Self-Lubricating and Shape-Stable Phase-Change Materials Based on Epoxy Resin and Vegetable Oils.

Palm or coconut oil is capable of dissolving in a mixture of bisphenol A-based epoxy resin and a high-temperature hardener (4,4'-diaminodiphenyl sulfone) when heated and then forms a dispersed phase as a result of cross-linking and molecular weight growth of the epoxy medium. Achieving the temporary miscibility between the curing epoxy matrix and the vegetable oil allows a uniform distribution of vegetable oil droplets in the epoxy medium. This novel approach to creating a dispersed phase-change material made a cured epoxy polymer containing up to 20% oil. The miscibility of epoxy resin and oil was studied by laser interferometry, and phase state diagrams of binary mixtures were calculated according to theory and experiments. A weak effect of oil on the viscosity and kinetics of the epoxy resin curing was demonstrated by rotational rheometry. According to differential scanning calorimetry and dynamic mechanical analysis, the oil plasticizes the epoxy matrix slightly, expanding its glass transition region towards low temperatures and reducing its elastic modulus. In the cured epoxy matrix, oil droplets have a diameter of 3-14 µm and are incapable of complete crystallization due to their multi-component chemical composition and non-disappeared limited miscibility. The obtained phase-change materials have relatively low specific energy capacity but can be used alternatively as self-lubricating low-noise materials due to dispersed oil, high stiffness, and reduced friction coefficient. Palm oil crystallizes more readily, better matching the creation of phase-change materials, whereas coconut oil crystallization is more suppressed, making it better for reducing the friction coefficient of the oil-containing material.

Epoxy Phase-Change Materials Based on Paraffin Wax Stabilized by Asphaltenes.

The usual problem of meltable phase-change agents is the instability in their form upon heating, which can be solved by placing them into a continuous polymer matrix. Epoxy resin is a suitable medium for dispersing molten agents, but it is necessary to make the obtained droplets stable during the curing of the formed phase-change material. This work shows that molten paraffin wax forms a Pickering emulsion in an epoxy medium and in the presence of asphaltenes extracted from heavy crude oil. Theoretical calculations revealed the complex equilibrium in the epoxy/wax/asphaltene triple system due to their low mutual solubility. Rheological studies showed the viscoplastic behavior of the obtained dispersions at 25 °C, which disappears upon the heating and melting of the paraffin phase. Wax and asphaltenes increased the viscosity of the epoxy medium during its curing but did not inhibit cross-linking or reduce the glass transition temperature of the cured polymer. As a result of curing, it is possible to obtain phase-change materials containing up to 45% paraffin wax that forms a dispersed phase with a size of 0.2-6.5 µm. The small size of dispersed wax can decrease its degree of crystallinity to 13-29% of its original value, reducing the efficiency of the phase-change material.

Palladin expression is a conserved characteristic of the desmoplastic tumor microenvironment and contributes to altered gene expression.

The stroma surrounding solid tumors contributes in complex ways to tumor progression. Cancer-associated fibroblasts (CAFs) are the predominant cell type in the tumor stroma. Previous studies have shown that the actin-binding protein palladin is highly expressed in the stroma of pancreas tumors, but the interpretation of these results is complicated by the fact that palladin exists as multiple isoforms. In the current study, the expression and localization of palladin isoform 4 was examined in normal specimens and adenocarcinomas of human pancreas, lung, colon, and stomach samples. Immunohistochemistry with isoform-selective antibodies revealed that expression of palladin isoform 4 was higher in adenocarcinomas versus normal tissues, and highest in CAFs. Immunohistochemistry staining revealed that palladin was present in both the cytoplasm and the nucleus of CAFs, and this was confirmed using immunofluorescence staining and subcellular fractionation of a pancreatic CAF cell line. To investigate the functional significance of nuclear palladin, RNA Seq analysis of palladin knockdown CAFs versus control CAFs was performed, and the results showed that palladin regulates the expression of genes involved in the biosynthesis and assembly of collagen, and organization of the extracellular matrix. These results suggested that palladin isoform 4 may play a conserved role in establishing the phenotype of CAFs in multiple tumor types.

Palladin is upregulated in kidney disease and contributes to epithelial cell migration after injury.

Recovery from acute kidney injury involving tubular epithelial cells requires proliferation and migration of healthy cells to the area of injury. In this study, we show that palladin, a previously characterized cytoskeletal protein, is upregulated in injured tubules and suggest that one of its functions during repair is to facilitate migration of remaining cells to the affected site. In a mouse model of anti-neutrophilic cytoplasmic antibody involving both tubular and glomerular disease, palladin is upregulated in injured tubular cells, crescents and capillary cells with angiitis. In human biopsies of kidneys from patients with other kidney diseases, palladin is also upregulated in crescents and injured tubules. In LLC-PK1 cells, a porcine proximal tubule cell line, stress induced by transforming growth factor-ß1 (TGF-ß1) leads to palladin upregulation. Knockdown of palladin in LLC-PK1 does not disrupt cell morphology but does lead to a defect in cell migration. Furthermore, TGF-ß1 induced increase in the 75 kDa palladin isoform occurs in both the nucleus and the cytoplasm. These data suggest that palladin expression is induced in injured cells and contributes to proper migration of cells in proximal tubules, possibly by regulation of gene expression as part of the healing process after acute injury.

Headless Myo10 is a negative regulator of full-length Myo10 and inhibits axon outgrowth in cortical neurons.

Myo10 is an unconventional myosin that localizes to and induces filopodia, structures that are critical for growing axons. In addition to the ~240-kDa full-length Myo10, brain expresses a ~165 kDa isoform that lacks a functional motor domain and is known as headless Myo10. We and others have hypothesized that headless Myo10 acts as an endogenous dominant negative of full-length Myo10, but this hypothesis has not been tested, and the function of headless Myo10 remains unknown. We find that cortical neurons express both headless and full-length Myo10 and report the first isoform-specific localization of Myo10 in brain, which shows enrichment of headless Myo10 in regions of proliferating and migrating cells, including the embryonic ventricular zone and the postnatal rostral migratory stream. We also find that headless and full-length Myo10 are expressed in embryonic and neuronal stem cells. To directly test the function of headless and full-length Myo10, we used RNAi specific to each isoform in mouse cortical neuron cultures. Knockdown of full-length Myo10 reduces axon outgrowth, whereas knockdown of headless Myo10 increases axon outgrowth. To test whether headless Myo10 antagonizes full-length Myo10, we coexpressed both isoforms in COS-7 cells, which revealed that headless Myo10 suppresses the filopodia-inducing activity of full-length Myo10. Together, these results demonstrate that headless Myo10 can function as a negative regulator of full-length Myo10 and that the two isoforms of Myo10 have opposing roles in axon outgrowth.

Myosin-X: a MyTH-FERM myosin at the tips of filopodia.

Myosin-X (Myo10) is an unconventional myosin with MyTH4-FERM domains that is best known for its striking localization to the tips of filopodia and its ability to induce filopodia. Although the head domain of Myo10 enables it to function as an actin-based motor, its tail contains binding sites for several molecules with central roles in cell biology, including phosphatidylinositol (3,4,5)-trisphosphate, microtubules and integrins. Myo10 also undergoes fascinating long-range movements within filopodia, which appear to represent a newly recognized system of transport. Myo10 is also unusual in that it is a myosin with important roles in the spindle, a microtubule-based structure. Exciting new studies have begun to reveal the structure and single-molecule properties of this intriguing myosin, as well as its mechanisms of regulation and induction of filopodia. At the cellular and organismal level, growing evidence demonstrates that Myo10 has crucial functions in numerous processes ranging from invadopodia formation to cell migration.

A novel form of motility in filopodia revealed by imaging myosin-X at the single-molecule level.

Although many proteins, receptors, and viruses are transported rearward along filopodia by retrograde actin flow, it is less clear how molecules move forward in filopodia. Myosin-X (Myo10) is an actin-based motor hypothesized to use its motor activity to move forward along actin filaments to the tips of filopodia. Here we use a sensitive total internal reflection fluorescence (TIRF) microscopy system to directly visualize the movements of GFP-Myo10. This reveals a novel form of motility at or near the single-molecule level in living cells wherein extremely faint particles of Myo10 move in a rapid and directed fashion toward the filopodial tip. These fast forward movements occur at approximately 600 nm/s over distances of up to approximately 10 microm and require Myo10 motor activity and actin filaments. As expected for imaging at the single-molecule level, the faint particles of GFP-Myo10 are diffraction limited, have an intensity range similar to single GFP molecules, and exhibit stepwise bleaching. Faint particles of GFP-Myo5a can also move toward the filopodial tip, but at a slower characteristic velocity of approximately 250 nm/s. Similar movements were not detected with GFP-Myo1a, indicating that not all myosins are capable of intrafilopodial motility. These data indicate the existence of a novel system of long-range transport based on the rapid movement of myosin molecules along filopodial actin filaments.