A skin adhesive patch is the most fundamental and widely used medical device for diverse health-care purposes. Conventional skin adhesive patches have been mainly utilized for routine medical purposes such as wound management, fixation of medical devices, and simple drug release. In contrast to traditional skin adhesive patches, recently developed patches incorporate multiple key functions of bulky medical devices into a thin, flexible patch based on emerging nanomaterials and flexible electronic technologies. Consequently, the meaning of the term "skin adhesive patch" becomes broader and smarter compared to the traditional term. This review summarizes recent efforts undertaken in the development of multifunctional advanced skin adhesive patches, and briefly describes future directions and challenges toward the next generation of smart skin adhesive patches for ubiquitous personalized health care.

The optical glow of ceramics that becomes established during the constant state of flash, known as Stage III in flash sintering experiments, is investigated. The specimen temperature in this state is obtained from in-situ experiments at the Pohang Light Source II. The measurements of the specimen temperature agree very well with the predictions from the black body radiation model. The optical emission spectrum from the specimen is measured from the visible into the deep infrared, and compared with black body radiation that would have been expected from Joule heating. It is concluded that the specimens radiate by electroluminescence, which is ascribed to electron-hole recombination of excitons. The phenomenon is likely the same as discovered by Nernst at the turn of the twentieth century.

␣-Synuclein is a phosphoprotein that accumulates as a major component of Lewy bodies in the brains of patients with Parkinson disease. Synphilin-1, which is also present in Lewy bodies, binds with ␣-synuclein and forms cytoplasmic inclusions in transfected cells. Yet the molecular determinants of this protein-protein interaction are unknown. Here we report that casein kinase II (CKII) phosphorylates synphilin-1 and that the ␤ subunit of this enzyme complex binds to synphilin-1. Additionally, both CKII ␣ and ␤ subunits are present within cytoplasmic inclusions in cells that overexpress synphilin-1. Notably, the interaction between synphilin-1 and ␣-synuclein is markedly dependent on phosphorylation. Inhibition of CKII activity by 5,6-dichloro-1-␤-D-ribofuranosylbenzimidazole blocks the binding between these two proteins and significantly reduces the percentage of cells that contain eosinophilic cytoplasmic inclusions. Mutation of the major CKII phosphorylation site in ␣-synuclein (S129A) has no significant impact on the binding between ␣-synuclein and synphilin-1 or on the formation of synphilin-1/␣-synuclein-positive inclusions. These data suggest that the CKII-mediated phosphorylation of synphilin-1 rather than that of ␣-synuclein is critical in modulating their tendency to aggregate into inclusions. These observations collectively indicate that a ubiquitous post-translational modification such as phosphorylation can regulate inclusion body formation in the context of ␣-synuclein and synphilin-1 interaction. Parkinson disease (PD)1 is a common neurodegenerative disorder characterized by the loss of dopaminergic neurons in the substantia nigra pars compacta. Accumulating evidence suggests that aberrations in protein processing or folding leading to the aggregation of pathogenic proteins or their partners are a common theme in many degenerative disorders affecting the brain, including PD (1-3). Lewy bodies, classically considered as pathological hallmark features of PD, are proteinaceous cytoplasmic inclusions that consist of many components, among which ␣-synuclein is a major constituent (4, 5). The first indication for the pathogenic role of ␣-synuclein in PD came from the linkage of mutations in its gene with autosomal dominant forms of PD (6, 7). Another component of Lewy bodies is synphilin-1, which was discovered by screening for proteins that interact with ␣-synuclein (8). Co-expression of these two proteins results in the formation of cytoplasmic inclusions in a small percentage of cultured cells (8, 9). But the molecular determinants that regulate this interaction and perhaps consequent inclusion body formation are unknown. Such factors would elucidate not only the genesis of these aggregates but could also provide clues about potential therapeutic targets if the inclusions or their precursors are pathogenic.Phosphorylation is a common post-translational modification that regulates the function and other properties of many proteins. ␣-Synuclein itself is phosphorylated both in vitro and in vivo by casein...

The potent neurotrophic factor glial cell-derived neurotrophic factor (GDNF) is a distant member of the transforming growth factor-β (TGF-β) superfamily of proteins. We report a transcription factor that is the first nuclear protein known to be induced by GDNF, thus designated murine GDNF inducible factor (mGIF). The cDNA was cloned in the course of investigating transcription factors that bind to Sp1 consensus sequences, using thein situfilter detection method, and it was found to encode a protein having the same C2–H2zinc finger motif as Sp1. Sequence analysis indicated that mGIF is homologous to the human TGF-β inducible early gene (TIEG) and human early growth response gene-α (EGR-α). mGIF is widely distributed in the adult mouse with high mRNA levels in kidney, lung, brain, liver, heart, and testis. In the adult brain, mGIF is abundantly expressed in hippocampus, cerebral cortex, cerebellum, and amygdala with lower amounts in striatum, nucleus accumbens, olfactory tubercle, thalamus, and substantia nigra. During development, mGIF mRNA also has a wide distribution, including in cerebral cortex, cerebellar primordium, kidney, intestine, liver, and lung. GDNF induces the expression of mGIF rapidly and transiently both in a neuroblastoma cell line and in primary cultures of rat embryonic cortical neurons. Co-transfection of theDrosophilaSL2 cells using mGIF expression plasmid and reporter constructs having Sp1 binding sites indicated that mGIF represses transcription from a TATA-containing as well as from a TATA-less promoter. These observations suggest that the zinc finger transcription factor mGIF could be important in mediating some of the biological effects of GDNF.