Protein synthesis is an important biological process required for long-term adaptive change in the nervous system1. Inhibiting protein synthesis blocks long-term memory storage in both invertebrates and vertebrates2. Protein synthesis is essential for maintenance of the late phases of some forms of long-term potentiation (LTP) and long-term depression (LTD)3, neuronal survival during development4, and for general maintenance of the neuron and its synaptic connections5. Measurement of rates of brain protein synthesis may be an important tool with which to study adaptive changes as well as neurodevelopmental disorders and disorders related to learning and memory.
We have developed a method to quantify rates of cerebral protein synthesis in vivo in an awake animal that offers inherent advantages over other techniques that estimate rates in ex vivo or in vitro preparations of brain tissue6. Foremost is the applicability to measurements in the intact brain in an awake animal. This is a key consideration because it allows measurements with synaptic structure and function in place and without concerns about post mortem effects. Moreover, the quantitative autoradiographic approach that we employ achieves a high degree of spatial localization. Whereas the energy of 14C is such that we cannot localize the tracer at the subcellular or cellular level, we can measure rates in cell layers and small brain regions such as hypothalamic nuclei, with approximately a 25 µm resolution7.
One challenge of in vivo measurements with radiotracers is to ensure that radiolabel measured is in the product of the reaction of interest rather than unreacted labeled precursor or other extraneous labeled metabolic products6. We chose L-[1-14C]-leucine as the tracer amino acid because it is either incorporated into protein or rapidly metabolized to 14CO2, which is diluted in the large pool of unlabeled CO2 in brain resulting from the high rate of energy metabolism8. Moreover, any 14C not incorporated into protein exists primarily as free [14C]-leucine, which over the 60 min experimental period, is almost entirely cleared from the tissue6. Proteins are then fixed to tissue with formalin and subsequently rinsed with waterto remove any free [14C]-leucine before autoradiography.
Another important consideration is the issue of the dilution of the specific activity of the precursor amino acid pool by unlabeled amino acids derived from tissue proteolysis. We have shown that in adult rat and mouse, about 40% of the precursor leucine pool for protein synthesis in the brain comes from amino acids derived from protein breakdown6. This must be included in the computation of regional rates of cerebral protein synthesis (rCPS) and must be confirmed in studies in which this relationship may change. The theoretical basis and the assumptions of the method have been presented in detail elsewhere6. In this paper, we focus on the procedural issues of the application of this methodology.
This method has been employed for the determination of rCPS in ground squirrels9, sheep10, rhesus monkeys11, rats12,13,14,15,16,17,18,19,20,21, a mouse model of Tuberous Sclerosis complex22, a mouse model of fragile X syndrome23,24,25,26, fragile X premutation mice27, and a mouse model of phenylketonuria28. In this manuscript, we present the procedures for measurement of rCPS with the in vivo autoradiographic L-[1-14C]-leucine method. We present rCPS in brain regions of an awake control mouse. We also demonstrate that in vivo administration of anisomycin, an inhibitor of translation, abolishes protein synthesis in the brain.