scholarly journals Impact of different temperature stimuli on the expression of myosin heavy chain isoforms during recovery from bupivacaine-induced muscle injury in rats

2019 ◽  
Vol 127 (1) ◽  
pp. 178-189
Author(s):  
Tsubasa Shibaguchi ◽  
Mizuki Hoshi ◽  
Toshinori Yoshihara ◽  
Hisashi Naito ◽  
Katsumasa Goto ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Heat Stress ◽  
Myosin Heavy Chain ◽  
Muscle Mass ◽  
Heavy Chain ◽  
Muscle Injury ◽  
Heat Exposure ◽  
Control Level ◽  
Male Wistar Rats ◽  
The Impact

Limited information exists regarding the impact of different temperature stimuli on myosin heavy chain (MyHC) expression in skeletal muscle during recovery from injury. Therefore, this experiment investigated the impact of both cold and heat exposure on the MyHC isoform profile in the rat soleus during recovery from injury. Male Wistar rats were randomly divided into control, bupivacaine-injected (BPVC), BPVC with icing, and BPVC with heat stress groups. Muscle injury was induced by intramuscular injection of bupivacaine into soleus muscles of male Wistar rats. Icing treatment (0°C for 20 min) was performed immediately after the injury. Intermittent heat stress (42°C for 30 min on alternating days) was carried out during 2–14 days after bupivacaine injection. In response to injury, a transient increase in developmental, IId/x, and IIb MyHC isoforms, as well as various types of hybrid fibers, followed by the recovery of the MyHC profile toward the control level, was noted in the regeneration of the soleus. The restoration of the MyHC profile in the regenerating muscle at whole-muscle and individual myofiber levels was partially delayed by icing but facilitated by heat stress. In addition, the application of repeated heat stress promoted the recovery of soleus muscle mass toward the control level following injury. We conclude that compared with acute and immediate cold (icing) treatment, chronic and repeated heat stress may be a more appropriate treatment for the enhancement of both normalization of the MyHC profile and restoration of muscle mass following injury. NEW & NOTEWORTHY Cold exposure (icing), but not heat exposure, has been well accepted as a first-aid treatment for accidental and/or sports-related injuries. However, recent evidence suggests the negative impact of icing treatment on skeletal muscle regeneration following injury. Here, we demonstrated that acute/immediate icing treatment delayed the restoration of the myosin heavy chain (MyHC) profile, but intermittent hyperthermia, repeated for several days, facilitated the recovery of both muscle mass and the MyHC profile in the regeneration of skeletal muscle following injury.

Pretranslational markers of contractile protein expression in human skeletal muscle: effect of limb unloading plus resistance exercise

2005 ◽  
Vol 98 (1) ◽  
pp. 46-52 ◽  
Author(s):  
F. Haddad ◽  
K. M. Baldwin ◽  
P. A. Tesch
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Molecular Markers ◽  
Resistance Exercise ◽  
Myosin Heavy Chain ◽  
Muscle Mass ◽  
Heavy Chain ◽  
Protein Gene ◽  
Contractile Protein ◽  
Mrna Levels

Previously, it has been shown that the human ground-based model consisting of unilateral limb suspension (ULLS) induces atrophy and reduced strength of the affected quadriceps muscle group. Resistance exercise (RE) involving concentric-eccentric actions, in the face of ULLS, is effective in ameliorating these deficits. The goal of the present study was to determine whether alterations in contractile protein gene expression, e.g., myosin heavy chain and actin, as studied at the pretranslational level, provide molecular markers concerning the deficits that occur in muscle mass/volume during ULLS, as well as its maintenance in response to ULLS plus RE. Muscle biopsies were obtained from the vastus lateralis muscle of 31 middle-aged men and women before and after 5 wk of ULLS, ULLS plus RE, or RE only. The RE paradigm consisted of 12 sessions of 4 sets of 7 concentric-eccentric knee extensions. Our findings show that there were net deficits in total RNA, total mRNA, and actin and myosin heavy chain mRNA levels of expression after ULLS ( P < 0.05), whereas these alterations were blunted in the two groups receiving RE. Additional observations involving IGF-I and its associated receptor and binding proteins suggest that RE postures the skeletal muscle for signaling processes that favor a greater anabolic state relative to that observed in the ULLS group. Collectively, these findings suggest that molecular markers of contractile protein gene expression serve as useful subcellular indicators for ascertaining the underlying mechanisms regulating alterations in muscle mass in human subjects in response to altered loading states.

scholarly journals AMPK Mediates Muscle Mass Change But Not the Transition of Myosin Heavy Chain Isoforms during Unloading and Reloading of Skeletal Muscles in Mice

2018 ◽  
Vol 19 (10) ◽  
pp. 2954 ◽  
Author(s):  
Tatsuro Egawa ◽  
Yoshitaka Ohno ◽  
Ayumi Goto ◽  
Shingo Yokoyama ◽  
Tatsuya Hayashi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Muscle Mass ◽  
Heavy Chain ◽  
Fiber Type ◽  
Dominant Negative ◽  
Hindlimb Unloading ◽  
Mass Change ◽  
Muscle Weight ◽  
Myhc Isoforms

5′AMP-activated protein kinase (AMPK) plays an important role in the regulation of skeletal muscle mass and fiber-type distribution. However, it is unclear whether AMPK is involved in muscle mass change or transition of myosin heavy chain (MyHC) isoforms in response to unloading or increased loading. Here, we checked whether AMPK controls muscle mass change and transition of MyHC isoforms during unloading and reloading using mice expressing a skeletal-muscle-specific dominant-negative AMPKα1 (AMPK-DN). Fourteen days of hindlimb unloading reduced the soleus muscle weight in wild-type and AMPK-DN mice, but reduction in the muscle mass was partly attenuated in AMPK-DN mice. There was no difference in the regrown muscle weight between the mice after 7 days of reloading, and there was concomitantly reduced AMPKα2 activity, however it was higher in AMPK-DN mice after 14 days reloading. No difference was observed between the mice in relation to the levels of slow-type MyHC I, fast-type MyHC IIa/x, and MyHC IIb isoforms following unloading and reloading. The levels of 72-kDa heat-shock protein, which preserves muscle mass, increased in AMPK-DN-mice. Our results indicate that AMPK mediates the progress of atrophy during unloading and regrowth of atrophied muscles following reloading, but it does not influence the transition of MyHC isoforms.

PSIII-11 Evaluating the Performance of Grow-finish Pigs Supplemented with Butipearl® Z and Kemtrace® Chromium During Natural Heat Stress Exposure

2021 ◽  
Vol 99 (Supplement_1) ◽  
pp. 174-174
Author(s):  
Mark Knauer ◽  
Venkatesh Mani ◽  
Tom Marsteller ◽  
Vanessa Iseri ◽  
Brian Kremer
Keyword(s):  
Heat Stress ◽  
Feed Intake ◽  
Heat Exposure ◽  
Muscle Growth ◽  
Negative Control ◽  
Intestinal Damage ◽  
Intestinal Health ◽  
Negative Effects ◽  
Curvilinear Relationships ◽  
The Impact

Abstract Heat stress (HS) severely impacts swine leading to compromised barrier integrity, diminished intestinal health and decreased performance. ButiPEARL® Z (BPZ) is an encapsulated formulation of zinc and butyrate shown to alleviate the impact of HS by improving intestinal health. KemTRACE® Chromium (KTCr) is an organic trace mineral shown to decrease the impact of stress and improve glucose utilization, leading to muscle growth and improved performance. To test the efficacy of BPZ and KTCr on mitigating stress from natural heat exposure, a grow-finish trial was conducted from June-September. There were four treatments: negative control (NC), NC+.45kg BPZ, NC+.91kg BPZ and NC+1.82kg BPZ. Three BPZ treatments were also supplemented with 200ppb KTCr. Pigs (n=480) were randomly assigned to 96 pens at 22.5kg. Performance was measured at d0, 28, 56 and at marketing. From d56 to market, ADFI was greater (P&lt; 0.05) for 0.45kg and 0.91kg BPZ when compared to NC and 1.82kg BPZ (3.40 and 3.35 vs. 3.26 and 3.27kg, respectively). Therefore, relationships between ADFI day 56 to market and ADFI day 0 to market with BPZ level were curvilinear (P&lt; 0.05). Both market weight and overall ADG tended (P&lt; 0.10) to have curvilinear relationships with BPZ level. While not different, 0.45kg and .91kg BPZ supplemented pigs were .97kg and 1.25kg heavier, respectively, on marketing day compared to control. No differences (P &gt;0.10) were observed for Feed:Gain. Part of the negative effects of HS include decrease in feed intake which contributes to intestinal damage and decreased performance. Data from this study show that both treatment combinations were able to improve feed intake and decrease stress which might have led to the improved weight gain at the end. The data provides evidence that the combination of BPZ and KTCr may alleviate the negative effects of HS and help with the performance of grow-finish pigs during heat stress.

Myosin Heavy Chain Expression in Skeletal Muscle Autografts under Neural or Aneural Conditions

1998 ◽  
Vol 75 (2) ◽  
pp. 135-147 ◽  
Author(s):  
Kotaro Yoshimura ◽  
William M. Kuzon ◽  
Kiyonori Harii
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain

The effect of glucocorticoids on the myosin heavy chain isoforms’ turnover in skeletal muscle

2003 ◽  
Vol 86 (2) ◽  
pp. 201-206 ◽  
Author(s):  
Teet Seene ◽  
Priit Kaasik ◽  
Ando Pehme ◽  
Karin Alev ◽  
Eva-Maria Riso
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms

scholarly journals Denervation Causes Fiber Atrophy and Myosin Heavy Chain Co-Expression in Senescent Skeletal Muscle

PLoS ONE ◽  
2012 ◽  
Vol 7 (1) ◽  
pp. e29082 ◽  
Author(s):  
Sharon L. Rowan ◽  
Karolina Rygiel ◽  
Fennigje M. Purves-Smith ◽  
Nathan M. Solbak ◽  
Douglas M. Turnbull ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fiber Atrophy

Differential patterns of transcript accumulation during human myogenesis

1987 ◽  
Vol 7 (11) ◽  
pp. 4100-4114
Author(s):  
P Gunning ◽  
E Hardeman ◽  
R Wade ◽  
P Ponte ◽  
W Bains ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Time Course ◽  
Human Skeletal Muscle ◽  
Transcript Accumulation ◽  
Mrna Accumulation ◽  
Adult Human ◽  
Alpha Actin

We evaluated the extent to which muscle-specific genes display identical patterns of mRNA accumulation during human myogenesis. Cloned satellite cells isolated from adult human skeletal muscle were expanded in culture, and RNA was isolated from low- and high-confluence cells and from fusing cultures over a 15-day time course. The accumulation of over 20 different transcripts was compared in these samples with that in fetal and adult human skeletal muscle. The expression of carbonic anhydrase 3, myoglobin, HSP83, and mRNAs encoding eight unknown proteins were examined in human myogenic cultures. In general, the expression of most of the mRNAs was induced after fusion to form myotubes. However, several exceptions, including carbonic anhydrase and myoglobin, showed no detectable expression in early myotubes. Comparison of all transcripts demonstrated little, if any, identity of mRNA accumulation patterns. Similar variability was also seen for mRNAs which were also expressed in nonmuscle cells. Accumulation of mRNAs encoding alpha-skeletal, alpha-cardiac, beta- and gamma-actin, total myosin heavy chain, and alpha- and beta-tubulin also displayed discordant regulation, which has important implications for sarcomere assembly. Cardiac actin was the only muscle-specific transcript that was detected in low-confluency cells and was the major alpha-actin mRNA at all times in fusing cultures. Skeletal actin was transiently induced in fusing cultures and then reduced by an order of magnitude. Total myosin heavy-chain mRNA accumulation lagged behind that of alpha-actin. Whereas beta- and gamma-actin displayed a sharp decrease after initiation of fusion and thereafter did not change, alpha- and beta-tubulin were transiently induced to a high level during the time course in culture. We conclude that each gene may have its own unique determinants of transcript accumulation and that the phenotype of a muscle may not be determined so much by which genes are active or silent but rather by the extent to which their transcript levels are modulated. Finally, we observed that patterns of transcript accumulation established within the myotube cultures were consistent with the hypothesis that myoblasts isolated from adult tissue recapitulate a myogenic developmental program. However, we also detected a transient appearance of adult skeletal muscle-specific transcripts in high-confluence myoblast cultures. This indicates that the initial differentiation of these myoblasts may reflect a more complex process than simple recapitulation of development.

scholarly journals Mutation of the IIB myosin heavy chain gene results in muscle fiber loss and compensatory hypertrophy

2001 ◽  
Vol 280 (3) ◽  
pp. C637-C645 ◽  
Author(s):  
David L. Allen ◽  
Brooke C. Harrison ◽  
Carol Sartorius ◽  
William C. Byrnes ◽  
Leslie A. Leinwand
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Body Mass ◽  
Heavy Chain ◽  
Compensatory Hypertrophy ◽  
Muscle Disease ◽  
Chain Gene ◽  
Fiber Types ◽  
Mouse Skeletal Muscle ◽  
Ultrastructural Studies

The fast skeletal IIb gene is the source of most myosin heavy chain (MyHC) in adult mouse skeletal muscle. We have examined the effects of a null mutation in the IIb MyHC gene on the growth and morphology of mouse skeletal muscle. Loss in muscle mass of several head and hindlimb muscles correlated with amounts of IIb MyHC expressed in that muscle in wild types. Decreased mass was accompanied by decreases in mean fiber number, and immunological and ultrastructural studies revealed fiber pathology. However, mean cross-sectional area was increased in all fiber types, suggesting compensatory hypertrophy. Loss of muscle and body mass was not attributable to impaired chewing, and decreased food intake as a softer diet did not prevent the decrease in body mass. Thus loss of the major MyHC isoform produces fiber loss and fiber pathology reminiscent of muscle disease.

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