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At least 19 recordsLinked to original sources
PubMed2006

Blood vessels and desmin control the positioning of nuclei in skeletal muscle fibers.

Skeletal muscle fibers contain hundreds to thousands of nuclei which lie immediately under the plasmalemma and are spaced out along the fiber, except for a small cluster of specialized nuclei at the neuromuscular junction. How the nuclei attain their positions along the fiber is not understood. Here we show that the nuclei are preferentially localized near blood vessels (BV), particularly in slow-twitch, oxidative fibers. Thus, in rat soleus muscle fibers, 81% of the nuclei appear next to BV. Lack of desmin markedly perturbs the distribution of nuclei along the fibers but does not prevent their close association with BV. Consistent with a role for desmin in the spacing of nuclei, we show that denervation affects the organization of desmin filaments as well as the distribution of nuclei. During chronic stimulation of denervated muscles, new BV form, along which muscle nuclei align themselves. We conclude that the positioning of nuclei along muscle fibers is plastic and that BV and desmin intermediate filaments each play a distinct role in the control of this positioning.

Animals↗
PubMed2005

Control of slow myosin heavy chain 2 gene expression by glycogen synthase kinase activity in skeletal muscle fibers.

Skeletal muscle fiber type and expression of slow muscle fiber type specific genes are regulated by fiber type specific cell signaling events initiated by innervation. In avian muscle fibers, expression of the slow myosin heavy chain 2 (MyHC2) gene defines fast versus slow muscle fiber types, and its expression is dependent on the transcription factor, nuclear factor of activated T cells (NFAT). Glycogen synthase kinase 3 (GSK3) phosphorylates NFAT and inhibits its transactivating potential. We report here that expression of the slow MyHC2 gene is dependent on GSK3 activity. Inhibition of GSK3 activity by SB216763 or LiCl induced expression of the slow MyHC2 gene in non-innervated medial adductor (MA) muscle fibers and in innervated fast pectoralis major (PM) muscle fibers. Innervation of MA and PM muscle fibers did not significantly alter GSK3 activity. However, inhibition of GSK3 activity increased NFAT-mediated transcriptional activity, required for full activation of the slow MyHC2 gene, and overexpression of GSK3 reduced NFAT-mediated transcription. Inhibition of GSK3 activity was sufficient to induce slow MyHC2 gene expression in non-innervated MA muscle fibers but not in non-innervated PM muscle fibers, suggesting that fiber type specific mechanisms differentially regulate slow MyHC2 gene expression in innervated muscle fibers.

Animals↗
PubMed2002

Different modes of hypertrophy in skeletal muscle fibers.

Skeletal muscles display a remarkable diversity in their arrangement of fibers into fascicles and in their patterns of innervation, depending on functional requirements and species differences. Most human muscle fascicles, despite their great length, consist of fibers that extend continuously from one tendon to the other with a single nerve endplate band. Other mammalian muscles have multiple endplate bands and fibers that do not insert into both tendons but terminate intrafascicularly. We investigated whether these alternate structural features may dictate different modes of cell hypertrophy in two mouse gracilis muscles, in response to expression of a muscle-specific insulin-like growth factor (IGF)-1 transgene (mIGF-1) or to chronic exercise. Both hypertrophic stimuli independently activated GATA-2 expression and increased muscle cross-sectional area in both muscle types, with additive effects in exercising myosin light chain/mIGF transgenic mice, but without increasing fiber number. In singly innervated gracilis posterior muscle, hypertrophy was characterized by a greater average diameter of individual fibers, and centralized nuclei. In contrast, hypertrophic gracilis anterior muscle, which is multiply innervated, contained longer muscle fibers, with no increase in average diameter, or in centralized nuclei. Different modes of muscle hypertrophy in domestic and laboratory animals have important implications for building appropriate models of human neuromuscular disease.

Animals↗
PubMed1994

G protein effects on Ca2+ release and excitation-contraction coupling in skeletal muscle fibers.

Skeletal muscle excitation-contraction (EC) coupling may involve secondary mechanisms, such as those involving G proteins. The aim of this study was to identify possible G protein effects on sarcoplasmic reticulum (SR) Ca2+ release, in general, and on voltage-dependent EC coupling, in particular. Effects of guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S) were studied using a single peeled rabbit skeletal muscle fiber preparation that is capable of releasing SR Ca2+ in response to transverse tubule (TT) depolarization. Because of possible nonspecific and residual effects of 200 microM GTP gamma S, a lower concentration of 50 microM GTP gamma S was used to stimulate G proteins in the peeled fiber system. Under conditions for steady-state (resting) polarization of TT, GTP gamma S rarely elicited SR Ca2+ release. When the TTs are in steady-state (resting) depolarization, 50 microM GTP gamma S or GTP elicited SR Ca2+ release and associated tension transients in only 69% of fibers tested. In contrast GTP gamma S always augmented Ca2+ release during TT depolarization-induced EC coupling. These results indicate the presence of at least two excitatory G proteins for SR Ca2+ release, only one of which is a modulator, albeit nonessential, of peeled fiber EC coupling.

Animals↗
PubMed1981

Calcium transients in asymmetrically activated skeletal muscle fibers.

Skeletal muscle fibers of the frog Rana temporaria were held just taut and stimulated transversely by unidirectional electrical fields. We observed the reversible effects of stimulus duration (0.1-100 ms) and strength on action potentials, intracellular Ca2+ transients (monitored by aequorin), and contractile force during fixed-end contractions. Long duration stimuli (e.g., 10 ms) induced a maintained depolarization on the cathodal side of a cell and a maintained hyperpolarization on its anodal side. The hyperpolarization of the side facing the anode prevented the action potential from reaching mechanical threshold during strong stimuli. Variation of the duration or strength of a stimulus changed the luminescent response from a fiber injected with aequorin. Thus, the intracellular Ca2+ released during excitation-contraction coupling could be changed by the stimulus parameters. Prolongation of a stimulus at field strengths above 1.1 x rheobase decreased the amplitude of aequorin signals and the force of contractions. The decreases in aequorin and force signals from a given fiber paralleled one another and depended on the stimulus strength, but not on the stimulus polarity. These changes were completely reversible for stimulus strengths up to at least 4.2 x rheobase. The graded decreases in membrane depolarization, aequorin signals, and contractile force were correlated with the previously described folding of myofibrils in fibers allowed to shorten in response to the application of a long duration stimulus. The changes in aequorin signals and force suggest an absence of myofilament activation by Ca2+ in the section of the fiber closest to the anode. The results imply that injected aequorin distributes circumferentially in frog muscle with a coefficient of at least 10(-7) cm2/s, which is not remarkably different from the previously measured coefficient of 5 x 10(-8) cm2/s for its diffusion lengthwise.

Action Potentials↗
PubMed1993

[A comparative study of the structural state of skeletal muscle and smooth muscle fiber tropomyosin in ghost skeletal muscle fibers by a fluorescent probe method].

The structural state of skeletal muscle and smooth muscle fiber tropomyosins in ghost fibers of skeletal muscles has been studied by means of polarization microfluorimetry. Tropomyosins and F-actin of ghost fibers were labelled with N-(iodoacetyl)-N-(1-naphthyl-5-sulfo)-ethylenediamine (1,5-IA-EDANS) or the phalloidin-rhodamine complex, respectively. It has been found that skeletal tropomyosin bound to ghost muscle fibers is more flexible in comparison with smooth muscle tropomyosin. The flexibility of the thin filaments of the ghost fibers labelled in F-actin by the phalloidin-rhodamine complex and containing smooth muscle tropomyosin is higher than that of the thin filaments containing the bound skeletal muscle protein.

Animals↗
PubMed2004

Innervation-dependent and fiber type-specific transcriptional regulation of the slow myosin heavy chain 2 promoter in avian skeletal muscle fibers.

Skeletal muscle fiber type is regulated, in part, by innervation leading to transcriptional regulation of fiber type-specific genes. Here, we report the initial characterization of the transcriptional regulation of the slow myosin heavy chain 2 (MyHC2) promoter in innervated and noninnervated slow medial adductor (MA) and fast pectoralis major (PM) muscle fibers in cell culture. The proximal 1358 bp of slow MyHC2 upstream DNA contains a functional E-box and binding sites for myocyte enhancer factor 2 (MEF2) and nuclear factor of activated T cells (NFAT). Mutagenesis studies indicated that both MEF2 and NFAT binding sites are required for innervation-induced slow MyHC2 promoter activity in MA muscle fibers. However, MEF2 transcription factor activity was unaffected by innervation and did not demonstrate fiber type-specific interactions with the slow MyHC2 MEF2 binding site. NFAT transcription factor activity did increase in innervated MA muscle fibers and not in PM muscle fibers, indicating innervation and muscle fiber type-specific regulation. However, transfection of constitutively active NFAT indicated that NFAT is insufficient to induce slow MyHC2 gene expression in either fast PM or slow MA muscle fibers without innervation. These results indicate the requirement for MEF2 and NFAT in innervation-induced slow MyHC2 gene expression and suggest that additional innervation-dependent and fiber type-specific control of slow MyHC2 gene expression resides in MA and PM muscle fibers, respectively.

Animals↗
PubMed2006

Mitochondrial DNA-deletion mutations accumulate intracellularly to detrimental levels in aged human skeletal muscle fibers.

Skeletal muscle-mass loss with age has severe health consequences, yet the molecular basis of the loss remains obscure. Although mitochondrial DNA (mtDNA)-deletion mutations have been shown to accumulate with age, for these aberrant genomes to be physiologically relevant, they must accumulate to high levels intracellularly and be present in a significant number of cells. We examined mtDNA-deletion mutations in vastus lateralis (VL) muscle of human subjects aged 49-93 years, using both histologic and polymerase-chain-reaction (PCR) analyses, to determine the physiological and genomic integrity of mitochondria in aging human muscle. The number of VL muscle fibers exhibiting mitochondrial electron-transport-system (ETS) abnormalities increased from an estimated 6% at age 49 years to 31% at age 92 years. We analyzed the mitochondrial genotype of 48 single ETS-abnormal, cytochrome c oxidase-negative/succinate dehydrogenase-hyperreactive (COX-/SDH++) fibers from normal aging human subjects and identified mtDNA-deletion mutations in all abnormal fibers. Deletion mutations were clonal within a fiber and concomitant to the COX-/SDH++ region. Quantitative PCR analysis of wild-type and deletion-containing mtDNA genomes within ETS-abnormal regions of single fibers demonstrated that these deletion mutations accumulate to detrimental levels (>90% of the total mtDNA).

Aged↗
PubMed2002

The adaptive potential of skeletal muscle fibers.

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 glycolytic. 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.

Adaptation, Physiological↗
PubMed1993

Effects of pressure on equatorial x-ray fiber diffraction from skeletal muscle fibers.

When skeletal muscle fibers are subjected to a hydrostatic pressure of 10 MPa (100 atmospheres), reversible changes in tension occur. Passive tension from relaxed muscle is unaffected, rigor tension rises, and active tension falls. The effects of pressure on muscle structure are unknown: therefore a pressure-resistant cell for x-ray diffraction has been built, and this paper reports the first study of the low-angle equatorial patterns of pressurized relaxed, rigor, and active muscle fibers, with direct comparisons from the same chemically skinned rabbit psoas muscle fibers at 0.1 and 10 MPa. Relaxed and rigor fibers show little change in the intensity of the equatorial reflections when pressurized to 10 MPa, but there is a small, reversible expansion of the lattice of 0.7 and 0.4%, respectively. This shows that the order and stability of the myofilament lattice is undisturbed by this pressure. The rise in rigor tension under pressure is thus probably due to axial shortening of one or more components of the sarcomere. Initial results from active fibers at 0.1 MPa show that when phosphate is added the lattice spacing and equatorial intensities change toward their relaxed values. This indicates cross-bridge detachment, as expected from the reduction in tension that phosphate induces. 10 MPa in the presence of phosphate at 11 degrees C causes tension to fall by a further 12%, but not change is detected in the relative intensity of the reflections, only a small increase in lattice spacing. Thus pressure appears to increase the proportion of attached cross-bridges in a low-force state.

Animals↗
PubMed2000

Effects of dihydropyridine receptor II-III loop peptides on Ca(2+) release in skinned skeletal muscle fibers.

In skeletal muscle fibers, the intracellular loop between domains II and III of the alpha(1)-subunit of the dihydropyridine receptor (DHPR) may directly activate the adjacent Ca(2+) release channel in the sarcoplasmic reticulum. We examined the effects of synthetic peptide segments of this loop on Ca(2+) release in mechanically skinned skeletal muscle fibers with functional excitation-contraction coupling. In rat fibers at physiological Mg(2+) concentration ([Mg(2+)]; 1 mM), a 20-residue skeletal muscle DHPR peptide [A(S(20)); Thr(671)-Leu(690); 30 microM], shown previously to induce Ca(2+) release in a triad preparation, caused only small spontaneous force responses in approximately 40% of fibers, although it potentiated responses to depolarization and caffeine in all fibers. The COOH-terminal half of A(S(20)) [A(S(10))] induced much larger spontaneous responses but also caused substantial inhibition of Ca(2+) release to both depolarization and caffeine. Both peptides induced or potentiated Ca(2+) release even when the voltage sensors were inactivated, indicating direct action on the Ca(2+) release channels. The corresponding 20-residue cardiac DHPR peptide [A(C(20)); Thr(793)-Ala(812)] was ineffective, but its COOH-terminal half [A(C(10))] had effects similar to A(S(20)). In the presence of lower [Mg(2+)] (0.2 mM), exposure to either A(S(20)) or A(C(10)) (30 microM) induced substantial Ca(2+) release. Peptide C(S) (100 microM), a loop segment reported to inhibit Ca(2+) release in triads, caused partial inhibition of depolarization-induced Ca(2+) release. In toad fibers, each of the A peptides had effects similar to or greater than those in rat fibers. These findings suggest that the A and C regions of the skeletal DHPR II-III loop may have important roles in vivo.

Amino Acid Sequence↗
PubMed1999

Constitutively active MuSK is clustered in the absence of agrin and induces ectopic postsynaptic-like membranes in skeletal muscle fibers.

In skeletal muscle fibers, neural agrin can direct the accumulation of acetylcholine receptors (AChR) and transcription of AChR subunit genes from the subsynaptic nuclei. Although the receptor tyrosine kinase MuSK is required for AChR clustering, it is less clear whether MuSK regulates gene transcription. To elucidate the role of MuSK in these processes, we constructed a constitutively active MuSK receptor, MuSKneuTMuSK, taking advantage of the spontaneous homodimerization of the transmembrane domain of neuT, an oncogenic variant of the neu/erbB2 receptor. In the extrasynaptic region of innervated muscle fibers, MuSKneuTMuSK formed highly concentrated aggregates that colocalized with AChR clusters. Associated with MuSK-induced AChR clusters was a normal complement of synaptic proteins. Moreover, transcription of the AChR-epsilon subunit gene was increased, albeit via an indirect mechanism by MuSK-induced aggregation of erbB receptors and neuregulin. Although neural agrin was not required, the activity of MuSKneuTMuSK was nevertheless potentiated by ectopic expression of a muscle agrin isoform inactive in AChR clustering. To define the role of the kinase domain in the formation of a postsynaptic-like membrane, a second fusion receptor, neuneuTMuSK, which included the MuSK kinase but not the MuSK extracellular domain, was expressed. Significantly, neuneuTMuSK induced AChR clusters that colocalized with aggregates of endogenous MuSK. Taken together, it was concluded that the MuSK kinase domain is sufficient to initiate the recruitment of additional MuSK receptors, which then develop into highly concentrated aggregates by means of a positive feedback loop to induce a postsynaptic membrane in the absence of neural agrin.

Agrin↗
PubMed2001

Muscle activity and muscle agrin regulate the organization of cytoskeletal proteins and attached acetylcholine receptor (AchR) aggregates in skeletal muscle fibers.

In innervated skeletal muscle fibers, dystrophin and beta-dystroglycan form rib-like structures (costameres) that appear as predominantly transverse stripes over Z and M lines. Here, we show that the orientation of these stripes becomes longitudinal in denervated muscles and transverse again in denervated electrically stimulated muscles. Skeletal muscle fibers express nonneural (muscle) agrin whose function is not well understood. In this work, a single application of > or = 10 nM purified recombinant muscle agrin into denervated muscles preserved the transverse orientation of costameric proteins that is typical for innervated muscles, as did a single application of > or = 1 microM neural agrin. At lower concentration, neural agrin induced acetylcholine receptor aggregates, which colocalized with longitudinally oriented beta-dystroglycan, dystrophin, utrophin, syntrophin, rapsyn, and beta 2-laminin in denervated unstimulated fibers and with the same but transversely oriented proteins in innervated or denervated stimulated fibers. The results indicate that costameres are plastic structures whose organization depends on electrical muscle activity and/or muscle agrin.

Agrin↗
PubMed2006

Parallel mechanisms for resting nucleo-cytoplasmic shuttling and activity dependent translocation provide dual control of transcriptional regulators HDAC and NFAT in skeletal muscle fiber type plasticity.

Skeletal muscle fibers exhibit plasticity of their physiological and biochemical properties in response to the firing pattern from the innervating motor neuron. In particular, the gene expression pattern generally characteristic of a slow twitch fiber can be induced in a fast twitch fiber by chronic slow fiber type electrical stimulation. We have studied the nucleo-cytoplasmic distribution of two transcriptional regulators of slow fiber type genes, HDAC4 and NFATc1, both in response to slow fiber type stimulation and in resting conditions using cultured fast twitch skeletal muscle fibers. HDAC4 is present in both cytoplasm and nuclei of resting fibers, and moves out of the nuclei in response to slow fiber type stimulation. The stimulation-dependent nuclear efflux of HDAC4 requires activation of nuclear CaMKII, which phosphorylates nuclear HDAC4 and thus allows its exit of the nucleus. In unstimulated resting fibers, a balance of nuclear efflux and influx of HDAC4 establishes the resting level of nuclear HDAC4. However, the nuclear efflux of HDAC4 in resting fibers does not involve CaMKII. Slow fiber type stimulation also causes NFATc1 translocation from the cytoplasm into muscle fiber nuclei following dephosphorylation by calcineurin (CaN) activated by the elevated cytosolic Ca2+ accompanying fiber stimulation. In resting fibers, NFATc1 exhibits balanced shuttling between cytoplasm and nucleus, but during this shuttling NFATc1 influx does not require CaN and NFATc1 efflux does not require the kinases involved in removing nuclear NFATc1 following prior activity. Thus different enzymes are responsible for HDAC4 nuclear efflux in resting and active fibers, and different pathways mediate NFATc1 nuclear influx and efflux in resting and active fibers. Such dual mechanisms for resting shuttling and active movements provide the potential for the resting level and the rate of translocation during fiber stimulation to be controlled independently for both of the transcriptional regulators HDAC4 and NFATc1.

Animals↗
PubMed1995

Effects of high energy phosphates and L-arginine on the electrical parameters of ischemic-reperfused rat skeletal muscle fibers.

In skeletal muscle, 4 h of ischemia followed by 30 min of reperfusion depolarizes the fibers, markedly increases the Cl- and glibenclamide-sensitive K+ conductances and reduces the excitability of the fibers. The ischemia-reperfusion also significantly decreases the ATP content of the muscles. In the present work, the electrical parameters of reperfused extensor digitorum longus muscle of rats were measured in vitro at 30 degrees C, by a computerized two-intracellular microelectrode technique, before and after in vivo pretreatment with equimolar doses of phosphocreatine disodium salt tetrahydrate, phosphocreatine di-L-arginine salt and L-arginine hydrochloride. In the same experimental situations the ATP content of the muscles was also measured. Both phosphocreatine salts prevented the increase of membrane ion conductance due to muscle reperfusion by preloading the muscle fibers with extra ATP. Phosphocreatine disodium salt also prevented the depolarization and restored the normal excitability of the reperfused fibers. In contrast, phosphocreatine di-L-arginine salt did not restore the resting potential nor the excitability of the fibers, but it decreased the amplitude of the action potential by reducing the overshoot. The pretreatment with L-arginine also failed to protect the electrical parameters of the fibers from the ischemic-reperfusion insult. Furthermore, the L-amino acid produced a more pronounced reduction of the excitability of the fibers by increasing the threshold current needed to elicit an action potential and reducing it overshoot. The in vitro application of L-arginine to the muscle also reduced the overshoot of the action potential, suggesting a direct interaction of the L-amino acid with Na+ channels.

Action Potentials↗
PubMed1993

Skeletal muscle fiber hyperplasia.

Skeletal muscle enlargement in adult animals has been ascribed primarily to changes in fiber cross-sectional area (i.e., fiber hypertrophy); however, recent evidence from several laboratories suggests strongly that fiber hyperplasia contributes to muscle mass increases in adult animals and possibly human athletes. Scientists have used three models to study the cellular mechanisms of muscle enlargement: compensatory hypertrophy, stretch, and exercise. Each of these models has provided direct as well as indirect evidence supporting the occurrence of muscle fiber hyperplasia. Direct counts of muscle fibers using nitric acid digestion techniques have shown that both exercise and stretch overload result in significant increases (range = 9-52%) in fiber number. Indirect fiber counts using histological cross-sections have suggested fiber hyperplasia (range = 10-82%) in all three models. Additionally, the expression of embryonic myosin isoforms have provided indirect evidence for new fiber formation in stretch overloaded muscle. Furthermore, satellite cells have been shown to be involved in muscle fiber hyperplasia in stretch and exercise.

Animals↗
PubMed1997

Functional morphology of serially linked skeletal muscle fibers.

In the skeletal muscle fiber organization of many vertebrate muscles, serial arrangements or linkages of muscle fibers along the muscle or fascicle are commonly found. These serially linked muscle fibers employ distinct junctional morphologies from muscle to muscle. Notable are the end-to-end linkages of muscle fibers through tendinous intersections (TIs), where many fibers end onto a continuous connective tissue plate with folded terminations similar to myotendinous junctions. Besides this end-to-end linkage, overlapping linkages or arrangements occur among nonspanning fibers terminating intrafascicularly. These nonspanning fibers bear tapering terminations with direct cell-cell (myomuscular) junctions or without any specialized junctions. Despite their overlapping linkages or tapering profiles, nonspanning fibers maintain a uniform sarcomere length along the linked fibers, suggesting that the overlapping-linked nonspanning fibers are equivalent to the end-to-end linked fibers in their mechanical capacity. However, the junctional compliance could differ in their extracellular elastic components and their organization at junctional sites, e.g., direct mechanical (myomuscular) junctions vs. indirect linkages through connective tissue. Increasing evidence suggests that the elastic components, including muscle fibers as well as connective tissues, are more critical than previously thought for the mode and/or the efficiency of tension transmission among serially arranged fibers and thus for the mechanical properties of the muscle.

Animals↗
PubMed2002

Myonuclear domain size varies along the lengths of maturing skeletal muscle fibers.

In a skeletal muscle fiber, each myonucleus is responsible for gene expression in its surrounding cytoplasm. The region of cytoplasm associated with an individual myonucleus is termed myonuclear domain. However, little is known about domain size variation within individual muscle fibers. This study tests the hypothesis that myonuclear domains expressing neonatal myosin within end regions of maturing fibers will be smaller than domains elsewhere in the fibers. The model used is chicken pectoralis, where we have previously shown that during development repression of neonatal myosin radiates from the central region towards the fiber ends. Samples excised from birds aged nine through to 115 days after hatching were sectioned transversely. Using computer image analysis and immunocytochemistry, fiber profiles were classified as neonatal, transforming or adult. Each profile was also located in an adjacent dystrophin-labelled section, where myonuclei were visualized using haematoxylin and bisbenzamide. Variation in myonuclear length with age was not found to be significant (p = 0.925). Myonuclei were counted, and formulae used to calculate mean myonuclear domain size for each profile type. Myonuclear number/mm fiber was calculated to be adult (mean = 108.57 myonuclei/mm), transforming (65.82) and neonatal (25.23). Transforming profiles had significantly (p=0.027) more myonuclei/mm than neonatal, as did adult (p=0.005). Volume of cytoplasm/myonucleus was adult (mean = 16,132 microm3/myonucleus), transforming (12,899) and neonatal (8,130). Transforming and adult profiles had significantly (p<0.001) larger myonuclear domains than did neonatal profiles. Transforming and adult profiles did not differ in either myonuclei/mm (p=0.302) or volume of cytoplasm/myonucleus (p=0.413). This study demonstrates smaller domains at the terminal tips of maturing muscle fibers.

Animals↗