Starvation leads to decreased levels of mRNA for myofibrillar proteins.
Malnutrition is a common complicating factor in surgical illness. To investigate the cellular changes and mechanisms responsible for the protein wasting associated with nutritional deprivation, Sprague-Dawley rats were subjected to total protein-calorie starvation for 3 (n = 12) or 5 days (n = 12) and compared to freely fed animals monitored for 3 (n = 8) or 5 (n = 8) days. Gastrocnemius protein and RNA content and levels of mRNA coding for the myofibrillar proteins myosin heavy chain, myosin light chain, and alpha-actin were measured. Starvation resulted in a significant decrease in gastrocnemius mass and protein content, and was associated with decreases in mRNA levels for the three myofibrillar proteins assayed. We conclude that changes in mRNA levels for these proteins likely contribute to the loss of peripheral protein which occurs during total nutritional deprivation. In addition, the changes in mRNA levels for these three structural proteins appear to be coordinate, suggesting that transcription of no single myofibrillar protein is rate-limiting in the regulation of skeletal muscle protein content.
Fong
Y
Y
Laboratory of Surgical Metabolism, New York Hospital-Cornell Medical Center, New York 10021.
Moldawer
L L
LL
Marano
M A
MA
Wei
H
H
Barber
A
A
Fischman
D A
DA
Lowry
S F
SF
D000199:Actins / Q000235:genetics*; D000818:Animals; D015342:DNA Probes; D008297:Male; D009218:Myosins / Q000235:genetics*; D011502:Protein-Energy Malnutrition / Q000378:metabolism; D012333:RNA, Messenger / Q000032:analysis / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013217:Starvation / Q000378:metabolism*
D000199:Actins; D015342:DNA Probes; D012333:RNA, Messenger; D009218:Myosins