ABSTRACT
Pheochromocytoma has a significant effect on perioperative hemodynamics; however, little is known about the changes caused by pheochromocytoma in pregnant women during cesarean delivery. Moreover, cesarean delivery in pregnant women with pheochromocytoma is often performed, along with pheochromocytoma removal, under general anesthesia depending on the time of delivery. Therefore, changes in the hemodynamics of these patients during cesarean delivery under spinal anesthesia combined with epidural anesthesia, along with their serum catecholamine concentration, have not been reported. In this report, we describe the changes in the maternal intraoperative hemodynamics and serum catecholamine level of a pregnant woman with pheochromocytoma who underwent cesarean delivery under combined spinal-epidural anesthesia at 35 weeks of gestation. No significant change in the hemodynamics and serum catecholamine level was observed, and the procedure was carried out safely. Cesarean delivery in an optimized pheochromocytoma patient under combined spinal-epidural anesthesia might be feasible without concurrent surgical removal of pheochromocytoma.
ABSTRACT
Before surgery and other invasive treatments, decisions must be made on whether to discontinue drugs and provide appropriate drug holidays especially for antithrombotic drugs, and this is made difficult by the large number of available drugs and associated guidelines. We have therefore developed an online application for perioperative drug discontinuation and resumption management, named Saga Application for Management of Drug Holidays in PeriOperative Periods (SAMPOP).Multidisciplinary medical staff at Saga University Hospital (SUH) worked together to build an evidence-based Perioperative Drug Discontinuation Management Database (PDDMD) and developed the user-friendly SAMPOP online application via preliminary verification at SUH. From September 2018 to February 2020, 420 medical staff at SUH, including physicians, nurses, and pharmacists, installed and tested SAMPOP.Rate per surgical procedure for forgetting to discontinue antithrombotic drugs preoperatively decreased from 0.18% to 0.09% as of August 2019, 12 months after the introduction of SAMPOP (Pâ=â.1359). In addition, six months later, it decreased further to 0.03% as of February 2020 (Pâ=â.0436). Forgetting to resume antithrombotic drugs postoperatively decreased from 0.20% to 0.02% as of August 2019, 12 months after the introduction of SAMPOP (Pâ=â.0008). There was no case of forgetting to resume the medication in the last 6 months.SAMPOP may be useful for management of drug holidays in the clinic and warrants further evaluation of its safety and efficacy.
Subject(s)
Blood Loss, Surgical/prevention & control , Fibrinolytic Agents/administration & dosage , Medication Therapy Management/organization & administration , Perioperative Period , Electronic Health Records , Humans , InternetABSTRACT
Robotically-assisted surgery using da Vinci® surgical system is a challenging technology as a minimally- invasive operation. However, few Japanese institutions employ robotic surgery for procedures involving the upper intestinal tract because its advantages have not been fully established. Robotic gastrectomy requires more complicated devices and procedures than con- ventional laparoscopic surgery. For example, da Vinci® system covers the patient's upper body during the operation, and anesthesiologists are forced to be far away from the head. This is a disadvantage for airway management, especially during emergency situation. Thus, all procedures and potential risk factors should be simulated and planned before the operation. In addi- tion to their role in anesthetic management, anesthesi- ologists are expected to play important roles as coordinators of the medical staffs during surgery.
Subject(s)
Anesthetics , Intestines/surgery , Robotic Surgical Procedures , Gastrectomy , Humans , Minimally Invasive Surgical Procedures , Robotic Surgical Procedures/instrumentationABSTRACT
According to a survey of anesthesia-related critical incidents by the Japanese Society of Anesthesiologists, hemorrhage was the major cause of cardiac arrest developing in the operating room. To deal with critical hemorrhage swiftly, not only cooperation between anesthesiologists and surgeons but also the linkage of operating rooms with transfusion management divisions and the blood center is important. It is desirable for the hospital transfusion committee to prepare hospital regulations on 'actions to be taken to manage critical hemorrhage', and practice the implementation of these guidelines by simulated drills. When critical hemorrhage occurs, a person in charge is appointed, and an emergency is declared (call for manpower and notification of the emergency to the transfusion management divisions). A person in charge comprehensively assesses the hemostatic condition, hemodynamics, laboratory data, and blood product supply system, and consults the operator regarding the continuation of surgery or changing surgical procedures. When time is short, the cross-matching test is omitted, and the ABO-identical blood is used. When a supply of the identical ABO-type blood is not available, compatible blood type is used. The evolving concept of hemostatic resuscitation seems to be important to prevent coagulopathy, which easily develops during massive hemorrhage. Anesthesiologists should be aware of the risk of such an emergency transfusion and procedures to be taken to switch to transfusion of the ABO-identical blood. Establishment of a hospital emergency transfusion system depends on the overall capability of the critical and crisis management systems of the hospital.
Subject(s)
Anesthesiology , Blood Transfusion , Hemorrhage/therapy , Intraoperative Care , Intraoperative Complications/therapy , Practice Guidelines as Topic , Risk Management , Societies, Medical , Blood Grouping and Crossmatching , Blood Loss, Surgical , Blood Transfusion/methods , Emergencies , Humans , Interdisciplinary Communication , Japan , Patient Care Team , Risk , Transfusion ReactionABSTRACT
It is known that mitochondrial DNA (mtDNA) replication is independent of the cell cycle. Even in post-mitotic cells in which nuclear DNA replication has ceased, mtDNA is believed to still be replicating. Here, we investigated the turnover rate of mtDNA in primary rat hepatocytes, which are quiescent cells. Southwestern blot analysis using 5-bromo-2'-deoxyuridine (BrdU) was employed to estimate the activity of full-length mtDNA replication and to determine efficient doses of replication inhibitors. Southern blot analysis showed that a two-day treatment with 20mM 2',3'-dideoxycytidine and 0.2mug/ml ethidium bromide caused a 37% reduction in the amount of mtDNA, indicating that the hepatocytes had a considerably high rate of turnover of mtDNA. Further, pulse-chase analysis using Southwestern analysis showed that the amount of newly synthesized mtDNA labeled with BrdU declined to 60% of the basal level within two days. Because the rate of reduction of the new mtDNA was very similar to the overall turnover rate described above, it appears that degrading mtDNA molecules were randomly chosen. Thus, we demonstrated that there is highly active and random turnover of mtDNA in hepatocytes.
Subject(s)
DNA, Mitochondrial/metabolism , Hepatocytes/cytology , Hepatocytes/metabolism , Mitochondria, Liver/genetics , Mitochondria, Liver/metabolism , Animals , Bromouracil/metabolism , Cells, Cultured , DNA Replication , Male , Rats , Rats, Sprague-Dawley , Time FactorsABSTRACT
During replication, human mitochondrial DNA (mtDNA) takes on a triple-stranded structure known as a D-loop, which is implicated in replication and transcription. 1-Methyl-4-phenylpyridinium ion (MPP+), a toxin inducing parkinsonism, inhibits mtDNA replication, possibly by resolving the D-loops. For initiation of mtDNA replication, mitochondria are thought to have another triple-stranded structure, an R-loop. The R-loop, which is resolved by a bacterial junction-specific helicase, RecG, is also resolved by MPP+. Because mitochondrial D-loops are likewise resolved by RecG, the D- and R-loops may share a similar branched structure. MPP+ resolves cruciform DNA in supercoiled DNA. MPP+ converts a stacked conformation to an extended conformation in a synthetic Holliday junction. This conversion is reversed by 1 mM Mg(2+), as is the resolution of the D-loops or cruciform DNA. These observations suggest that the junction structure of mitochondrial D- and R-loops is affected by MPP+.
Subject(s)
1-Methyl-4-phenylpyridinium/chemistry , 1-Methyl-4-phenylpyridinium/pharmacology , DNA, Mitochondrial/chemistry , DNA, Mitochondrial/drug effects , Escherichia coli Proteins , Nucleic Acid Conformation/drug effects , Parkinsonian Disorders , Bacterial Proteins/chemistry , Bacterial Proteins/pharmacology , DNA Helicases/chemistry , DNA Helicases/pharmacology , DNA, Superhelical/chemistry , DNA, Superhelical/drug effects , Dose-Response Relationship, Drug , HeLa Cells , Humans , Intercalating Agents/chemistry , Intercalating Agents/pharmacology , Magnesium/pharmacology , Parkinsonian Disorders/chemically inducedABSTRACT
During replication, mitochondrial DNA (mtDNA) takes on a triple-stranded structure called a D-loop. Although their physiological roles are not understood, D-loops are implicated in replication and transcription of mtDNA. Little is known about the turnover of D-loops. We investigated the effects of mitochondrial transcription factor A (TFAM) and single-stranded DNA-binding protein (mtSSB) on D-loops. In human HeLa cells, TFAM and mtSSB are, respectively, 1700- and 3000-fold more abundant than mtDNA. This level of TFAM is two orders of magnitude higher than reported previously and is sufficient to wrap human mtDNA entirely. TFAM resolves D-loops in vitro if added in similar stoichiometries. mtSSB inhibits the resolution of mtDNA by TFAM but enhances resolution by RecG, a junction-specific helicase from Escherichia coli. Hence, mtSSB functions in both stabilization and resolution. We propose that TFAM and mtSSB are cooperatively involved in stabilizing D-loops and in the maintenance of mtDNA.