Case Report: Hepatocellular adenoma due to long-term oral stanozolol administration.

This article presents a case of a 15-year-old male with a 6-year history of aplastic anemia treated with long-term oral stanozolol to promote hematopoiesis. Throughout this period, he underwent regular outpatient follow-up assessments of blood and liver function parameters. While abnormal liver function was recorded on several occasions and treated with oral hepatoprotective drugs, no abdominal imaging test was conducted.

Multiomics Landscape Uncovers the Molecular Mechanism of the Malignant Evolution of Lung Adenocarcinoma Cells to Chronic Low Dose Cadmium Exposure.

Cadmium (Cd) from cigarette smoke and polluted air can lead to lung adenocarcinoma after long-term inhalation. However, most studies are based on short-term exposure to this toxic metal at high concentrations. Here, we investigate the effects of long-term exposure of A549 cells (lung adenocarcinoma) to cadmium at low concentrations using morphological and multiomics analyses.

[Effect of superantigen SEA on mitochondrial membrane potential of Molt-4 cell].

Aim: To explore the effect of superantigen staphylococcal enterotoxin A(SEA) on mitochondrial membrane potential of Molt-4 cell.

Methods: Cell counting kit-8(CCK-8) was used to detect the proliferation of T cell in different concentration and time, We employed JC-1 to estimate mitochondrialmembrane potential (δψm) of Molt-4 cell induced by SEA using flow cytometry (FCM).

Results: The proliferative activity of T cell treated with SEA(1 mg/L) was changed obviously compared with control.

Significance of Tyr302, His235 and Asp194 in the α-amylase from Bacillus licheniformis.

The calcium-binding residues, Tyr302 and His235, and the sodium-binding residue, Asp194, on the activity of Bacillus licheniformis α-amylase were investigated using site-directed mutagenesis. Tyr302 and His235 were replaced by Asn and Asp, respectively, to produce the mutants Y302N and H235D; Asp194 was replaced by Ala to produce D194A. The mutant amylases were purified to homogeneity; each was ~53 kDa.