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The effects of fasting or hypoxia on rates of protein synthesis in vivo in subcellular fractions of rat heart and gastrocnemius muscle.

ABSTRACT: We measured rates of protein synthesis in vivo in subcellular fractions (soluble, myofibrillar and stromal fractions) of the heart and the gastrocnemius from rats after fasting or under hypoxic conditions (i.e. atmospheres containing 5% or 10% O2). Such interventions are known to inhibit protein synthesis under some circumstances. The recovery of tissue protein after fractionation was 80-100%. The proportions of protein present in the soluble and stromal fractions were different in the two muscles. The rates of protein synthesis in the myofibrillar and stromal fractions were less than those for total mixed tissue protein, whereas the rate for soluble protein was greater. Both fasting and moderate hypoxia (10% O2 for 24 h) inhibited protein synthesis in the gastrocnemius. In this tissue, the synthesis of the myofibrillar fraction was apparently the most sensitive to inhibition, and this resulted in some significant increases in the soluble-fraction/myofibrillar-fraction protein-synthesis rate ratios. In the heart, fasting inhibited protein synthesis, but moderate hypoxia (10% O2 for 24 h) did not. The rate of protein synthesis in the cardiac myofibrillar fraction was again more sensitive to fasting than were the rates in the other fractions, but it was not as sensitive as that in the gastrocnemius. Under severely hypoxic conditions (5% O2 for 1 or 2 h), protein synthesis was decreased in all fractions in both tissues. These results suggest that the rates of protein synthesis in these relatively crude subcellular fractions vary.

SUBMITTER: Preedy VR

PROVIDER: S-EPMC1135609 | biostudies-other | 1989 Jan

REPOSITORIES: biostudies-other

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Project description:BackgroundHypoxemia in humans may occur during high altitude mountaineering and in patients suffering from ventilatory insufficiencies such as cardiovascular- or respiratory disease including Chronic Obstructive Pulmonary Disease (COPD). In these conditions, hypoxemia has been correlated to reduced appetite and decreased food intake. Since hypoxemia and reduced food intake intersect in various physiological and pathological conditions and both induce loss of muscle mass, we investigated whether hypoxia aggravates fasting-induced skeletal muscle atrophy and evaluated underlying protein turnover signaling.MethodsMice were kept under hypoxic (8% oxygen) or normoxic conditions (21% oxygen), or were pair-fed to the hypoxia group for 12 days. Following an additional 24 hours of fasting, muscle weight and protein turnover signaling were assessed in the gastrocnemius muscle by RT-qPCR and Western blotting.ResultsLoss of gastrocnemius muscle mass in response to fasting in the hypoxic group was increased compared to the normoxic group, but not to the pair-fed normoxic control group. Conversely, the fasting-induced increase in poly-ubiquitin conjugation, and expression of the ubiquitin 26S-proteasome E3 ligases, autophagy-lysosomal degradation-related mRNA transcripts and proteins, and markers of the integrated stress response (ISR), were attenuated in the hypoxia group compared to the pair-fed group. Mammalian target of rapamycin complex 1 (mTORC1) downstream signaling was reduced by fasting under normoxic conditions, but sustained under hypoxic conditions. Activation of AMP-activated protein kinase (AMPK) / tuberous sclerosis complex 2 (TSC2) signaling by fasting was absent, in line with retained mTORC1 activity under hypoxic conditions. Similarly, hypoxia suppressed AMPK-mediated glucocorticoid receptor (GR) signaling following fasting, which corresponded with blunted proteolytic signaling responses.ConclusionsHypoxia aggravates fasting-induced muscle wasting, and suppresses AMPK and ISR activation. Altered AMPK-mediated regulation of mTORC1 and GR may underlie aberrant protein turnover signaling and affect muscle atrophy responses in hypoxic skeletal muscle.

Project description:Muscle fiber deformation is related to its cellular structure, as well as its architectural arrangement within the musculoskeletal system. While playing an important role in aponeurosis displacement, and efficiency of force transmission to the tendon, such deformation also provides important clues about the underlying mechanical structure of the muscle. We hypothesized that muscle fiber cross section would deform asymmetrically to satisfy the observed constant volume of muscle during a contraction. Velocity-encoded, phase-contrast, and morphological magnetic resonance imaging techniques were used to measure changes in fascicle length, pinnation angle, and aponeurosis separation of the human gastrocnemius muscle during passive and active eccentric ankle joint movements. These parameters were then used to subsequently calculate the in-plane muscle area subtended by the two aponeuroses and fascicles and to calculate the in-plane (dividing area by fascicle length), and through-plane (dividing muscle volume by area) thicknesses. Constant-volume considerations of the whole-muscle geometry require that, as fascicle length increases, the muscle fiber cross-sectional area must decrease in proportion to the length change. Our empirical findings confirm the definition of a constant-volume rule that dictates that changes in the dimension perpendicular to the plane, i.e., through-plane thickness, (-6.0% for passive, -3.3% for eccentric) equate to the reciprocal of the changes in area (6.8% for passive, 3.7% for eccentric) for both exercise paradigms. The asymmetry in fascicle cross-section deformation for both passive and active muscle fibers is established in this study with a ∼22% in-plane and ∼6% through-plane fascicle thickness change. These fiber deformations have functional relevance, not only because they affect the force production of the muscle itself, but also because they affect the characteristics of adjacent muscles by deflecting their line of pull.

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The effects of fasting or hypoxia on rates of protein synthesis in vivo in subcellular fractions of rat heart and gastrocnemius muscle.

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