Proteomic profiling of carbonic anhydrase CA3 in skeletal muscle

Introduction Carbonic anhydrase (CA) is a key enzyme that mediates the reversible hydration of carbon dioxide. Skeletal muscles contain high levels of the cytosolic isoform CA3. This enzyme has antioxidative function and plays a crucial role in the maintenance of intracellular pH homeostasis. Areas covered Since elevated levels of serum CA3, often in combination with other muscle-specific proteins, are routinely used as a marker of general muscle damage, it was of interest to examine recent analyses of this enzyme carried out by modern proteomics. This review summarizes the mass spectrometry-based identification and evaluation of CA3 in normal, adapting, dystrophic, and aging skeletal muscle tissues. Expert opinion The mass spectrometric characterization of CA3 confirmed this enzyme as a highly useful marker of both physiological and pathophysiological alterations in skeletal muscles. Cytosolic CA3 is clearly enriched in slow-twitching type I fibers, which makes it an ideal marker for studying fiber type shifting and muscle adaptations. Importantly, neuromuscular diseases feature distinct alterations in CA3 in skeletal muscle tissues versus biofluids, such as serum. Characteristic changes of CA3 in age-related muscle wasting and dystrophinopathy established this enzyme as a suitable biomarker candidate for differential diagnosis and monitoring of disease progression and therapeutic impact.

Automated summary

Carbonic anhydrase (CA) is a key enzyme in mediating the reversible hydration of carbon dioxide. Skeletal muscles contain high levels of cytosolic isoform CA3, which has antioxidative function and plays a crucial role in maintaining intracellular pH homeostasis. Recent proteomics analyses have confirmed CA3 as a valuable marker for both physiological and pathophysiological alterations in skeletal muscles, especially in slow-twitching type I fibers. Changes in CA3 levels in neuromuscular diseases, age-related muscle wasting, and dystrophinopathy establish this enzyme as a suitable biomarker for disease diagnosis and monitoring.