A case report of ciprofol overdose during anesthesia/analgesia and literature review: clinical presentation, blood pressure, and management.

Ciprofol is a novel intravenous anesthetic agent and a highly selective gamma-aminobutyric acid-A receptor agonist, similar to propofol. This is the first report about ciprofol overdose occurring during the maintenance phase of anesthesia for a surgical intervention. The accidental administration of an excessive ciprofol dose to a 37-year-old woman admitted to our hospital for laparoscopic myomectomy occurred during the first 3 minutes of maintenance anesthesia, in which the administered dose was 3.67 mg/kg instead of 0.06 mg/kg. The patient's bispectral index (BIS) decreased to 0 after 6 minutes and returned to 26 after 23 minutes, after which the surgery was restarted and successfully completed with the planned ciprofol maintenance anesthesia dose. During the 23 minutes after ciprofol overdose, the patient's vital signs were stable with the lowest mean arterial pressure being 69.3 mmHg. The patient regained consciousness quickly and recovered well after myomectomy. The patient's BIS decreased progressively, whereas her blood pressure, heart rate, and oxygen saturation did not change significantly. In the present case of ciprofol overdose, the observed stable blood pressure protected against organ injury during laparoscopic myomectomy.

Construction of a Corneal Stromal Equivalent with SMILE-Derived Lenticules and Fibrin Glue.

The scarcity of corneal tissue to treat deep corneal defects and corneal perforations remains a challenge. Currently, small incision lenticule extraction (SMILE)-derived lenticules appear to be a promising alternative for the treatment of these conditions. However, the thickness and toughness of a single piece of lenticule are limited. To overcome these limitations, we constructed a corneal stromal equivalent with SMILE-derived lenticules and fibrin glue. In vitro cell culture revealed that the corneal stromal equivalent could provide a suitable scaffold for the survival and proliferation of corneal epithelial cells, which formed a continuous pluristratified epithelium with the expression of characteristic markers. Finally, anterior lamellar keratoplasty in rabbits demonstrated that the corneal stromal equivalent with decellularized lenticules and fibrin glue could repair the anterior region of the stroma, leading to re-epithelialization and recovery of both transparency and ultrastructural organization. Corneal neovascularization, graft degradation, and corneal rejection were not observed within 3 months. Taken together, the corneal stromal equivalent with SMILE-derived lenticules and fibrin glue appears to be a safe and effective alternative for the repair of damage to the anterior cornea, which may provide new avenues in the treatment of deep corneal defects or corneal perforations.

Thioredoxin Binding Protein-2 Regulates Autophagy of Human Lens Epithelial Cells under Oxidative Stress via Inhibition of Akt Phosphorylation.

Oxidative stress plays an essential role in the development of age-related cataract. Thioredoxin binding protein-2 (TBP-2) is a negative regulator of thioredoxin (Trx), which deteriorates cellular antioxidant system. Our study focused on the autophagy-regulating effect of TBP-2 under oxidative stress in human lens epithelial cells (LECs). Human lens epithelial cells were used for cell culture and treatment. Lentiviral-based transfection system was used for overexpression of TBP-2. Cytotoxicity assay, western blot analysis, GFP/mCherry-fused LC3 plasmid, immunofluorescence, and transmission electronic microscopy were performed. The results showed that autophagic response of LECs with increased LC3-II, p62, and GFP/mCherry-LC3 puncta (P < 0.01) was induced by oxidative stress. Overexpression of TBP-2 further strengthens this response and worsens the cell viability (P < 0.01). Knockdown of TBP-2 attenuates the autophagic response and cell viability loss induced by oxidative stress. TBP-2 mainly regulates autophagy in the initiation stage, which is mTOR-independent and probably caused by the dephosphorylation of Akt under oxidative stress. These findings suggest a novel role of TBP-2 in human LECs under oxidative stress. Oxidative stress can cause cell injury and autophagy in LECs, and TBP-2 regulates this response. Hence, this study provides evidence regarding the role of TBP-2 in lens and the possible mechanism of cataract development.