Myofibrillar Fraction Research Articles

Characterization of myofibrillar adenosine triphosphatase activity and liberation of actin from myofibrils upon heating chicken breast meat.

Denaturation of actin and myosin in myofibrils induced by heating at 50°C was investigated to reveal the mechanism of irreversible liberation of actin from myofibrils on heating at lower temperatures than conventional cooking. Denaturation of these proteins was determined by Mg2+ -ATPase (adenosine triphosphatase) and Ca2+ -ATPase activities. When minced meat was heated for 20min, actin was liberated accompanying denaturation of 80% of actin and 50%of myosin. Heating of the myofibrillar fraction (MFF) isolated from meat homogenate induced much slower denaturation of actin than myosin. When MFF was heated with sarcoplasmic fractions, denaturation of actin was facilitated, suggesting that sarcoplasmic fractions contain factors to facilitate actin denaturation. Inosine-5'-monophosphate, a component of sarcoplasmic fractions, was shown to have no effect on actin and myosin denaturation. These results suggest that heating meat at 50°C dissociates binding ('Bond A') between actin and myosin participating in ATPaseactivities, resulting in denaturation of both proteins under influence of sarcoplasmic components. Although denaturation of actin and myosin disrupted Bond A, actin was not liberated simultaneously, suggesting the presence of another bond ('Bond B', more heat-stable than Bond A) between both proteins and necessity of disruption of Bond B for actin release from myofibrils.

Enhanced skeletal muscle regrowth and remodelling in massaged and contralateral non-massaged hindlimb.

Muscle fibre cross sectional area is enhanced with massage in the form of cyclic compressive loading during regrowth after atrophy. Massage enhances protein synthesis of the myofibrillar and cytosolic, but not the mitochondrial fraction, in muscle during regrowth. Focal adhesion kinase activation and satellite cell number are elevated in muscles undergoing massage during regrowth. Muscle fibre cross sectional area and protein synthesis of the myofibrillar fraction, but not DNA synthesis, are elevated in muscle of the contralateral non-massaged limb. Massage in the form of cyclic compressive loading is a potential anabolic intervention during muscle regrowth after atrophy. Massage, in the form of cyclic compressive loading (CCL), is associated with multiple health benefits, but its potential anabolic effect on atrophied muscle has not been investigated. We hypothesized that the mechanical activity associated with CCL induces an anabolic effect in skeletal muscle undergoing regrowth after a period of atrophy. Fischer-Brown Norway rats at 10months of age were hindlimb unloaded for a period of 2weeks. The rats were then allowed reambulation with CCL applied at a 4.5N load at 0.5Hz frequency for 30min every other day for four bouts during a regrowth period of 8days. Muscle fibre cross sectional area was enhanced by 18% with massage during regrowth compared to reloading alone, and this was accompanied by elevated myofibrillar and cytosolic protein as well as DNA synthesis. Focal adhesion kinase phosphorylation indicated that CCL increased mechanical stimulation, while a higher number of Pax7+ cells likely explains the elevated DNA synthesis. Surprisingly, the contralateral non-massaged limb exhibited a comparable 17% higher muscle fibre size compared to reloading alone, and myofibrillar protein synthesis, but not DNA synthesis, was also elevated. We conclude that massage in the form of CCL induces an anabolic response in muscles regrowing after an atrophy-inducing event. We suggest that massage can be used as an intervention to aid in the regrowth of muscle lost during immobilization.

The effect of CaCl2 marination on the tenderizing pathway of goose meat during conditioning

In order to figure out the effect of CaCl2 on the tenderizing pathway of goose meat, breast muscles of thirty-two Eastern Zhejiang White Geese were divided into three treatments: the control, 150 and 300mM CaCl2. Shear force, myofibrillar fraction index (MFI), actin filaments and F-actin, G-actin and tropomodulins (Tmods) levels were investigated during 168h. Results showed that 300mM treatment had lower shear force at 48, 96 and 168h and higher MFI at 24, 48, 96 and 168h than the control. The rate of actin filaments disruption, the decrease of F-actin, the degradation of Tmods, the increase of G-actin in 300mM treatment was faster than 150mM treatment; the rate in the control was the slowest among treatments. CaCl2 accelerated the transformation of F-actin into G-actin. We concluded that CaCl2 tenderized goose meat by depolymerizing actin filaments and cleaving Tmods.

Proteomic approach to investigate the impact of different dietary supplementation on lamb meat tenderness

The aim of this study was to evaluate the effect of dietary supplementation of linseed and/or quinoa on tenderness and on proteome of lamb meat. Thirty-two Italian Merino lambs were distributed into 4 groups with different diet: control (CO) with no supplemental fat, linseed (LS), quinoa (QS) and QS+LS diets. Meat obtained by lamb fed linseed showed the lowest values of WBSF (P<0.001), hardness (P<0.01), gumminess (P<0.01) and chewiness (P<0.01). Proteomic changes of myofibrillar and sarcoplasmic proteins were estimated with SDS-PAGE, Western Blot and Two-Dimensional Gel Electrophoresis. In linseed group proteomic analysis revealed a degradation of desmin and TnT proteins complex and a major number of spots and phosphorylation isoforms of fast MLC2 patterns. Meat obtained by lamb fed quinoa showed a minor effect on the instrumental evaluation of meat tenderness and a major number of spots ascribed to sarcoplasmic proteins and fMHC. Data suggest that dietary supplementation may act on meat tenderness and on proteolytic pattern of myofibrillar fraction.

Influence of Nrf2 activators on subcellular skeletal muscle protein and DNA synthesis rates after 6weeks of milk protein feeding in older adults.

In older adults, chronic oxidative and inflammatory stresses are associated with an impaired increase in skeletal muscle protein synthesis after acute anabolic stimuli. Conjugated linoleic acid (CLA) and Protandim have been shown to activate nuclear factor erythroid-derived 2-like 2 (Nrf2), a transcription factor for the antioxidant response element and anti-inflammatory pathways. This study tested the hypothesis that compared to a placebo control (CON), CLA and Protandim would increase skeletal muscle subcellular protein (myofibrillar, mitochondrial, cytoplasmic) and DNA synthesis in older adults after 6weeks of milk protein feeding. CLA decreased oxidative stress and skeletal muscle oxidative damage with a trend to increase messenger RNA (mRNA) expression of a Nrf2 target, NAD(P)H dehydrogenase quinone 1 (NQO1). However, CLA did not influence other Nrf2 targets (heme oxygenase-1 (HO-1), glutathione peroxidase 1 (Gpx1)) or protein or DNA synthesis. Conversely, Protandim increased HO-1 protein content but not the mRNA expression of downstream Nrf2 targets, oxidative stress, or skeletal muscle oxidative damage. Rates of myofibrillar protein synthesis were maintained despite lower mitochondrial and cytoplasmic protein syntheses after Protandim versus CON. Similarly, DNA synthesis was non-significantly lower after Protandim compared to CON. After Protandim, the ratio of protein to DNA synthesis tended to be greater in the myofibrillar fraction and maintained in the mitochondrial and cytoplasmic fractions, emphasizing the importance of measuring both protein and DNA synthesis to gain insight into proteostasis. Overall, these data suggest that Protandim may enhance proteostatic mechanisms of skeletal muscle contractile proteins after 6weeks of milk protein feeding in older adults.

The effect of Cytochalasin B and Jasplakinolide on depolymerization of actin filaments in goose muscles during postmortem conditioning

Breast muscles of twenty-four Eastern Zhejiang White Geese were randomly divided into three groups: control, Cytochalasin B (Cyt B) and Jasplakinolide (Jasp) treatments during postmortem conditioning. The myofibrillar fraction index (MFI), actin filaments and the levels of F-actin, G-actin and actin associated proteins (cofilins and tropomodulins) during conditioning were investigated. In control, the degraded tropomodulins, increased G-actin and disrupted actin filaments were observed at 4 and 7days; the increase of MFI and decrease of F-actin content were shown during conditioning. Cyt B treatments accelerated the transformation from F-actin to G-actin, weakened actin filaments and increased MFI compared to the control, while Jasp gained the opposite effect against Cyt B. We concluded that depolymerization of actin filaments regulated by tropomodulins contributed to myofibrillar fraction during conditioning. This work provided a new pathway of tenderization by the depolymerization of actin filaments.

Influence of transport conditions and pre-slaughter water shower spray during summer on protein characteristics and water distribution of broiler breast meat.

This study investigated the effects of pre-slaughter transport during summer and subsequent water shower spray on broiler meat quality and protein characteristics. Arbor Acres broiler chickens (n = 126, 42 days old, mixed sex, 2.5-3 kg) were randomly categorized into three treatments: (i) control group without transport (C); (ii) 30 min transport (T); and (iii) 30 min transport followed by 10 min water shower spray and 20 min lairage (T/W). Each treatment consisted of six replicates with seven birds each. Ambient temperature was 32-35°C during transportation. Results indicated that transport during high ambient temperature denatured myosin and sarcoplasmic proteins, led to decreased protein solubility and resulted in glycogen phosphorylase precipitated to the myofibrillar fraction. Furthermore, meat quality in the transport group showed a pale, soft and exudative (PSE)-like syndrome. Water shower spray during lairage after transport reduced the degree of protein denaturation and lessened the deterioration of meat quality.

Changes in Myofibrillar and Sarcoplasmic Proteins in Salami Processing Added withLactobacillus Sakei/Staphylococcus CarnosusAccording to Modulated Differential Scanning Calorimetry and the Color Profile

Changes in the thermal and color profiles of the sarcoplasmic and myofibrillar protein fractions were analyzed during the fermentation and ripening processes of salami added with Lactobacillus sakei and Staphylococcus carnosus using modulated differential scanning calorimetry, CIELAB and reflectance. The results of the pre and postfermentation stages for the myofibrillar and sarcoplasmic fractions showed a decrease in transition temperatures (Tm) without variation in the degradation enthalpy (ΔHd). Thus, the sarcoplasmic protein fraction in these stages showed Cp values between 0.18 and 1.0 J/gC while for myofibrillar was 0.22 and 0.07 J/gC. However, in the postripening stage, the ΔHd increased to 364.1 J/g for myofibrillar fraction and 1292 J/g for sarcoplasmic fractions. Seventh day corresponds to the turning point in L*, a decreasing trend was observed in L* and the reflectance percentage in postripening stage, which can reflect structural changes in proteins. Practical Applications This study facilitates a comparison of the changes in sarcoplasmic and myofibrillar protein fractions during three stages of salami processing, correlating these changes with the bacterial population dynamics focused on the behavior of a starter culture, pH and aw. Likewise, the possibility of using a methodology such as modulated differential scanning calorimetry and color to analyze protein changes in a complex matrix such as salami is intriguing.

Influence of starter cultures and KCl on some biochemical, microbiological and sensory features of soppressata molisana, an Italian fermented sausage

The effect of a multiple strain starter (KSL: Kocuria varians, Staphylococcus xylosus and Lactobacillus sakei) on the quality of soppressata molisana was investigated during 50 days of ripening. When compared with control batches (C, traditional production without starter and KS, addition of K. varians and S. xylosus as starter), soppressata produced with KSL showed positive results in terms of proteolysis progression, reduction of biogenic amines (BA) and sensory features. The partial substitution of 50 % NaCl with 50 % KCl further improved the quality of soppressata molisana produced with KSL as starter. In fact, the K+ ions seemed to stimulate the growth of added bacteria, with a resulting additional lowering of the pH and BA formation, and higher proteolysis. Moreover, the addition of KCl did not alter the sensory profile of final products. The analysis of data collected during the fermentation and the drying phases, which followed one other, allowed the individuation of different proteolytic events. Specifically, the proteolysis of the myofibrillar fraction occurred more slowly than that of the sarcoplasmic one. Also, the analysis of fractionated muscle proteins allowed to appreciate that sarcoplasmic proteins were hydrolyzed by both endogenous and microbial enzymes, whereas myofibrillar proteins showed a higher resistance to microbial enzymes, and were primarily hydrolyzed by endogenous ones. In conclusion the combined use of KSL and KCl as partial substitute of NaCl, allowed the production of soppressata molisana having an excellent quality, and features consistent with the guidelines of WHO on the sodium and potassium intake.

Sumoylated α-skeletal muscle actin in the skeletal muscle of adult rats.

Skeletal muscles are composed of two major muscle fiber types: slow-twitch oxidative fibers and fast-twitch glycolytic fibers. The proteins in these muscle fibers are known to differ in their expression, relative abundance, and post-translational modifications. In this study, we report a previously unreported post-translational modification of α-skeletal muscle actin in the skeletal muscles of adult male F344 rats in vivo. Using two-dimensional electrophoresis (2D-PAGE), we first examined the differences in the protein expression profiles between the soleus and plantaris muscles. We found higher intensity protein spots at approximately 60kDa and pH 9 on 2D-PAGE for the soleus muscle compared with the plantaris muscle. These spots were identified as α-skeletal muscle actin by liquid chromatography-nanoelectrospray ionization-tandem mass spectrometry and western blot analyses. In addition, we found that the 60kDa α-skeletal muscle actin is modified by small ubiquitin-like modifier (SUMO) 1, using 2D-PAGE and western blot analyses. Furthermore, we found that α-skeletal muscle actin with larger molecular weight was localized in the nuclear and cytosol of the skeletal muscle, but not in the myofibrillar fraction by the combination of subcellular fractionation and western blot analyses. These results suggest that α-skeletal muscle actin is modified by SUMO-1 in the skeletal muscles, localized in nuclear and cytosolic fractions, and the extent of this modification is much higher in the slow muscles than in the fast muscles. This is the first study to show the presence of SUMOylated actin in animal tissues.

In-depth characterisation of the lamb meat proteome from longissimus lumborum

Lamb is one of the major red meats consumed globally, both as a key component in the diet of some countries, and as a niche meat product in others. Despite this relatively wide consumption, an in-depth description of the global protein composition of lamb has not been reported. In this study, we investigated the proteome of the 48h post-mortem lamb longissimus lumborum through separation of the samples into sarcoplasmic, myofibrillar and insoluble fractions, followed by an in-depth shotgun proteomic evaluation and bioinformatic analysis. As a result, 388 ovine-specific proteins were identified and characterised. The 207 proteins found in the sarcoplasmic fraction were dominated by glycolytic enzymes and mitochondrial proteins. This fraction also contained several sarcomeric proteins, e.g., myosin light chains and titin. Some of them might be the degradation products from the post-mortem proteolysis. Actin, myosin and tropomyosin were abundant in the myofibrillar fraction while nebulin and titin were also present. Collagen type I, III and IV were found in the insoluble fraction but there were also sequences from myosin and titin. The present study also confirms the existence of at least 300 predicted protein sequences obtained from the latest issue of the sheep genome (version 3) with high confidence.

Effects of vacuum and modified atmosphere on textural parameters and structural proteins of cultured meagre (Argyrosomus regius) fillets.

The influence of two preservation strategies (vacuum package and modified atmosphere package) on the post-mortem changes of textural parameters, pH, water holding capacity, sarcoplasmic and myofibrillar proteins, and collagen content of meagre (Argyrosomus regius) fillets was studied. Fillets were stored in a cold room in aerobic (control, C), vacuum (V) and modified atmosphere (MA) package. Samples were withdrawn at six sampling points throughout 15-day storage, and post-mortem changes were assessed. The textural parameters were significantly enhanced in V and MA compared to C. Both V and MA treatments reduced the intensity of a group of myofibrillar protein fractions (140-195 kDa) and increased insoluble collagen compared to C. Consequently, the post-mortem flesh softening in C was attributed to increased proteolysis in both intracellular and extracellular structural proteins. The preservation of the textural and biochemical characteristics of meagre fillets subjected to V and MA treatments makes these two treatments highly recommendable for the commercialization of meagre fillets.

Gelation Characteristics of Surimi Gel from Silver Carp (Hypophthalmichthys molitrix) by Application of Acid-Alkali Processes

Textural characteristics of silver carp surimi gel prepared from acid- and alkali-produced protein isolates were investigated and compared to the surimi gels derived by conventional methods. The acid-aided method showed the most efficiency to recover proteins (86.2%) in comparison to the alkaline-aided (79.8%) and conventional (76.7%) methods. In the washing of fish mince, every step resulted in reduction of sarcoplasmic protein, and consequently the myofibrillar fraction became more concentrated, as shown by the protein patterns in wash water. Some myofibrillar proteins (mainly actin and myosin) were removed along with sarcoplasmic proteins during washing, reducing yield efficiency during the conventional method of making surimi. During the pH shifting process, myosin heavy chain (MHC) was degraded during low (2.5) pH solubilization, whereas there was only a minimal loss of MHC by either hydrolysis or proteolysis during alkaline solubilization. The breaking force and breaking distance of surimi gel prepared in the pH-shifting processes were significantly (p < 0.05) greater than those of surimi gel made by conventional methods, as were expressible moisture, cohesiveness, and springiness. In conclusion, the pH-shifting technique can be considered as an efficient alternative process in recovery of greater quantities of functional protein from silver carp fillet.

The effect of high hydrostatic pressure on the muscle proteins of rainbow trout (Oncorhynchus mykiss Walbaum) fillets wrapped with chitosan-based edible film during cold storage (4±1°C)

This study was to determine the effects of changes that occurred in the muscle proteins of fresh rainbow trout (Oncorhynchus mykiss) fillets during storage at 4±1°C as a result of packaging in vacuum (C), subject to high pressure after packaging in vacuum high hydrostatic pressue (HHP), packaged in vacuum after wrapping with chitosan film (CFW) and subject to high pressure after wrapping with chitosan-based film and packaged in vacuum (HHP+CFW ). Samples were subjected to SDS-PAGE in four-day intervals and the densitometric analyses of the gels were carried out. According to the results, minor changes were determined in the major bands of the sarcoplasmic and myofibrillar muscle fractions of trouts as a result of HHP application and CFW. The most important change occurred in the myofibrillar muscle fraction as a decrease in the densities of the bands at 200 and 31.4 kDa after HHP application. Similarly, the sarcoplasmic muscle fraction of trout fillet decreased in the densities of the bands at 39.3, 26.6 and 23.3 kDa after HHP application. In addition, it is thought that the bands that occur at 30 kDa in the myofibrillar muscle fraction and at 20.7 kDa at the sarcoplasmic muscle fraction may be related with the degradation of trouts during cold storage.

Mechanisms of radical formation in beef and chicken meat during high pressure processing evaluated by electron spin resonance detection and the addition of antioxidants

The generation of radicals during high pressure (HP) processing of beef loin and chicken breast was studied by spin trapping and electron spin resonance detection. The pressurization resulted in a higher level of spin adducts in the beef loin than in the chicken breast. It was shown that radicals were formed in the sarcoplasmic and myofibrillar fractions as well as in the non-soluble protein fraction due to the HP treatment, indicating that other radicals than iron-derived radicals were formed, and most likely protein-derived radicals. The addition of iron as well as the natural antioxidants caffeic acid, rosemary extract, and ascorbic acid resulted in an increased formation of radicals during the HP treatment, whereas addition of ethylendiamintetraacetic acid (EDTA) reduced the radical formation. This suggests that iron-species (protein-bound or free) catalyses the formation of radicals when meat systems are submitted to HP.

Effect of pre-rigor temperature incubation on sarcoplasmic protein solubility, calpain activity and meat properties in porcine muscle

The aim of the study was to investigate the effect of pre-rigor temperature incubation on sarcoplasmic protein characteristics in relation to meat properties within porcine muscle. Porcine Longissimus dorsi muscles were incubated at temperatures of 0, 10, 20, 30 and 40 °C to 6 h post mortem. Incubation at 40 °C induced a significant decrease of sarcoplasmic protein solubility and an increase in proteins in the myofibrillar fraction. The protein relocation was followed till 72 h post mortem but had largely been completed by the end of the temperature incubation at 6 h. SDS-PAGE and Western blot analyses suggested that phosphorylase and creatine kinase precipitated onto the myofilaments during incubation at 40 °C. Drip loss increased following incubation at 40 °C, indicating that the precipitation of phosphorylase and creatine kinase may be a factor of reduced water-holding capacity at the combination of high temperature and low pH. Incubation at 40 °C resulted in substantially lower shear force in parallel with loss of extractable activity of μ- and m-calpain, suggesting a rapid activation of both enzymes at high temperatures and low pH early post mortem.

High pressure treatment of brine enhanced pork semitendinosus: Effect on microbial stability, drip loss, lipid and protein oxidation, and sensory properties

Abstract The microbiological stability, the meat and sensory quality of high pressure treated (600 MPa for 6 min) brine enhanced pork semitendinosus was evaluated during 8 weeks at 2 °C. Microbial growth was not observed, thus 600 MPa ensured a microbial shelf life of 8 weeks. Drip-loss was significantly reduced after HP treatment and remained low during storage indicating no further release of meat juice from the meat. Lipid oxidation, monitored as TBARS, remained lower than the sensorial unacceptable limit. Pressure did not affect the content of free thiol groups in the sarcoplasmic and myofibrillar protein fractions, whereas the storage resulted in a decrease in the sarcoplasmic fraction and an increase in the myofibrillar fraction. Western blotting revealed that some proteins were oxidized before HP treatment and the pressurization caused an increase in oxidation of certain proteins. SDS-PAGE profiles showed major changes of the protein structures due to the pressurization but not during storage. The sensory characteristics were not affected much by the pressure treatment or during storage. Industrial relevance High pressure can produce meat products with long shelf-life without compromising the meat and sensory quality. Meat quality, monitored as drip loss, lipid and protein oxidation, and protein modification, did change due to the pressure treatment or during the subsequent storage, but had no effect in the sensory assessment.

Effects of leucine and its metabolite β‐hydroxy‐β‐methylbutyrate on human skeletal muscle protein metabolism

Maintenance of skeletal muscle mass is contingent upon the dynamic equilibrium (fasted losses–fed gains) in protein turnover. Of all nutrients, the single amino acid leucine (Leu) possesses the most marked anabolic characteristics in acting as a trigger element for the initiation of protein synthesis. While the mechanisms by which Leu is ‘sensed’ have been the subject of great scrutiny, as a branched-chain amino acid, Leu can be catabolized within muscle, thus posing the possibility that metabolites of Leu could be involved in mediating the anabolic effect(s) of Leu. Our objective was to measure muscle protein anabolism in response to Leu and its metabolite HMB. Using [1,2-13C2]Leu and [2H5]phenylalanine tracers, and GC-MS/GC-C-IRMS we studied the effect of HMB or Leu alone on MPS (by tracer incorporation into myofibrils), and for HMB we also measured muscle proteolysis (by arteriovenous (A–V) dilution). Orally consumed 3.42 g free-acid (FA-HMB) HMB (providing 2.42 g of pure HMB) exhibited rapid bioavailability in plasma and muscle and, similarly to 3.42 g Leu, stimulated muscle protein synthesis (MPS; HMB +70%vs. Leu +110%). While HMB and Leu both increased anabolic signalling (mechanistic target of rapamycin; mTOR), this was more pronounced with Leu (i.e. p70S6K1 signalling ≤90 min vs. ≤30 min for HMB). HMB consumption also attenuated muscle protein breakdown (MPB; −57%) in an insulin-independent manner. We conclude that exogenous HMB induces acute muscle anabolism (increased MPS and reduced MPB) albeit perhaps via distinct, and/or additional mechanism(s) to Leu.

High early post-mortem temperature induces activation of AMP-activated protein kinase and development of pale, soft and exudative characteristics in turkey muscles

This study investigated the effect of early post-mortem temperature on development of a turkey muscle's pale, soft and exudative (PSE) characteristics. Muscles obtained at 20min post-mortem were incubated at 0, 20 and 40°C until 4h post-mortem and then stored at 4°C. During incubation, the 40°C group had greater rate of pH decline, lactate accumulation and R-values increase than other groups. Moreover, AMP-activated protein kinase (AMPK) activation at 1h post-mortem was higher in the 40°C group than the other groups. At 24h post-mortem, the 40°C group had higher L* values and drip loss; SDS-PAGE and western blotting indicated that lower protein solubility (sarcoplasmic, myofibrillar) in the 40°C group resulted from phosphorylase denaturation and further adhere to myofibrillar fraction. These results suggest that high temperature early post-mortem could induce AMPK activation, which results in rapid glycolysis, thus affecting protein solubility and generating PSE characteristics.

Aging and Regenerative Capacity of Skeletal Muscle in Rats

The objective of the study was to examine skeletal muscle regeneration capacity of young and very old rats during autotransplantation. In 3.5 and 30 month-old Wistar rats, gastrocnemius muscle was removed and grafted back to its original bed. Incorporation of 3H leucine into myofibrillar and sarcoplasmic protein fractions, their relative contents in autografts and synthesis rate of MyHC and actin were recorded. The relative muscle mass of old rats was about 67% of that of young rats; the absolute mass of autografted muscle was 61% intact in the young rat group and 51% in the old rat group. Content of myofibrillar protein in the autografts of young rats was 46% of the intact muscle content, and 39% in the old rat group. In conclusion, the difference in skeletal muscle regeneration capacity of young and very old rats is about ten percent. In the autografts of both young and old rats, the regeneration of the contractile apparatus is less effective in comparison with the sarcoplasmic compartment.