[Application value of combined deep inhalation and breath-hold technique guided by four-dimensional CT in preoperative localization of solitary pulmonary nodules].

Objective: To explore the clinical value of four dimensional computed tomography (4 D CT) guided combined with deep inhalation and breath hold (DIBH) technique in the preoperative localization of solitary pulmonary nodules. Methods: The data of a total of 106 patients with solitary pulmonary nodules from March 2018 to May 2021 in the Ningbo First Hospital were collected retrospectively. Among them, there were 26 males and 80 females aged from 21 to 83 (47.4±14.2) years. According to different localization methods, 53 cases were divided into the control group, as the pulmonary nodules were located by CT guided injection of indocyanine green under calm breathing and 53 cases were divided into in the experimental group, as those patients were treated with indocyanine green injection under the guidance of 4 D CT combined with DIBH technology to locate pulmonary nodules. The three-dimensional distance deviation between pulmonary nodules and indocyanine green injection points was compared between the two groups to obtain the accuracy of pulmonary nodule localization. The preoperative positioning time of the two groups was compared by timing. Results: Among the 106 patients, there were 46 pure ground glass nodules, 32 sub solid nodules and 28 solid nodules, all of which were successfully localized before operation, with a success rate of 100%. The size of pulmonary nodules in the control group was (9.1±2.3) mm and the three-dimensional deviation[M(Q1, Q3)]between indocyanine green injection site and pulmonary nodules was X axis [7.0 (3.7, 12.6)] mm, Y axis [6.6 (2.9, 11.2)] mm, Z axis [3.0 (2.0, 6.0)]mm, respectively, and the preoperative positioning time was (11.4±3.8) min. The size of pulmonary nodules in the experimental group was (8.9±2.1) mm, and the deviations in 3 D direction were X axis [4.8 (3.0, 7.9)]mm, Y axis [3.8 (1.3, 7.5)]mm, Z axis [4.0 (2.0, 6.0)] mm, respectively. The preoperative positioning time was (9.3±3.0) min. There were statistically significant differences in preoperative positioning time and deviation of X and Y axis between the experimental group and the control group (P<0.05), but no statistically significant differences was found in deviation of Z axis (P>0.05). Conclusion: 4 D CT guided DIBH technology could improve the accuracy of preoperative localization of pulmonary nodules and save operation time, which is worthy of popularization.

Process of aerenchyma formation and reactive oxygen species induced by waterlogging in wheat seminal roots.

The development and regulation of aerenchyma in waterlogged conditions were studied in the seminal roots of wheat. Evans blue staining and the first cell death position indicated that the cortical cell death began at the root mid-cortex cells in flooding conditions. Continuous waterlogging treatment caused the spread of cell death from the mid-cortex to the neighboring cells and well-developed aerenchyma was formed after 72 h. Meanwhile, the formation of radial oxygen loss barrier was observed in the exodermis owing to the induction of Casparian bands and lignin deposition. Analysis of aerenchyma along the wheat root revealed that aerenchyma formed at 10 mm from the root tip, significantly increased toward the center of the roots, and decreased toward the basal region of the root. In situ detection of radial oxygen species (ROS) showed that ROS accumulation started in the mid-cortex cells, where cell death began indicating that cell death was probably accompanied by ROS production. Further waterlogging treatments resulted in the accumulation of ROS in the cortical cells, which were the zone for aerenchyma development. Accumulation and distribution of H2O2 at the subcellular level were revealed by ultracytochemical localization, which further verified the involvement of ROS in the cortical cell death process (i.e., aerenchyma formation). Furthermore, gene expression analysis indicated that ROS production might be the result of up-regulation of genes encoding for ROS-producing enzymes and the down-regulation of genes encoding for ROS-detoxifying enzymes. These results suggest that aerenchyma development in wheat roots starts in the mid-cortex cells and its formation is regulated by ROS.

Cell wall degradation and the dynamic changes of Ca2+ and related enzymes in the developing aerenchyma of wheat (Triticum aestivum L.) under waterlogging.

This research was aimed to study the cell wall degradation and the dynamic changes of Ca2+ and related enzymes in developing aerenchyma of wheat root under waterlogging. An examination of morphological development by light and electron microscope revealed that the structure of cell wall in middle cortical cells remained intact after 12 h of waterlogging and turned thinner after waterlogging for 24 h. At 48 h, the aerenchyma has been formed. The cellulase activity gradually increased in middle cortical cells within 24 h of waterlogging, and decreased with the formation of aerenchyma. Fluorescence detection and subcellular localization of Ca2+ showed the dynamic changing of Ca2+ at the cellular and subcellular levels during the development of aerenchyma. The activity of Ca2+-ATPase enhanced markedly in intercellular space, plasma membrane and tonoplast of some middle cortical cells after 8 h of waterlogging and remained high after 24 h, but it decreased after 48 h of waterlogging. All these suggests that cellulase, Ca2+ and Ca2+-ATPase show a dynamic distribution during the aerenchyma development which associated with the cell wall degradation of middle cortical cells. Moreover, there is a feedback regulation between Ca2+ and Ca2+-ATPase.

[Ventricular arrhythmias in patients with cor pulmonale].

This paper reported the results of 24 hours continuous ECG, day time and overnight arterial blood gas/pH and serum electrolytes in 20 patients with cor pulmonale, in order to investigate the rule of changes of ventricular arrhythmias (VA). The results were as follows: (1) Incidence of VA in 24 hours Holter Monitoring was 100%. (2) Frequent VPBs were increased significantly in period of acute attack (40%, P less than 0.05). (3) Non-sustained VT in the nocturnal (40%) was more than the day time in period of attack (P less than 0.05). (4) Relationship between VA and variables in period of attack: PaCO2 (r = 0.90) greater than arterial blood pH (r = -0.87) greater than PaO2 (r = -0.63); in relieved period VA were only related to serum potassium (r = -0.86). The authors speculated the severity of VA in period of attack was related with worse of arterial blood gas/pH, cardiac dysfunction and compensated enhance of sympathetic activity. It seems that the view accorded with theory of Yin-Yang in TCM.

Partial amino acid sequence of apolipoprotein(a) shows that it is homologous to plasminogen.

Apolipoprotein(a) [apo(a)] is a glycoprotein with Mr approximately equal to 280,000 that is disulfide linked to apolipoprotein B in lipoprotein(a) particles. Elevated plasma levels of lipoprotein(a) are correlated with atherosclerosis. Partial amino acid sequence of apo(a) shows that it has striking homology to plasminogen. Plasminogen is a plasma serine protease zymogen that consists of five homologous and tandemly repeated domains called kringles and a trypsin-like protease domain. The amino-terminal sequence obtained for apo(a) is homologous to the beginning of kringle 4 but not the amino terminus of plasminogen. Apo(a) was subjected to limited proteolysis by trypsin or V8 protease, and fragments generated were isolated and sequenced. Sequences obtained from several of these fragments are highly (77-100%) homologous to plasminogen residues 391-421, which reside within kringle 4. Analysis of these internal apo(a) sequences revealed that apo(a) may contain at least two kringle 4-like domains. A sequence obtained from another tryptic fragment also shows homology to the end of kringle 4 and the beginning of kringle 5. Sequence data obtained from two tryptic fragments show homology with the protease domain of plasminogen. One of these sequences is homologous to the sequences surrounding the activation site of plasminogen. Plasminogen is activated by the cleavage of a specific arginine residue by urokinase and tissue plasminogen activator; however, the corresponding site in apo(a) is a serine that would not be cleaved by tissue plasminogen activator or urokinase. Using a plasmin-specific assay, no proteolytic activity could be demonstrated for lipoprotein(a) particles. These results suggest that apo(a) contains kringle-like domains and an inactive protease domain.