calpastatin and Muscle-Weakness

calpastatin has been researched along with Muscle-Weakness* in 2 studies

Other Studies

2 other study(ies) available for calpastatin and Muscle-Weakness

Article	Year
Skeletal muscle-specific calpastatin overexpression mitigates muscle weakness in aging and extends life span. Journal of applied physiology (Bethesda, Md. : 1985), 2021, 08-01, Volume: 131, Issue:2 Topics: Aging; Animals; Calcium-Binding Proteins; Calpain; Longevity; Mice; Muscle Weakness; Muscle, Skeletal	2021
Muscle-specific calpastatin overexpression prevents diaphragm weakness in cecal ligation puncture-induced sepsis. Journal of applied physiology (Bethesda, Md. : 1985), 2014, Oct-15, Volume: 117, Issue:8 Recent work indicates that infections are a major contributor to diaphragm weakness in patients who are critically ill and mechanically ventilated, and that diaphragm weakness is a risk factor for death and prolonged mechanical ventilation. Infections activate muscle calpain, but many believe this is an epiphenomenon and that other proteolytic processes are responsible for infection-induced muscle weakness. We tested the hypothesis that muscle-specific overexpression of calpastatin (CalpOX; an endogenous calpain inhibitor) would attenuate diaphragm dysfunction in cecal ligation puncture (CLP)-induced sepsis. We studied 1) wild-type (WT) sham-operated mice, 2) WT CLP-operated mice, 3) CalpOX sham-operated mice, and 4) CalpOX CLP-operated mice (n = 9-10/group). Twenty-four hours after surgery, we assessed the diaphragm force-frequency relationship, diaphragm mass, and total protein content and diaphragm levels of talin and myosin heavy chain (MHC). CLP markedly reduced diaphragm-specific force generation (force/cross-sectional area), which was prevented by calpastatin overexpression (force averaged 21.4 ± 0.5, 6.9 ± 0.8, 22.4 ± 1.0, and 18.3 ± 1.3 N/cm(2), respectively, for WT sham, WT CLP, CalpOX sham, and CalpOX CLP groups, P < 0.001). Diaphragm mass and total protein content were similar in all groups. CLP induced talin cleavage and reduced MHC levels; CalpOX prevented these alterations. CLP-induced sepsis rapidly reduces diaphragm-specific force generation and is associated with cleavage and/or depletion of key muscle proteins (talin, MHC), effects prevented by muscle-specific calpastatin overexpression. These data indicate that calpain activation is a major cause of diaphragm weakness in response to CLP-induced sepsis. Topics: Animals; Calcium-Binding Proteins; Calpain; Cecum; Diaphragm; Ligation; Mice; Muscle Proteins; Muscle Weakness; Muscles; Myosin Heavy Chains; Sepsis; Talin	2014

Article

Year

Skeletal muscle-specific calpastatin overexpression mitigates muscle weakness in aging and extends life span.

Journal of applied physiology (Bethesda, Md. : 1985), 2021, 08-01, Volume: 131, Issue:2

Topics: Aging; Animals; Calcium-Binding Proteins; Calpain; Longevity; Mice; Muscle Weakness; Muscle, Skeletal

2021

Muscle-specific calpastatin overexpression prevents diaphragm weakness in cecal ligation puncture-induced sepsis.

Journal of applied physiology (Bethesda, Md. : 1985), 2014, Oct-15, Volume: 117, Issue:8

Recent work indicates that infections are a major contributor to diaphragm weakness in patients who are critically ill and mechanically ventilated, and that diaphragm weakness is a risk factor for death and prolonged mechanical ventilation. Infections activate muscle calpain, but many believe this is an epiphenomenon and that other proteolytic processes are responsible for infection-induced muscle weakness. We tested the hypothesis that muscle-specific overexpression of calpastatin (CalpOX; an endogenous calpain inhibitor) would attenuate diaphragm dysfunction in cecal ligation puncture (CLP)-induced sepsis. We studied 1) wild-type (WT) sham-operated mice, 2) WT CLP-operated mice, 3) CalpOX sham-operated mice, and 4) CalpOX CLP-operated mice (n = 9-10/group). Twenty-four hours after surgery, we assessed the diaphragm force-frequency relationship, diaphragm mass, and total protein content and diaphragm levels of talin and myosin heavy chain (MHC). CLP markedly reduced diaphragm-specific force generation (force/cross-sectional area), which was prevented by calpastatin overexpression (force averaged 21.4 ± 0.5, 6.9 ± 0.8, 22.4 ± 1.0, and 18.3 ± 1.3 N/cm(2), respectively, for WT sham, WT CLP, CalpOX sham, and CalpOX CLP groups, P < 0.001). Diaphragm mass and total protein content were similar in all groups. CLP induced talin cleavage and reduced MHC levels; CalpOX prevented these alterations. CLP-induced sepsis rapidly reduces diaphragm-specific force generation and is associated with cleavage and/or depletion of key muscle proteins (talin, MHC), effects prevented by muscle-specific calpastatin overexpression. These data indicate that calpain activation is a major cause of diaphragm weakness in response to CLP-induced sepsis.

Topics: Animals; Calcium-Binding Proteins; Calpain; Cecum; Diaphragm; Ligation; Mice; Muscle Proteins; Muscle Weakness; Muscles; Myosin Heavy Chains; Sepsis; Talin

2014