. Despite considerably impaired muscle function and earlier fatigue onset, muscle NKA content and homogenate α1 and α2 abundances were unchanged, thus being resilient to inactivity induced by ULLS. Nonetheless, fiber type-specific downregulation with inactivity and upregulation with RT of several NKA isoforms indicate complex regulation of muscle NKA expression in humans.

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