Bright Bifacial White-Light Illumination by Highly Deformable Electroluminescent Devices Based on Transparent Ionic-Hydrogel Electrodes and Quantum-Dot Color Conversion.

Deformable alternating-current electroluminescent (ACEL) devices are of increasing interest because of their potential to drive innovation in soft optoelectronics. Despite the research focus on efficient white ACEL devices, achieving deformable devices with high luminance remains difficult. In this study, this challenge is addressed by fabricating white ACEL devices using color-conversion materials, transparent and durable hydrogel electrodes, and high-k nanoparticles. The incorporation of quantum dots enables the highly efficient generation of red and green light through the color conversion of blue electroluminescence. Although the ionic-hydrogel electrode provides high toughness, excellent light transmittance, and superior conductivity, the luminance of the device is remarkably enhanced by the incorporation of a high-k dielectric, BaTiO3. The fabricated ACEL device uniformly emits very bright white light (489 cd m-2) with a high color-rendering index (91) from both the top and bottom. The soft and tough characteristics of the device allow seamless operation in various deformed states, including bending, twisting, and stretching up to 400%, providing a promising platform for applications in a wide array of soft optoelectronics.

Synthesis of UV/blue light-emitting aluminum hydroxide with oxygen vacancy and their application to electrically driven light-emitting diodes.

Aluminum hydroxide nanoparticles, one of the essential luminescent materials for display technology, bio-imaging, and sensors due to their non-toxicity, affordable pricing, and rare-earth-free phosphors, are synthesized via a simple method at a reaction time of 10 min at a low temperature of 200 °C. By controlling the precursor's ratio of aluminum acetylacetonate to oleic acid, UV or blue light-emitting aluminum hydroxides with oxygen defects and carbonyl radicals can be synthesized. As a result, aluminum hydroxide (Al(OH)3-x ) nanoparticles overwhelmingly emit UVA light (390 nm) because of the oxygen defects in nanoparticles, and carbon-related radicals on the nanoparticles are responsible for the blue-light emission at 465 nm. Electrically driven light-emitting devices are applied using luminescent aluminum hydroxide as an emissive layer, that consists of a cost-efficient inverted bottom-emission structure as [ITO (cathode)/ZnO/emissive layers/2,2'-bis(4-(carbazol-9-yl)phenyl)-biphenyl (BCBP)/MoO3/Al (anode)]. The device with aluminum hydroxide as an emissive layer shows a maximum luminance of 215.48 cd m-2 and external quantum efficiency (EQE) of 0.12%. The new method for synthesizing UV-blue emitting aluminum hydroxides and their application to LEDs will contribute to developing the field of non-toxic optoelectronic material or UV-blue emitting devices.

Double-Stranded RNA Enhances Matrix Metalloproteinase-1 and -13 Expressions through TLR3-Dependent Activation of Transglutaminase 2 in Dermal Fibroblasts.

UV-irradiation induces the secretion of double-stranded RNA (dsRNA) derived from damaged noncoding RNAs in keratinocytes, which enhance the expression of matrix metalloproteinases (MMP) in non-irradiated dermal fibroblasts, leading to dysregulation of extracellular matrix homeostasis. However, the signaling pathway responsible for dsRNA-induced MMP expression has not been fully understood. Transglutaminase 2 (TG2) is an enzyme that modifies substrate proteins by incorporating polyamine or crosslinking of proteins, thereby regulating their functions. In this study, we showed that TG2 mediates dsRNA-induced MMP-1 expression through NF-κB activation. Treatment of poly(I:C), a synthetic dsRNA analogue binding to toll-like receptor 3 (TLR3), generates ROS, which in turn activates TG2 in dermal fibroblast. Subsequently, TG2 activity enhances translocation of p65 into the nucleus, where it augments transcription of MMP. We confirmed these results by assessing the level of MMP expression in Tlr3-/-, TG2-knockdowned and Tgm2-/- dermal fibroblasts after poly(I:C)-treatment. Moreover, treatment with quercetin showed dose-dependent suppression of poly(I:C)-induced MMP expression. Furthermore, ex vivo cultured skin from Tgm2-/- mice exhibited a significantly reduced level of MMP mRNA compared with those from wild-type mice. Our results indicate that TG2 is a critical regulator in dsRNA-induced MMP expression, providing a new target and molecular basis for antioxidant therapy in preventing collagen degradation.

Transglutaminase 2 mediates UVB-induced matrix metalloproteinase-1 expression by inhibiting nuclear p65 degradation in dermal fibroblasts.

Matrix metalloproteinases (MMPs) play a key role in tissue remodelling by cleaving extracellular matrix (ECM) components. In the skin, UV irradiation increases expression of MMPs that causes dysregulation of ECM homeostasis in dermis, leading to acceleration of skin aging. However, the mediator(s) that links UV irradiation to the upregulation of MMPs have not been fully defined. Previously, we showed that UVB irradiation activated transglutaminase 2 (TG2) in keratinocytes, eliciting an inflammatory response by activating NF-κB signalling. In this study, we reported the role of TG2 in mediating the UVB-induced expression of MMP-1. In human dermal fibroblasts, UVB irradiation enhanced the expression and activity of TG2, which in turn promotes the expression of MMP-1. Analyses of MMP-1 promoter showed that activation of the NF-κB signalling pathway, rather than AP-1, was responsible for the TG2-mediated upregulation of MMP-1. Moreover, Western blot analysis revealed that TG2 increased the activity of NF-κB by inhibiting degradation of p65 in the nucleus. Furthermore, ex vivo skin from TG2-knockout mice exhibited significantly reduced levels of MMP-1 compared to that from wild-type mice. These results indicate that TG2 functions as a mediator for the UVB-induced expression of MMP-1 in dermal fibroblasts, providing a new target for preventing skin photodamage.

Transglutaminase 2 mediates UV-induced skin inflammation by enhancing inflammatory cytokine production.

UV irradiation elicits acute inflammation in the skin by increasing proinflammatory cytokine production in keratinocytes. However, the downstream protein target(s) that link UV radiation to the activation of signaling pathways responsible for cytokine expression have not been fully elucidated. In this study, we report a novel role of transglutaminase 2 (TG2), a member of the TG enzyme family whose activities are critical for cornified envelope formation, in mediating UV-induced inflammation. Our results showed that TG2-deficient mice exhibited reduced inflammatory responses to UV irradiation, including reduced erythema, edema, dilation of blood vessels, inflammatory cell infiltration, and levels of inflammatory cytokines. Using primary mouse keratinocytes and HaCaT cells, we found that UV irradiation-induced cytokine production by activating TG2, but not by upregulating TG2 expression, and that ER calcium release triggered by the UV-induced activation of phospholipase C was required for TG2 activation. Moreover, TG2 activity enhanced p65 phosphorylation, leading to an increase in NF-κB transcriptional activity. These results indicate that TG2 is a critical mediator of cytokine expression in the UV-induced inflammatory response of keratinocytes, and suggest that TG2 inhibition might be useful for preventing UV-related skin disorders, such as photoaging and skin cancer caused by chronic UV exposure.

Deubiquitinating enzyme USP22 positively regulates c-Myc stability and tumorigenic activity in mammalian and breast cancer cells.

The proto-oncogene c-Myc has a pivotal function in growth control, differentiation, and apoptosis and is frequently affected in human cancer, including breast cancer. Ubiquitin-specific protease 22 (USP22), a member of the USP family of deubiquitinating enzymes (DUBs), mediates deubiquitination of target proteins, including histone H2B and H2A, telomeric repeat binding factor 1, and cyclin B1. USP22 is also a component of the mammalian SAGA transcriptional co-activating complex. In this study, we explored the functional role of USP22 in modulating c-Myc stability and its physiological relevance in breast cancer progression. We found that USP22 promotes deubiquitination of c-Myc in several breast cancer cell lines, resulting in increased levels of c-Myc. Consistent with this, USP22 knockdown reduces c-Myc levels. Furthermore, overexpression of USP22 stimulates breast cancer cell growth and colony formation, and increases c-Myc tumorigenic activity. In conclusion, the present study reveals that USP22 in breast cancer cell lines increases c-Myc stability through c-Myc deubiquitination, which is closely correlated with breast cancer progression.

A tactile sensor using a conductive graphene-sponge composite.

For sensors that emulate human tactile perception, we suggest a simple method for fabricating a highly sensitive force sensor using a conductive polyurethane sponge where graphene flakes are self-assembled into the porous structure of the sponge. The complete sensor device shows a sensitive and reliable detection response for a broad range of pressure and dynamic pressure that correspond to human tactile perception. Sensitivity of the sensor to detect vibration is also confirmed with vertical actuations due to slipping over micro-scale ridge structures attached on the sensors. Based on the sensor's ability to detect both pressure and vibration, the sensor can be utilized as a flexible tactile sensor.

Ubiquitin-specific protease 22 (USP22) positively regulates RCAN1 protein levels through RCAN1 de-ubiquitination.

Protein ubiquitination can be reversed by de-ubiquitinating enzymes (DUBs), which are classified into two main classes, cysteine proteases and metalloproteases. Cysteine proteases include ubiquitin-specific proteases (USPs) and ubiquitin C-terminal hydrolases. USP22 is a USP family member and a component of the mammalian Spt-Ada-Gcn5 acetyltransferase transcriptional coactivating complex. Regulator of calcineurin 1 (RCAN1; also known as DSCR1 or MCIP1) functions as an endogenous inhibitor of calcineurin signaling. In the present study, we have identified a novel interaction between USP22 and RCAN1 (RCAN1-1S) in the mammalian cells. In addition, the overexpression of USP22 caused the increase of RCAN1 protein stability. USP22 antagonized the actions of FBW7, NEDD4-2, and ß-TrCP E3 ligase on RCAN1 and promoted RCAN1 de-ubiquitination. Moreover, we found that RCAN1 was bound to USP22 in basal conditions, and interferon-α (IFN-α) treatment caused the dissociation of RCAN1 from USP22, which subsequently triggered RCAN1 ubiquitination and proteasome degradation. Taken together, these results suggest that USP22 positively regulates RCAN1 levels, which would consequently affect diverse RCAN1-linked cellular processes, such as the inflammatory process involving the release of IFN-α.

Histone deacetylase 3 promotes RCAN1 stability and nuclear translocation.

Regulator of calcineurin 1 (RCAN1; also referred as DSCR1 or MCIP1) is located in close proximity to a Down syndrome critical region of human chromosome 21. Although RCAN1 is an endogenous inhibitor of calcineurin signaling that controls lymphocyte activation, apoptosis, heart development, skeletal muscle differentiation, and cardiac function, it is not yet clear whether RCAN1 might be involved in other cellular activities. In this study, we explored the extra-functional roles of RCAN1 by searching for novel RCAN1-binding partners. Using a yeast two-hybrid assay, we found that RCAN1 (RCAN1-1S) interacts with histone deacetylase 3 (HDAC3) in mammalian cells. We also demonstrate that HDAC3 deacetylates RCAN1. In addition, HDAC3 increases RCAN1 protein stability by inhibiting its poly-ubiquitination. Furthermore, HDAC3 promotes RCAN1 nuclear translocation. These data suggest that HDAC3, a new binding regulator of RCAN1, affects the protein stability and intracellular localization of RCAN1.