Hepatocellular carcinoma(HCC)is a highly heterogeneous malignancy with poor prognosis,closely linked to oxidative stress,metabolic reprogramming,and tumor microenvironment alterations.Aldehyde dehydrogenase(ALDH)plays multifaceted roles in HCC by regulating oxidative stress,modulating glucose and lipid metabolism,sustaining cancer stem cell properties,and promoting immune evasion,making it a promising therapeutic target.This review summarizes the expression patterns and mechanistic functions of ALDH in HCC,highlights advances in ALDH-targeted therapies,including inhibitors such as disulfiram and diethylaminobenzaldehyde,and ALDH-based peptide vaccines-and discusses their potential in combination with immunotherapy and chemotherapy.Current evidence suggests that ALDH inhibition can suppress tumor growth,reverse drug resistance,and enhance antitumor immunity.Future research should aim to improve drug selectivity and safety,and to develop personalized combination strategies to optimize clinical outcomes in HCC patients.

Hepatocellular carcinoma(HCC)is a highly heterogeneous malignancy with poor prognosis,closely linked to oxidative stress,metabolic reprogramming,and tumor microenvironment alterations.Aldehyde dehydrogenase(ALDH)plays multifaceted roles in HCC by regulating oxidative stress,modulating glucose and lipid metabolism,sustaining cancer stem cell properties,and promoting immune evasion,making it a promising therapeutic target.This review summarizes the expression patterns and mechanistic functions of ALDH in HCC,highlights advances in ALDH-targeted therapies,including inhibitors such as disulfiram and diethylaminobenzaldehyde,and ALDH-based peptide vaccines-and discusses their potential in combination with immunotherapy and chemotherapy.Current evidence suggests that ALDH inhibition can suppress tumor growth,reverse drug resistance,and enhance antitumor immunity.Future research should aim to improve drug selectivity and safety,and to develop personalized combination strategies to optimize clinical outcomes in HCC patients.

Background: and Purpose By measuring a newly defined parameter, the carotid–cerebral pulse wave velocity (ccPWV), this study aimed to determine the association of intracranial artery calcification (IAC) with arterial stiffness as reflected by the pulse wave velocity between the carotid and middle cerebral arteries using transcranial Doppler sonography in patients with acute stroke. Methods: We recruited 146 patients with ischemic stroke from our stroke center. Computed tomography of the head was used to assess the presence and severity of IAC. Arterial stiffness was evaluated using ccPWV. Data are presented as quartiles of ccPWV. A multivariable logistic regression model was used to assess the independent relationship between ccPWV and IAC. Results: The IAC prevalence increased with the ccPWV quartile, being 54%, 76%, 83%, and 89% for quartiles 1, 2, 3, and 4, respectively (p<0.001) as did IAC scores, with median [interquartile range] values of 0 [0–2], 3 [2–4], 4 [2–5], and 5 [4–6], respectively (p<0.001). After additionally adjusting for age and hypertension, a significant correlation was only found between quartiles 3 and 4 of ccPWV and IAC scores. The odds ratio (95% confidence interval) for the IAC scores was 1.78 (1.28–2.50) (p=0.001) in quartile 4 of ccPWV and 1.45 (1.07–1.95) (p=0.015) in quartile 3 compared with quartile 1. Conclusions We found that in patients with acute ischemic stroke, ccPWV was positively related to the degree of IAC. Future longitudinal cohort studies may help to identify the potential role of IAC in the progression of cerebral arterial stiffness.

Objective To clone and express the cell signaling protein 14-3-3 gene from Toxoplasma gondii RH strain. Methods Toxoplasma RH strain tachyzoites, which maintained by mouse passage, were harvested from ascites of mice and genomic DNA was prepared. A pair of primers were designed and synthesized based on the sequence of Toxo 14-3-3 cDNA. A specific fragment of Toxo 14-3-3 gene was obtained by RT-PCR amplification from Toxoplasma genomic DNA. The PCR products were ligated to pGEM-T. The EcoRI / Xho I restricted fragments, confirmed by PCR and EcoRI / XhoI digestion, were cloned into expression vector pET28a and the recombinants were transformd into E.coli BL21. Fusion expression was induced by isopropyl-beta-D-thiogalactoside (IPTG) and confirmed by Western blotting with rabbit anti-Toxoplasma sera. Results The molecular size of Toxo 14-3-3 was 803 bp, which is highly homologous to the previous report cloned from the parasites of intestinal epithelial stage in cat. High expression was obtained in pET28a/ Toxo 14-3-3/E.coli BL21 when confirmed by Western blotting. Conclusion The recombinant construction of Toxo 14-3-3 was generated and expression was induced.