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1.
J Strength Cond Res ; 37(10): 1963-1968, 2023 Oct 01.
Article in English | MEDLINE | ID: mdl-37729511

ABSTRACT

ABSTRACT: Larsen, F, Loturco, I, Sigvaldsen, E, Strand, MF, Kalhovde, JM, and Haugen, T. Reliability and validity of different lower-limb strength tests to determine 1RM in the Keiser A300 leg press. J Strength Cond Res 37(10): 1963-1968, 2023-The aim of this study was to explore the reliability and validity of different lower-limb strength tests to determine the one-repetition maximum (1RM) value in the Keiser A300 leg press. Twenty-eight recreationally active subjects performed load-velocity (L-V) relationship, 1RM, isometric midthigh pull (IMTP), and maximal repetitions to failure (MRF) tests on 3 separated sessions. Predicted 1RMs for the L-V relationship were estimated from a linear regression equation, correlating movement velocity and relative loads. The number of repetitions from the MRF tests (at loads relative to bodyweight) and peak force from the IMTP tests were used in regression equations to predict 1RM. The level of significance was set to ρ ≤ 0.05. All 1RM prediction methods were highly comparable with the traditional 1RM test, as only trivial and nonsignificant differences were observed. Furthermore, the L-V relationship was the most reliable (intraclass correlation coefficient [± 95% confidence interval] = 0.99 [0.98, 0.996]; effect size = -0.01 [-0.38, 0.36], standard error of the measurement = 6.4 kg; coefficient of variation = 3.0 [2.2-3.8]% and valid (r = 0.95 [0.89, 0.98], effect size = 0.08 [-0.29, 0.45], standard error of the estimate = 20.4 kg; coefficient of variation = 7.4 [5.5-9.3]%) when compared with direct 1RM measurements. The L-V relationship test showed a significant change score relationship (r = 0.41 [0.04, 0.68]) against the direct 1RM measurements. In conclusion, the tests used in this study cannot be used interchangeably, but they represent a good alternative in training settings where 1RM testing is not feasible.


Subject(s)
Leg , Humans , Reproducibility of Results , Body Weight , Correlation of Data , Linear Models
2.
PLoS One ; 18(7): e0288649, 2023.
Article in English | MEDLINE | ID: mdl-37440572

ABSTRACT

OBJECTIVES: The purpose of this study was to explore the validity and reliability of three different strength testing approaches to determine one-repetition maximum (1RM) in the bench press and prone bench pull. METHODS: Twenty-eight recreationally active subjects (25 ± 2 years, 178 ± 8 cm, 78 ± 9 kg) were assessed for load-velocity (L-V) relationship, 1RM, maximal isometric force (MIF), and maximal repetitions to failure (MRF) in a Smith Machine on three separated sessions. Linear regression was used for L-V relationship, MIF, and MRF to predict 1RM. Level of significance was set to ρ ≤ 0.05. RESULTS: Reliability analyses of the varying 1RM estimations revealed mean differences from 0.6 to -1.3 kg (mainly trivial effects) between test days 1 and 2, intraclass correlation coefficient was > 0.96, and coefficient of variation (CV) was in the range 2.3-8.3% for all tests. Regarding validity, all 1RM predictions exhibited a mean difference ≤ 1.3 kg (trivial), except for the L-V relationship method that underestimated the predicted 1RM by 5 kg (small) compared to the actual bench press 1RM. However, the L-V relationship method showed the least mean absolute errors. CVs were in the range 4.5-13.2%. Standard error of the estimate was in the range 3.2-9.7 kg. Change scores for all tests were significantly correlated with change scores in actual 1RM, except for MIF in the prone bench pull. Smallest deviations in 1RM predictions were observed for the L-V relationship approach. CONCLUSIONS: All 1RM prediction methods were highly comparable to the traditional 1RM test. However, given the high variability associated with individual predictions for each method, they cannot be used interchangeably.


Subject(s)
Resistance Training , Weight Lifting , Humans , Reproducibility of Results , Muscle Strength , Linear Models , Resistance Training/methods
3.
Am J Physiol Regul Integr Comp Physiol ; 293(2): R844-53, 2007 Aug.
Article in English | MEDLINE | ID: mdl-17522120

ABSTRACT

In this study the stress protein response to unaccustomed maximal eccentric exercise in humans was investigated. Eleven healthy males performed 300 maximal eccentric actions with the quadriceps muscle. Biopsies from vastus lateralis were collected at 30 min and 4, 8, 24, 96, and 168 h after exercise. Cellular regulation and localization of heat shock protein (HSP) 27, alpha B-crystallin, and HSP70 were analyzed by immunohistochemistry, ELISA technique, and Western blotting. Additionally, mRNA levels of HSP27, alpha B-crystallin, and HSP70 were quantified by Northern blotting. After exercise (30 min), 81 +/- 8% of the myofibers showed strong HSP27 staining (P < 0.01) that gradually decreased during the following week. alpha B-Crystallin mimicked the changes observed in HSP27. After exercise (30 min), the ELISA analysis showed a 49 +/- 13% reduction of the HSP27 level in the cytosolic fraction (P < 0.01), whereas Western blotting revealed a 15-fold increase of the HSP27 level in the myofibrillar fraction (P < 0.01). The cytosolic HSP70 level increased to 203 +/- 37% of the control level 24 h after exercise (P < 0.05). After 4 days, myofibrillar-bound HSP70 had increased approximately 10-fold (P < 0.01) and was accompanied by strong staining on cross sections. mRNA levels of HSP27, alpha B-crystallin, and HSP70 were all elevated the first day after exercise (P < 0.01); HSP70 mRNA showed the largest increase (20-fold at 8 h). HSP27 and alpha B-crystallin seemed to respond immediately to maximal eccentric exercise by binding to cytoskeletal/myofibrillar proteins, probably to function as stabilizers of disrupted myofibrillar structures. Later, mRNA and total HSP protein levels, especially HSP70, increased, indicating that HSPs play a role in skeletal muscle recovery and remodeling/adaptation processes to high-force exercise.


Subject(s)
Exercise/physiology , HSP70 Heat-Shock Proteins/metabolism , Heat-Shock Proteins/metabolism , Myofibrils/metabolism , Neoplasm Proteins/metabolism , Quadriceps Muscle/physiology , Adaptation, Physiological/physiology , Adult , Creatine Kinase/blood , Cytosol/metabolism , HSP27 Heat-Shock Proteins , HSP70 Heat-Shock Proteins/genetics , Heat-Shock Proteins/genetics , Humans , Immunohistochemistry , Male , Molecular Chaperones , Neoplasm Proteins/genetics , Pain/metabolism , Pain/physiopathology , Quadriceps Muscle/cytology , RNA, Messenger/metabolism , Torque , alpha-Crystallin B Chain/genetics , alpha-Crystallin B Chain/metabolism
4.
J Gene Med ; 7(2): 218-27, 2005 Feb.
Article in English | MEDLINE | ID: mdl-15515140

ABSTRACT

BACKGROUND: Injection of DNA encoding exogenic proteins into muscle tissue combined with electroporation often results in a transient increase of the encoded protein concentration in the muscle and the blood. The reduction is normally due to an immune response against the exogenic protein but other factors may also be involved. How various electroporation parameters affect the concentration kinetics of syngenic and exogenic proteins is studied in relation to immune response and muscle damage after electroporation-mediated DNA transfer to muscle. METHODS: Electroporation was applied to mouse quadriceps and rat tibialis anterior muscles after injection of DNA encoding either secreted alkaline phosphatase (SEAP), beta-galactosidase (beta-gal), luciferase or a mouse IgG molecule. Protein concentrations in blood or muscle and antibody responses were measured for a period up to 3 months. Tissue inflammation and muscle cell damage were studied on muscle cross-sections and assessed by measuring the concentrations of creatine phosphokinase (CPK) in blood. RESULTS: Mice with the highest SEAP concentration in blood at day 7 also had the highest rate of decrease afterwards, the strongest antibody responses against SEAP and the highest acute levels of CPK in blood. DNA-transfected muscle fibers were significantly reduced in number from days 7 to 14. Mononuclear cells surrounded the reporter gene expressing muscle fibers, thus indicating a cellular immune response. When using DNA encoding a syngenic protein the protein concentration in blood was relatively stabile over a 3-month period, but showed different kinetics for various electroporation parameters. CONCLUSIONS: Our findings suggest that the optimal electroporation parameters for DNA vaccination may be different from the optimal parameters for long-term expression of genes encoding syngenic proteins.


Subject(s)
Antibody Formation/immunology , DNA/metabolism , Electroporation/methods , Gene Expression , Genetic Therapy/methods , Immunotherapy/methods , Muscle, Skeletal/metabolism , Alkaline Phosphatase/blood , Alkaline Phosphatase/genetics , Alkaline Phosphatase/metabolism , Animals , Creatine Kinase/blood , DNA/immunology , DNA Primers , Enzyme-Linked Immunosorbent Assay , Genetic Vectors/genetics , Histocytochemistry , Immunoglobulin G/blood , Immunoglobulin G/genetics , Immunoglobulin G/metabolism , Immunoglobulin lambda-Chains/genetics , Kinetics , Luciferases/metabolism , Male , Muscle, Skeletal/pathology , Rats , Rats, Wistar , beta-Galactosidase
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