Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains

Lehti, Maarit; Kivelä, Riikka; Komi, Paavo V.; Komulainen, Jyrki; Kainulainen, Heikki; Kyröläinen, Heikki

doi:10.1152/japplphysiol.90660.2008

Cited by 42 publications

(37 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…To test this hypothesis, we focused on MARP2/ANKRD2, since MARP2 interacts directly with connectin/titin at the N2A region (15,25), where it competes with p94 (17). In addition, MARP2's expression is sensitive to muscle conditions (26,27), and it modulates transcription factors such as YB1, PML, and p53 by binding them (28). Consistent with these reports, we observed that the MARP2 protein was increased in WTex mice compared with WT mice (Figure 4, A and B; Supplemental Figure 7).…”

Section: Figuresupporting

confidence: 87%

“…In other words, the loss of p94 protease activity may disrupt a MARP2-mediated stressresponse pathway, resulting in muscle degeneration. This notion is also supported by the observations that exercise induces p94 proteolytic activity and the upregulated transcription of MARP2 in human skeletal muscles (20,27) and that p94 is mislocalized in LGMD2A patients (37).…”

Section: Figurementioning

confidence: 57%

See 1 more Smart Citation

Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy

et al. 2010

View full text Add to dashboard Cite

Limb-girdle muscular dystrophy type 2A (LGMD2A) is a genetic disease that is caused by mutations in the calpain 3 gene (CAPN3), which encodes the skeletal muscle-specific calpain, calpain 3 (also known as p94). However, the precise mechanism by which p94 functions in the pathogenesis of this disease remains unclear. Here, using p94 knockin mice (termed herein p94KI mice) in which endogenous p94 was replaced with a proteolytically inactive but structurally intact p94:C129S mutant protein, we have demonstrated that stretch-dependent p94 distribution in sarcomeres plays a crucial role in the pathogenesis of LGMD2A. The p94KI mice developed a progressive muscular dystrophy, which was exacerbated by exercise. The exercise-induced muscle degeneration in p94KI mice was associated with an inefficient redistribution of p94:C129S in stretched sarcomeres. Furthermore, the p94KI mice showed impaired adaptation to physical stress, which was accompanied by compromised upregulation of muscle ankyrin-repeat protein-2 and hsp upon exercise. These findings indicate that the stretchinduced dynamic redistribution of p94 is dependent on its protease activity and essential to protect muscle from degeneration, particularly under conditions of physical stress. Furthermore, our data provide direct evidence that loss of p94 protease activity can result in LGMD2A and molecular insight into how this could occur.

show abstract

Section: Figuresupporting

confidence: 87%

Section: Figurementioning

confidence: 57%

Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy

et al. 2010

View full text Add to dashboard Cite

show abstract

“…Titin content was reduced due to direct damage or degradation of titin following a single high-intensity eccentric resistance exercise of human M. vastus lateralis (Trappe et al, 2002). However, Lehti et al (2009) reported no change in titin mRNA expression 2 days after fatiguing jumping exercise. Examination of muscle adaptation after training periods (8-15 weeks) including stretch-shortening exercises and explosive jump squat training resulted in no changes in titin isoforms (Kyrolainen et al, 2005;McGuigan et al, 2003).…”

Section: Introductionmentioning

confidence: 96%

Does weightlifting increase residual force enhancement?

Siebert

Kurch²,

Blickhan

et al. 2016

Journal of Biomechanics

View full text Add to dashboard Cite

“…Furthermore, the mRNA expression of these atrogenes is elevated in sarcopenic muscle (43) and reduced following muscle hypertrophy (51), suggesting a role in the regulation of muscle mass. The calpains are components of the Ca 2ϩ -dependent protein degradation pathway and have been implicated in muscle proteolysis following muscle-damaging exercise (14,28). The role of these factors in regulating exercise-mediated protein breakdown to nondamaging exercise is not well defined.…”

mentioning

confidence: 99%

Muscle protein synthesis and gene expression during recovery from aerobic exercise in the fasted and fed states

Harber

Konopka

Jemioło

et al. 2010

American Journal of Physiology-Regulatory, Integrative and Comp

View full text Add to dashboard Cite

Harber MP, Konopka AR, Jemiolo B, Trappe SW, Trappe TA, Reidy PT. Muscle protein synthesis and gene expression during recovery from aerobic exercise in the fasted and fed states. Am J Physiol Regul Integr Comp Physiol 299: R1254 -R1262, 2010. First published August 18, 2010 doi:10.1152/ajpregu.00348.2010.-The purpose of this investigation was to assess mixed-muscle fractional synthesis rate (FSR) and the expression of genes involved in skeletal muscle remodeling after aerobic exercise in the fasted and fed states. Eight recreationally active males (25 Ϯ 1 yr; V O2 max: 52 Ϯ 2 ml·kg Ϫ1 ·min Ϫ1 ) performed 60-min of cycle ergometry at 72 Ϯ 1% V O2 max on two occasions in a counter-balanced design. Subjects ingested a noncaloric placebo (EX-FAST) or a beverage containing (per kg body wt): 5 kcal, 0.83 g carbohydrate, 0.37 g protein, and 0.03 g fat (EX-FED) immediately and 1 h after exercise. FSR was assessed at rest and following exercise with the use of a L-[ring 2 H5]-phenylalanine infusion combined with muscle biopsies at 2 and 6 h postexercise. mRNA expression was assessed at 2 and 6 h postexercise via real-time RT-PCR. FSR was higher (P Ͻ 0.05) after exercise in both EX-FAST (0.112 Ϯ 0.010%·h Ϫ1 ) and EX-FED (0.129 Ϯ 0.014%·h Ϫ1 ) compared with rest (0.071 Ϯ 0.005%·h Ϫ1 ). Feeding attenuated the mRNA expression (P Ͻ 0.05) of proteolytic factors MuRF-1 (6 h) and calpain-2 (2 and 6 h) postexercise but did not alter FOXO3A, calpain-1, caspase3, or myostatin mRNA expression compared with EX-FAST. Myogenic regulatory factor (MRF4) mRNA was also attenuated (P Ͻ 0.05) at 2 and 6 h postexercise in EX-FED compared with EX-FAST. These data demonstrate that a nonexhaustive bout of aerobic exercise stimulates skeletal muscle FSR in the fasted state and that feeding does not measurably enhance FSR between 2 and 6 h after aerobic exercise. Additionally, postexercise nutrient intake attenuates the expression of factors involved in the ubiquitin-proteosome and Ca 2ϩ -dependent protein degradation pathways. These data provide insight into the role of feeding on muscle protein metabolism during recovery from aerobic exercise. protein turnover; endurance; proteolysis; muscle-specific RING finger protein-1; calpain AEROBIC EXERCISE ACUTELY (8, 44) and chronically (41, 45) alters skeletal muscle protein metabolism. The influence of nutrient supply (i.e., feeding) on skeletal muscle protein kinetics following exercise that is considered to be aerobic or endurancenatured remains relatively unexplored. Levenhagen et al. (29) initially showed that ingestion of minimal amounts of carbohydrate (8 g) combined with 10 g of protein creates a positive protein balance across the leg following aerobic exercise, apparently through promoting muscle protein synthesis with little influence on protein breakdown. Recently, it was reported that coingestion of protein and carbohydrate following aerobic exercise stimulates muscle protein synthesis greater than carbohydrate intake alone and yields a net positive whole-body protein balance (24). Whi...

show abstract

Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains

Abstract: Lehti M, Kivelä R, Komi P, Komulainen J, Kainulainen H, Kyrölä inen H. Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains.

Cited by 42 publications

References 56 publications

Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy

Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy

Does weightlifting increase residual force enhancement?

Muscle protein synthesis and gene expression during recovery from aerobic exercise in the fasted and fed states

Contact Info

Product

Resources

About