Magnetic skyrmion moved by the spin-Hall effect is promising for the application of the generation racetrack memories. However, the Magnus force causes a deflected motion of skyrmion, which limits its application. Here, we create an antiferromagnetic skyrmion by injecting a spin-polarized pulse in the nanostripe and investigate the spin Hall effect-induced motion of antiferromagnetic skyrmion by micromagnetic simulations. In contrast to ferromagnetic skyrmion, we find that the antiferromagnetic skyrmion has three evident advantages: (i) the minimum driving current density of antiferromagnetic skyrmion is about two orders smaller than the ferromagnetic skyrmion; (ii) the velocity of the antiferromagnetic skyrmion is about 57 times larger than the ferromagnetic skyrmion driven by the same value of current density; (iii) antiferromagnetic skyrmion can be driven by the spin Hall effect without the influence of Magnus force. In addition, antiferromagnetic skyrmion can move around the pinning sites due to its property of topological protection. Our results present the understanding of antiferromagnetic skyrmion motion driven by the spin Hall effect and may also contribute to the development of antiferromagnetic skyrmion-based racetrack memories.

Abstract-Cytochrome P450 1B1, expressed in vascular smooth muscle cells, can metabolize arachidonic acid in vitro into several products including 12-and 20-hydroxyeicosatetraenoic acids that stimulate vascular smooth muscle cell growth. This study was conducted to determine whether cytochrome P450 1B1 contributes to angiotensin II-induced rat aortic smooth muscle cell migration, proliferation, and protein synthesis. Angiotensin II stimulated migration of these cells, measured by the wound healing approach, by 1. Metabolism of arachidonic acid to 5-, 12-, 15-, and 20-hydoxyeicosatetraenoic acids in these cells was not altered, but angiotensin II-and arachidonic acid-induced reactive oxygen species production and extracellular signal-regulated kinase 1/2 and p38 mitogen-activated protein kinase activity were inhibited by 2,4,3Ј,5Ј-tetramethoxystilbene and cytochrome P450 1B1 small hairpin RNA (shRNA) and by Tempol, which inactivates reactive oxygen species. Tempol did not alter cytochrome P450 1B1 activity. These data suggest that angiotensin II-induced vascular smooth muscle cell migration and growth are mediated by reactive oxygen species generated from arachidonic acid by cytochrome P450 1B1 and activation of extracellular signal-regulated kinase 1/2 and p38 mitogen-activated protein kinase. (Hypertension. 2010;55:1461-1467.) Key Words: angiotensin II Ⅲ CYP1B1 Ⅲ vascular smooth muscle cell growth Ⅲ ROS T he renin-angiotensin system is one of the major components of the mechanisms that contribute to the regulation of blood volume and vascular resistance. 1 Angiotensin II (Ang II), the main biologically active agent of this system, also stimulates vascular smooth muscle cell (VSMC) hypertrophy and/or hyperplasia and inflammation and contributes to the development of hypertension, atherosclerosis, heart failure, and restenosis after vascular injury. [1][2][3][4][5][6] The pathophysiological actions of Ang II are mediated by activation of Ն1 serine-threonine and tyrosine kinase, generation of oxygen radicals, 7-9 and/or release of arachidonic acid (AA) by cytosolic phospholipase A 2 (cPLA 2 ) and production of its metabolites, 12-hydroxyeicosatetraenoic acid (12-HETE) and 20-HETE, generated via lipoxygenase and/or cytochrome P450 (CYP) 4A, respectively. 10 -18 Both 12-and 20-HETE promote VSMC migration, hyperplasia, and/or hypertrophy. 11,19 -22 CYP enzymes that metabolize xenobiotics, including polycyclic aromatic hydrocarbons and endobiotics, such as fatty acids and retinoids, are also expressed in extrahepatic tissues, including the cardiovascular system. 23-27 CYP1A1-encoded enzymes are expressed in vascular endothelium and smooth muscle cells, with much higher levels of activity in endothelial cells, whereas CYP1B1 is highly expressed in VSMCs and, to a lesser degree, in endothelial cells, 28,29 but shear stress upregulates mRNA and protein levels of CYP1A1 and CYP1B1 in endothelial cells. 30 Whether CYP1A1 and CYP1B1 contribute to the vascular function is not known. Recombinant CYP1B1 has been shown to me...

Chiral magnets endowed with topological spin textures are expected to have promising applications in next‐generation magnetic memories. In contrast to the well‐studied 2D or 3D magnetic skyrmions, the authors report the discovery of 1D nontrivial magnetic solitons in a transition metal dichalcogenide 2H‐TaS2 via precise intercalation of Cr elements. In the synthetic Cr1/3TaS2 (CTS) single crystal, the coupling of the strong spin–orbit interaction from TaS2 and the chiral arrangement of the magnetic Cr ions evoke a robust Dzyaloshinskii–Moriya interaction. A magnetic helix having a short spatial period of ≈25 nm is observed in CTS via Lorentz transmission electron microscopy. In a magnetic field perpendicular to the helical axis, the helical spin structure transforms into a chiral soliton lattice (CSL) with the spin structure evolution being consistent with the chiral sine‐Gordon theory, which opens promising perspectives for the application of CSL to fast‐speed nonvolatile magnetic memories. This work introduces a new paradigm to soliton physics and provides an effective strategy for seeking novel 2D magnets.

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Controllable manipulations of magnetic skyrmions are essential for next-generation spintronic devices. Here, the duplication and merging of skyrmions, as well as logical AND and OR functions, are designed in antiferromagnetic (AFM) materials with a cusp or smooth Y-junction structures. The operational time are in the dozens of picoseconds, enabling ultrafast information processing. A key factor for the successful operation is the relatively complex Y-junction structures, where domain walls propagate through in a controlled manner, without significant risks of pinning, vanishing or unwanted depinning of existing domain walls, as well as the nucleation of new domain walls. The motions of a multi-bit, namely the motion of an AFM skyrmion-chain in racetrack, are also investigated. Those micromagnetic simulations may contribute to future AFM skyrmion-based spintronic devices, such as nanotrack memory, logic gates and other information processes.

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Reactive oxygen species (ROS) contribute to various models of hypertension, including deoxycorticosterone acetate (DOCA)-salt-induced hypertension. Recently, we have shown that ROS, generated by cytochrome P-450 1B1 (CYP1B1) from arachidonic acid, mediate vascular smooth muscle cell growth caused by angiotensin II. This study was conducted to determine the contribution of CYP1B1 to hypertension and associated pathophysiological changes produced by DOCA (30 mg/kg) given subcutaneously per week with 1% NaCl + 0.1% KCl in drinking water to uninephrectomized rats for 6 wk. DOCA-salt treatment increased systolic blood pressure (SBP). Injections of the selective inhibitor of CYP1B1, 2,3',4,5'-tetramethoxystilbene (TMS; 300 μg/kg ip every 3rd day) initiated at the 4th week of DOCA-salt treatment normalized SBP and decreased CYP1B1 activity but not its expression in the aorta, heart, and kidney. TMS also inhibited cardiovascular and kidney hypertrophy, prevented the increase in vascular reactivity and endothelial dysfunction, and minimized the increase in urinary protein and K(+) output and the decrease in urine osmolality, Na(+) output, and creatinine clearance associated with DOCA-salt treatment. These pathophysiological changes caused by DOCA-salt treatment and associated increase in vascular superoxide production, NADPH oxidase activity, and expression of NOX-1, and ERK1/2 and p38 MAPK activities in the aorta, heart, and kidney were inhibited by TMS. These data suggest that CYP1B1 contributes to DOCA-salt-induced hypertension and associated pathophysiological changes, most likely as a result of increased ROS production and ERK1/2 and p38 MAPK activity, and could serve as a novel target for the development of agents like TMS to treat hypertension.

Angiotensin II (Ang II) stimulates protein synthesis by activating spleen tyrosine kinase (Syk) and DNA synthesis through epidermal growth factor receptor (EGFR) transactivation in vascular smooth muscle cells (VSMCs). This study was conducted to determine whether Syk mediates Ang II-induced migration of aortic VSMCs using a scratch wound approach. Treatment with Ang II (200 nM) for 24 h increased VSMC migration by 1.56 Ϯ 0.14-fold. Ang II-induced VSMC migration and Syk phosphorylation as determined by Western blot analysis were minimized by the Syk inhibitor piceatannol (10 M) and by transfecting VSMCs with dominant-negative but not wild-type Syk plasmid. Ang II-induced VSMC migration and Syk phosphorylation were attenuated by inhibitors of c-Src [4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP2)], p38 mitogen-activated protein kinase (MAPK) [4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)1H-imidazole (SB202190)], and extracellular signal-regulated kinase (ERK) 1/2 [1,4-diamino-2,3-dicyano-1,4-bis(2-aminophenylthio) butadiene (U0126)]. SB202190 attenuated p38 MAPK and c-Src but not ERK1/2 phosphorylation, indicating that p38 MAPK acts upstream of c-Src and Syk. The c-Src inhibitor PP2 attenuated Syk and ERK1/2 phosphorylation, suggesting that c-Src acts upstream of Syk and ERK1/2. Ang II-and epidermal growth factor (EGF)-induced VSMC migration and EGFR phosphorylation were inhibited by the EGFR blocker 4-(3-chloroanilino)-6,7-dimethoxyquinazoline (AG1478) (2 M). Neither the Syk inhibitor piceatannol nor the dominant-negative Syk mutant altered EGFinduced cell migration or Ang II-and EGF-induced EGFR phosphorylation. The c-Src inhibitor PP2, dominant negative mutant of Src or Src small interfering RNA did not alter EGF-induced VSMC migration and EGFR, ERK1/2, and p38 MAPK phosphorylation. The ERK1/2 inhibitor U0126 (10 M) attenuated EGF-induced cell migration and ERK1/2 but not EGFR phosphorylation. These data suggest that Ang II stimulates VSMC migration via p38 MAPKactivated c-Src through Syk and via EGFR transactivation through ERK1/2 and partly through p38 MAPK.