Hand-assisted sputum excretion can effectively reduce postoperative pulmonary complications of esophageal cancer.

BACKGROUND: This study explores whether postoperative hand-assisted expectoration can reduce postoperative pulmonary complications (PPCs) in patients with esophageal cancer. METHODS: A retrospective analysis was performed on 543 patients undergoing radical esophageal cancer (EC) surgery in our hospital from October 2018 to August 2019, 156 of whom received postoperative handassisted sputum excretion (pulmonary rehabilitation, PR) and 387 of whom who did not receive postoperative hand-assisted sputum excretion (no pulmonary rehabilitation, NPR). Because the clinical characteristics of the two groups were not balanced, we used propensity score matching (PSM) to account for the variable factors of age, gender, body mass index (BMI), chronic respiratory comorbidity, smoking index, operation time, operation method, pathological stage. The main observation index used was PPCs. RESULTS: Among these 543 patients, 365 were male (67.2%), while 178 were female (32.8%). The age ranged from 30 to 82 years, with an average of 63.6±7.5 years old. In all, 342 patients (63%) underwent video-assisted thoracic surgery (VATS) surgery, while 201 patients (37%) underwent thoracotomy. Furthermore, 72 patients in the PR group received preoperative rehabilitation training and postoperative hand-assisted sputum excretion (combination pulmonary rehabilitation, CPR), while 87 patients only received postoperative hand-assisted sputum excretion (postoperative pulmonary rehabilitation, PPR). The patients in the PR group and the NPR group were uneven in terms of clinical characteristics, and we performed PSM as a result. After matching, PPC incidence in patients in the PR group was lower than that in the NPR group (P<0.05). CONCLUSIONS: Our results show that hand-assisted sputum excretion after EC surgery can reduce PPCs.

Evaluation of the Structure and Biological Activities of Condensed Tannins from Acanthus ilicifolius Linn and Their Effect on Fresh-Cut Fuji Apples.

Condensed tannins (CTS) have been isolated and purified from leaves of Acanthus ilicifolius Linn. And their structures were investigated by three methods: 13C nuclear magnetic resonance (13C NMR), reversed-phase high-performance liquid chromatography (RP-HPLC), and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). The results showed that the CTS were a mixture of catechin/epicatechin, galatechin/epicatechin, and amphicin/epigalin, and that the polymer chain lengths were 3-mers to 14-mers. Antityrosinase activities and antioxidant activities of the CTS from A. ilicifolius leaves were further studied. The IC50 of the CTS on mushroom tyrosinase activity was determined to be 19.7 ± 0.13 µg/mL, and inhibition type analyses indicated that the CTS were mixed type inhibitors and their inhibition CTS was reversible. The CTS from A. ilicifolius leaves also exhibited potential antioxidant activity. The IC50 of DPPH and ABTS scavenging activities were 104 ± 0.894 µg/mL and 86 ± 0.616 µg/mL, respectively. And the FRAP value was 758.28 ± 2.42 mg AAE/g. In addition, we found that the CTS from A. ilicifolius leaves had an excellent effect on preserving the quality of fresh-cut apples by preventing apples from browning through reducing polyphenol oxidase activities in apples.

Competitive Inhibition of Lysine Acetyltransferase 2B by a Small Motif of the Adenoviral Oncoprotein E1A.

The adenovirus early region 1A (E1A) oncoprotein hijacks host cells via direct interactions with many key cellular proteins, such as KAT2B, also known as PCAF (p300/CBP associated factor). E1A binds the histone acetyltransferase (HAT) domain of KAT2B to repress its transcriptional activation. However, the molecular mechanism by which E1A inhibits the HAT activity is not known. Here we demonstrate that a short and relatively conserved N-terminal motif (cNM) in the intrinsically disordered E1A protein is crucial for KAT2B interaction, and inhibits its HAT activity through a direct competition with acetyl-CoA, but not its substrate histone H3. Molecular modeling together with a series of mutagenesis experiments suggests that the major helix of E1A cNM binds to a surface of the acetyl-CoA pocket of the KAT2B HAT domain. Moreover, transient expression of the cNM peptide is sufficient to inhibit KAT2B-specific H3 acetylation H3K14ac in vivo Together, our data define an essential motif cNM in N-terminal E1A as an acetyl-CoA entry blocker that directly associates with the entrance of acetyl-CoA binding pocket to block the HAT domain access to its cofactor.