History of fertility preservation

Fertility preservation refers to a procedure performed to maintain the ability to become pregnant before receiving treatment with a risk of fertility loss, such as chemo- or radiation therapy. Examples of fertility-preserving procedures include freezing, sperm freezing, embryo freezing through in vitro fertilization, and ovarian tissue freezing.Current Concepts: Until the late 1990s, awareness of fertility preservation among clinicians and patients was relatively low, and the only way to preserve and restore fertility in women with cancer was the cryopreservation of embryos. However, as the survival rate of cancer patients increased and the treatment results of various diseases improved, interest in quality of life such as pregnancy and childbirth after treatment gradually increased, and became a driving force for the development of fertility preservation. In the 2000s, several centers began cryopreserving ovarian tissue, including primordial follicles from young patients before chemotherapy. Currently, ovarian tissue cryopreservation can be used in combination with in vitro maturation and egg vitrification techniques. Novel methods to improve follicle survival after transplantation are currently being investigated. Methods to improve follicle survival after transplantation and new ovarian protective agents to protect the ovaries from cytotoxic agents are currently being studied.Discussion and Conclusion: Advances in fertility-preserving technologies in the future will contribute to the delivery of healthy children by providing tailored treatments and more individualized fertility-preserving strategies to patients whose fertility is at risk.

The Factors Associated with High-Sensitivity C-Reactive Protein in Postmenopausal Women: Based on Korea National Health and Nutrition Examination Survey 2016–2017

Background@#Postmenopausal status increases the risk of cardiovascular disease, and C-reactive protein (CRP) constitutes an independent cardiovascular risk factor. This study aimed to investigate the factors associated with increased high-sensitivity CRP (hs-CRP) level in postmenopausal women. @*Methods@#We included postmenopausal women without laboratory test results that suggested acute inflammation who participated in the Korea National Health and Nutrition Examination Survey between 2016 and 2017. The participants were divided into high and low hs-CRP groups (cutoff value, 3.0 mg/L). We investigated factors that influenced the hs-CRP level with logistic regression analysis. @*Results@#The total number of subjects was 2,739, of whom 76.4% had low hs-CRP levels and 23.6% had high hs-CRP levels. The mean age and body mass index were higher in the high than in the low hs-CRP group. In the simple logistic regression analysis, high hs-CRP level was associated with smoking, whereas low hs-CRP level was associated with aerobic exercise, use of oral contraceptives, and history of pregnancy in postmenopausal women. When the analysis was adjusted for confounding variables, histories of smoking and pregnancy had a statistically significant association with high hs-CRP level. @*Conclusion@#This study showed that the important modifiable risk factors of elevated hs-CRP level in postmenopausal women of Korea include obesity, smoking, and lack of aerobic exercise, but well-controlled prospective investigations should be considered.

ERK-mediated phosphorylation of BIS regulates nuclear translocation of HSF1 under oxidative stress

B-cell lymphoma (BCL)-2-interacting cell death suppressor (BIS) has diverse cellular functions depending on its binding partners. However, little is known about the effects of biochemical modification of BIS on its various activities under oxidative stress conditions. In this study, we showed that H₂O₂ reduced BIS mobility on SDS–polyacrylamide gels in a time-dependent manner via the activation of extracellular signaling-regulated kinase (ERK). The combined results of mass spectroscopy and computational prediction identified Thr285 and Ser289 in BIS as candidate residues for phosphorylation by ERK under oxidative stress conditions. Deletion of these sites resulted in a partial reduction in the H₂O₂-induced mobility shift relative to that of the wild-type BIS protein; overexpression of the deletion mutant sensitized A172 cells to H₂O₂-induced cell death without increasing the level of intracellular reactive oxygen species. Expression of the BIS deletion mutant decreased the level of heat shock protein (HSP) 70 mRNA following H₂O₂ treatment, which was accompanied by impaired nuclear translocation of heat shock transcription factor (HSF) 1. Co-immunoprecipitation assays revealed that the binding of wild-type BIS to HSF1 was decreased by oxidative stress, while the binding of the BIS deletion mutant to HSF1 was not affected. These results indicate that ERK-dependent phosphorylation of BIS has a role in the regulation of nuclear translocation of HSF1 likely through modulation of its interaction affinity with HSF1, which affects HSP70 expression and sensitivity to oxidative stress.

Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle

BCL-2 interacting cell death suppressor (BIS), which is ubiquitously expressed, has important roles in various cellular processes, such as apoptosis, the cellular stress response, migration and invasion and protein quality control. In particular, BIS is highly expressed in skeletal and cardiac muscles, and BIS gene mutations result in human myopathy. In this study, we show that mRNA and protein levels of BIS were markedly increased during skeletal myogenesis in C2C12 cells and mouse satellite cells. BIS knockdown did not prevent the early stage of skeletal myogenesis, but did induce muscle atrophy and a decrease in the diameter of myotubes. BIS knockdown significantly suppressed the expression level of myosin heavy chain (MyHC) without changing the expression levels of myogenic marker proteins, such as Mgn, Cav-3 and MG53. In addition, BIS endogenously interacted with MyHC, and BIS knockdown induced MyHC ubiquitination and degradation. From these data, we conclude that molecular association of MyHC and BIS is necessary for MyHC stabilization in skeletal muscle.

Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle

BCL-2 interacting cell death suppressor (BIS), which is ubiquitously expressed, has important roles in various cellular processes, such as apoptosis, the cellular stress response, migration and invasion and protein quality control. In particular, BIS is highly expressed in skeletal and cardiac muscles, and BIS gene mutations result in human myopathy. In this study, we show that mRNA and protein levels of BIS were markedly increased during skeletal myogenesis in C2C12 cells and mouse satellite cells. BIS knockdown did not prevent the early stage of skeletal myogenesis, but did induce muscle atrophy and a decrease in the diameter of myotubes. BIS knockdown significantly suppressed the expression level of myosin heavy chain (MyHC) without changing the expression levels of myogenic marker proteins, such as Mgn, Cav-3 and MG53. In addition, BIS endogenously interacted with MyHC, and BIS knockdown induced MyHC ubiquitination and degradation. From these data, we conclude that molecular association of MyHC and BIS is necessary for MyHC stabilization in skeletal muscle.

Total Brain Failure: Controversies / 대한간질학회지

No abstract available.