Icariin Improves Cognitive Impairment after Traumatic Brain Injury by Enhancing Hippocampal Acetylation / 中国结合医学杂志

<p><b>OBJECTIVE</b>To examine the effect of icariin (ICA) on the cognitive impairment induced by traumatic brain injury (TBI) in mice and the underlying mechanisms related to changes in hippocampal acetylation level.</p><p><b>METHODS</b>The modifified free-fall method was used to establish the TBI mouse model. Mice with post-TBI cognitive impairment were randomly divided into 3 groups using the randomised block method (n=7): TBI (vehicle-treated), low-dose (75 mg/kg) and high-dose (150 mg/kg) of ICA groups. An additional sham-operated group (vehicle-treated) was employed. The vehicle or ICA was administrated by gavage for 28 consecutive days. The Morris water maze (MWM) test was conducted. Acetylcholine (ACh) content, mRNA and protein levels of choline acetyltransferase (ChAT), and protein levels of acetylated H3 (Ac-H3) and Ac-H4 were detected in the hippocampus.</p><p><b>RESULTS</b>Compared with the sham-operated group, the MWM performance, hippocampal ACh content, mRNA and protein levels of ChAT, and protein levels of Ac-H3 and Ac-H4 were signifificantly decreased in the TBI group (P<0.05). High-dose of ICA signifificantly ameliorated the TBI-induced weak MWM performance, increased hippocampal ACh content, and mRNA and protein levels of ChAT, as well as Ac-H3 protein level compared with the TBI group (P<0.05).</p><p><b>CONCLUSION</b>ICA improved post-TBI cognitive impairment in mice by enhancing hippocampal acetylation, which improved hippocampal cholinergic function and ultimately improved cognition.</p>

[Cloning, fusion expression and identification of thioredoxin encoding gene from Toxoplasma gondii].

OBJECTIVE: To clone and express the thioredoxin (Trx) from RH strain tachyzoites of Toxoplasma gondii, establish the prokaryotic expression vector and purify the recombinant protein, then produce the polyclonal anti-Trx antibody in rabbits. METHODS: Trx fragment was amplified by PCR and cloned into the pET-28a (+) vector, and the recombinant protein was induced with IPTG and purified by Ni-NTA affinity chromatography. The polyclonal antibody specificity was detected by Western blotting. RESULTS: The trx gene was amplified from T. gondii cDNA by PCR. The recombinant plasmid trx/pET-28a (+) was usefully constructed, and the recombinant TRX protein was expressed and purified. The TRX polyclonal antibody was also obtained. The specific band of TRX was detected by Western blotting. CONCLUSIONS: Western blotting can detect the specificity of polyclonal anti-Trx antibody, which will facilitate the biological functions of Trx.