Glucocorticoids Do Not Regulate the Expression of Proteolytic Genes in Skeletal Muscle from Cushing's Syndrome Patients

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Abstract
Glucocorticoids signal enhanced,proteolysis in various instances,of muscle,atrophy,and increased,gene,expression,of components,of the lysosomal, Ca,1-activated proteinase), ubiquitin, 14-kDa ubiquitin-activating enzyme E2, and 20S proteasome subunits (i.e. critical components of the ubiquitin-proteasome,proteolytic process) in skeletal muscle,from such patients. Thus, in striking contrast with animal studies, glu- cocorticoids,did not regulate,the expression,of muscle,proteolytic genes in Cushing’s syndrome. In humans, messenger RNA levels, for at least ubiquitin and proteasome subunits, are elevated in acute situations of muscle wasting, such as head trauma or sepsis. Because Cushing’s syndrome is a chronic catabolic condition, we suggest that the lack of regulation,of proteolytic genes,in such,patients,may,rep- resent an adaptive regulatory mechanism, preventing sustained in- creased,protein,breakdown,and,avoiding,rapid,muscle,wasting. (J Clin Endocrinol Metab 82: 3161‐3164, 1997) A DMINISTRATION of glucocorticoids results in an im-

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