MT-I/II expression was measured by quantitative reverse-transcriptase PCR and enzyme-linked immunosorbent assay. The study utilised a MT-I/II2/2 mouse strain that still produces MT-I and MT-II mRNAs but premature stop codons in the open-reading-frame result in production of greatly truncated peptides consisting of 10 and 15 amino acids from the N-terminus, respectively. This allowed for liver zinc content after brain injury to be measured in a mouse without fully functional MT-I/II protein. When the UC1MT antibody was initially characterised for its ability to detect MT-I and MT-II by ELISA, the discovery of MT-III was relatively recent and no test for cross-reactivity of MTIII with this antibody has since been published. It was necessary to demonstrate that the UC1MT ELISA is specific for MT-I/II and does not cross-react with MT-III, the brain-specific MT isoform. It is apparent from the curves that the UC1MT antibody displays little cross reactivity with MT-III. Displacement curves were set up to determine if matrix effects that could interfere with the ELISA were present in mouse brain or liver tissue homogenates. Such curves have not been Octinoxate published previously for the UC1MT ELISA technique. The term ����matrix effects��’relates to substances in complex biological samples that do not directly cause false-positive detection in an immunoassay but have the capacity to displace the antibodyantigen interaction. Displacement curves are similar to standard curves except that serial dilution of the Taltirelin analyte is performed in analyte-free matrix, in this case tissue homogenate from MT-I/II2/2 mouse brain and liver was used. Using MT-I/II-free brain and liver homogenates with total protein concentration of 0.1 mg/ml or 0.01 mg/ml, we observed no deviation of the slope of the displacement curves from the standard curve which indicates that no matrix effects are present under these assay conditions, in these tissues. We have determined that concentrations higher than 0.1 mg/ml begin to interfere with the assay in most of the tissue types tested. However, it was determined that there were significant and comparable increases in plasma corticosterone concentrations in cryolesioned and sham-injured animals. This indicates that animal handling is the most likely responsible for the increases in plasma corticosterone rather than the brain injury. Quantitative RT-PCR was carried out on liver samples from sham-injured animals but no significant increases in MT-I or MT-II mRNA expression were observed after sham surgery, despite the ability of the procedure to increase plasma corticosterone. In summary, the increases in plasma corticosterone after brain injury or sham surgery are not sufficient to induce hepatic MT-I/II expression alone and it is likely that another process is responsible for the increased hepatic expression of MT-I/II after brain injury. The glucocorticoid, corticosterone, is the primary stress hormone produced by the adrenal gland in rodents.