Insulin is a well-known anabolic hormone. The mechanism of insulin's p
rotein anabolic effect remains controversial. Although insulin undoubt
edly inhibits protein degradation, its effect on protein synthesis is
incompletely defined. Recent studies reviewed in this article highligh
t the methodologic limitations in studying the effect of insulin on pr
otein synthesis. These methodological issues are related to the hypoam
inoacidemia that ensues after insulin administration and to the diffic
ulty in measuring the obligatory precursor pool (aminoacyl tRNA) label
. Differential responses to unweighing in different muscle proteins ha
s been demonstrated. The protein loss during unweighing is due to the
loss of myofibrillar proteins, although sarcoplasmic proteins are spar
ed. A recent study has found that lipid emulsion has no effect on whol
e protein degradation but decreases forearm protein degradation and sy
nthesis. Age-related muscle wasting in humans has been shown to be rel
ated to a decline in fractional myofibrillar protein synthesis rate. A
lthough some progress has been made by recent studies, refined methodo
logies are needed to define the regulation of muscle protein turnover
in humans.