Role of Protein Carbonylation in Skeletal Muscle Mass Loss Associated with Chronic Conditions

Esther Barreiro, Esther Barreiro

Abstract

Muscle dysfunction, characterized by a reductive remodeling of muscle fibers, is a common systemic manifestation in highly prevalent conditions such as chronic heart failure (CHF), chronic obstructive pulmonary disease (COPD), cancer cachexia, and critically ill patients. Skeletal muscle dysfunction and impaired muscle mass may predict morbidity and mortality in patients with chronic diseases, regardless of the underlying condition. High levels of oxidants may alter function and structure of key cellular molecules such as proteins, DNA, and lipids, leading to cellular injury and death. Protein oxidation including protein carbonylation was demonstrated to modify enzyme activity and DNA binding of transcription factors, while also rendering proteins more prone to proteolytic degradation. Given the relevance of protein oxidation in the pathophysiology of many chronic conditions and their comorbidities, the current review focuses on the analysis of different studies in which the biological and clinical significance of the modifications induced by reactive carbonyls on proteins have been explored so far in skeletal muscles of patients and animal models of chronic conditions such as COPD, disuse muscle atrophy, cancer cachexia, sepsis, and physiological aging. Future research will elucidate the specific impact and sites of reactive carbonyls on muscle protein content and function in human conditions.

Keywords: COPD; aging; cancer-induced cachexia; cigarette smoking; disuse muscle atrophy; oxidants; protein carbonylation; septic muscles; skeletal muscle wasting and dysfunction.

Figures

Figure 1
Figure 1
Oxidative stress results from the imbalance between the production of oxidants and the effects of antioxidants in favor of the former.
Figure 2
Figure 2
Reactive oxygen species (ROS) that are not scavenged by cellular antioxidants oxidize key cellular structures such as membrane lipids, nuclear DNA, and proteins. Oxidative damage of proteins exerts different effects such as alteration of enzyme activity and DNA binding of transcription factors and may also render the proteins more susceptible to be degraded.
Figure 3
Figure 3
Representative 1D immunoblot with molecular weights corresponding to the detection of carbonylated proteins in crude muscle homogenates of the diaphragm muscle in three patients with severe chronic obstructive pulmonary disease (COPD). For detailed information see reference [23].
Figure 4
Figure 4
Representative 2D immunoblot with molecular weights corresponding to the detection of carbonylated proteins in crude muscle homogenates of the diaphragm muscle in one patient with COPD. For detailed information see reference [23].
Figure 5
Figure 5
Representative example of reactive carbonyl immunostaining in the extensor digitorum longus muscle of a tumor-bearing rat. Note that the intensity of the protein carbonylation staining differed among the fibers. A darker intensity was observed in the fast-twitch fibers compared to the slow-twitch fibers. For more information see reference [33].

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