Remote optical fiber sensing based on reflectance due to the swelling of polymer particles produced by dispersion polymerization

Poly (4-vinyl pyridine) particles produced by dispersion polymerization were suspended in a hydrogel membrane and used for remote measurements employing fiber optic sensors. The refractive index of poly(4-vinyl pyridine) particles is higher than the refractive index of the hydrogel. At low pH, protonation of the poly(vinyl pyridine) causes the particles to swell reducing their refractive index and lowering membrane turbidity. The membrane response to pH was monitored using instrumentation originally that was constructed by Michael Civiello and was further developed in this work. A new hydrogel, HYPAN, was evaluated as the medium in which the particles are suspended. Methods for attaching a polymer layer to the distal end of an optical fiber were also examined. A 1310 nm wavelength source and an InGaAs detector were installed in the remote sensing instrument to improve signal quality by lowering the noise associated with the signal. The noise associated with the instrument response results from two sources, one being Rayleigh scattering of the laser pulse as it travels down the optical fiber. The other contribution to the background is the reflection from the optical fiber connector/polymer interface at the distal end of the optical fiber. The use of longer wavelength source compared to 834 nm reduced the background signal. The noise associated with the signal at the longer wavelength, however, is increased compared to the original, 834 nm. The use of angled connectors in the instrument reduced the background of the signal and enhanced the turbidity signal by a factor of three. Using and improving the instrumentation designed for remote optical sensing, it was possible to detect pH changes through 500 meters of optical fiber. The particles produced from 4-vinyl pyridine showed quick response times and relatively large changes in response when placed in a HYPAN membrane. The pKa of these particles was determined to be approximately 4.6 through 500 meters of fiber. Sensors were constructed on the top of an optical fiber connector, because we could not develop a convenient method for attaching a polymer layer on the distal end of an unconnectorized optical fiber

Characteristics of ferroelectric-ferroelastic domains in N{\'e}el-type skyrmion host GaV4_4S8_8

GaV$_4$S$_8$ is a multiferroic semiconductor hosting N{\'e}el-type magnetic skyrmions dressed with electric polarization. At T$_s$ = 42K, the compound undergoes a structural phase transition of weakly first-order, from a non-centrosymmetric cubic phase at high temperatures to a polar rhombohedral structure at low temperatures. Below T$_s$, ferroelectric domains are formed with the electric polarization pointing along any of the four $\left< 111 \right>$ axes. Although in this material the size and the shape of the ferroelectric-ferroelastic domains may act as important limiting factors in the formation of the N{\'e}el-type skyrmion lattice emerging below T$_C$=13\:K, the characteristics of polar domains in GaV$_4$S$_8$ have not been studied yet. Here, we report on the inspection of the local-scale ferroelectric domain distribution in rhombohedral GaV$_4$S$_8$ using low-temperature piezoresponse force microscopy. We observed mechanically and electrically compatible lamellar domain patterns, where the lamellae are aligned parallel to the (100)-type planes with a typical spacing between 100 nm-1.2 $\mu$m. We expect that the control of ferroelectric domain size in polar skyrmion hosts can be exploited for the spatial confinement and manupulation of N{\'e}el-type skyrmions

Mesin Pencari Berbasiskan Semantik Untuk Bahasa Indonesia

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Identification of palmitoyltransferase and thioesterase enzymes that control the subcellular localization of axon survival factor nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2).

The NAD-synthesizing enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) is a critical survival factor for axons and its constant supply from neuronal cell bodies into axons is required for axon survival in primary culture neurites and axon extension in vivo. Recently, we showed that palmitoylation is necessary to target NMNAT2 to post-Golgi vesicles, thereby influencing its protein turnover and axon protective capacity. Here we find that NMNAT2 is a substrate for cytosolic thioesterases APT1 and APT2 and that palmitoylation/depalmitoylation dynamics are on a time scale similar to its short half-life. Interestingly, however, depalmitoylation does not release NMNAT2 from membranes. The mechanism of palmitoylation-independent membrane attachment appears to be mediated by the same minimal domain required for palmitoylation itself. Furthermore, we identify several zDHHC palmitoyltransferases that influence NMNAT2 palmitoylation and subcellular localization, among which a role for zDHHC17 (HIP14) in neuronal NMNAT2 palmitoylation is best supported by our data. These findings shed light on the enzymatic regulation of NMNAT2 palmitoylation and highlight individual thioesterases and palmitoyltransferases as potential targets to modulate NMNAT2-dependent axon survival.This work was supported by a Medical Research Council studentship (to S. M.) and a Biotechnology and Biological Sciences Research Council Institute Strategic Programme Grant (to M. P. C.)

Axonal trafficking of NMNAT2 and its roles in axon growth and survival in vivo

The NAD-synthesizing enzyme NMNAT2 is critical for axon survival in primary culture and its depletion may contribute to axon degeneration in a variety of neurodegenerative disorders. Here we discuss several recent reports from our laboratory that establish a critical role for NMNAT2 in axon growth in vivo in mice and shed light on the delivery and turnover of this survival factor in axons. In the absence of NMNAT2, axons fail to extend more than a short distance beyond the cell body during embryonic development, implying a requirement for NMNAT2 in axon maintenance even during development. Furthermore, we highlight findings regarding the bidirectional trafficking of NMNAT2 in axons on a vesicle population that undergoes fast axonal transport in primary culture neurites and in mouse sciatic nerve axons in vivo. Surprisingly, loss of vesicle association boosts the axon protective capacity of NMNAT2, an effect that is at least partially mediated by a longer protein half-life of cytosolic NMNAT2 variants. Analysis of wild-type and variant NMNAT2 in mouse sciatic nerves and Drosophila olfactory receptor neuron axons supports the existence of a similar mechanism in vivo, highlighting the potential for regulation of NMNAT2 stability and turnover as a mechanism to modulate axon degeneration in vivo

Axonal trafficking of NMNAT2 and its roles in axon growth and survival in vivo.

The NAD-synthesizing enzyme NMNAT2 is critical for axon survival in primary culture and its depletion may contribute to axon degeneration in a variety of neurodegenerative disorders. Here we discuss several recent reports from our laboratory that establish a critical role for NMNAT2 in axon growth in vivo in mice and shed light on the delivery and turnover of this survival factor in axons. In the absence of NMNAT2, axons fail to extend more than a short distance beyond the cell body during embryonic development, implying a requirement for NMNAT2 in axon maintenance even during development. Furthermore, we highlight findings regarding the bidirectional trafficking of NMNAT2 in axons on a vesicle population that undergoes fast axonal transport in primary culture neurites and in mouse sciatic nerve axons in vivo. Surprisingly, loss of vesicle association boosts the axon protective capacity of NMNAT2, an effect that is at least partially mediated by a longer protein half-life of cytosolic NMNAT2 variants. Analysis of wild-type and variant NMNAT2 in mouse sciatic nerves and Drosophila olfactory receptor neuron axons supports the existence of a similar mechanism in vivo, highlighting the potential for regulation of NMNAT2 stability and turnover as a mechanism to modulate axon degeneration in vivo

Subcellular localization determines the stability and axon protective capacity of axon survival factor Nmnat2.

Axons require a constant supply of the labile axon survival factor Nmnat2 from their cell bodies to avoid spontaneous axon degeneration. Here we investigate the mechanism of fast axonal transport of Nmnat2 and its site of action for axon maintenance. Using dual-colour live-cell imaging of axonal transport in SCG primary culture neurons, we find that Nmnat2 is bidirectionally trafficked in axons together with markers of the trans-Golgi network and synaptic vesicles. In contrast, there is little co-migration with mitochondria, lysosomes, and active zone precursor vesicles. Residues encoded by the small, centrally located exon 6 are necessary and sufficient for stable membrane association and vesicular axonal transport of Nmnat2. Within this sequence, a double cysteine palmitoylation motif shared with GAP43 and surrounding basic residues are all required for efficient palmitoylation and stable association with axonal transport vesicles. Interestingly, however, disrupting this membrane association increases the ability of axonally localized Nmnat2 to preserve transected neurites in primary culture, while re-targeting the strongly protective cytosolic mutants back to membranes abolishes this increase. Larger deletions within the central domain including exon 6 further enhance Nmnat2 axon protective capacity to levels that exceed that of the slow Wallerian degeneration protein, Wld(S). The mechanism underlying the increase in axon protection appears to involve an increased half-life of the cytosolic forms, suggesting a role for palmitoylation and membrane attachment in Nmnat2 turnover. We conclude that Nmnat2 activity supports axon survival through a site of action distinct from Nmnat2 transport vesicles and that protein stability, a key determinant of axon protection, is enhanced by mutations that disrupt palmitoylation and dissociate Nmnat2 from these vesicles