Spin-Orbit Effects on Exciton Complexes in Diamond.

Ultrafine splittings are found in the optical absorption spectra of boron-doped diamond measured with high resolution. An analytical model of an exciton complex is developed, which permits assigning all absorption lines and sizing the interactions among the constituent charges and crystal field. We conclude that the entry of split-off holes in the acceptor-bound exciton fine structure yields two triplets separated by a spin-orbit splitting of 14.3 meV. Our findings thereby resolve a long-standing controversy [R. Sauer et al., Revised fine splitting of excitons in diamond, Phys. Rev. Lett. 84, 4172 (2000).PRLTAO0031-900710.1103/PhysRevLett.84.4172; M. Cardona et al., Comment on "Revised fine splitting of excitons in diamond,", Phys. Rev. Lett. 86, 3923 (2001).PRLTAO0031-900710.1103/PhysRevLett.86.3923; R. Sauer and K. Thonke, Sauer and Thonke reply, Phys. Rev. Lett. 86, 3924 (2001).PRLTAO0031-900710.1103/PhysRevLett.86.3924], revealing the underlying physics common in diverse semiconductors, including diamond.

A 3.06 µm Single-Photon Avalanche Diode Pixel with Embedded Metal Contact and Power Grid on Deep Trench Pixel Isolation for High-Resolution Photon Counting.

In this study, a 3.06 µm pitch single-photon avalanche diode (SPAD) pixel with an embedded metal contact and power grid on two-step deep trench isolation in the pixel is presented. The embedded metal contact can suppress edge breakdown and reduce the dark count rate to 15.8 cps with the optimized potential design. The embedded metal for the contact is also used as an optical shield and a low crosstalk probability of 0.4% is achieved, while the photon detection efficiency is as high as 57%. In addition, the integration of a power grid and the polysilicon resistor on SPAD pixels can help to reduce the voltage drop in anode power supply and reduce the power consumption with SPAD multiplication, respectively, in a large SPAD pixel array for a high-resolution photon-counting image sensor.

Nectin-like molecule-5 regulates intimal thickening after carotid artery ligation in mice.

OBJECTIVE: Intimal thickening is considered to result from the dedifferentiation of medial smooth muscle cells (SMCs) from a contractile to a synthetic phenotype, and their subsequent migration and proliferation. It is unknown whether nectin-like molecule (Necl)-5, which is overexpressed in cancer cells, is involved in intimal thickening. APPROACH AND RESULTS: Necl-5 was upregulated in mouse carotid artery after ligation. Compared with wild-type mice, intimal thickening after carotid artery ligation was milder in Necl-5 knockout mice. In vitro, the expression levels of SMC differentiation markers were higher, whereas the expression level of an SMC dedifferentiation marker was lower, in Necl-5 knockout mouse aortic SMCs (MASMCs) compared with wild-type MASMCs. The migration, proliferation, and extracellular signal-regulated kinase activity in response to serum were decreased in Necl-5 knockout MASMCs compared with wild-type MASMCs. In wild-type MASMCs, inhibition of extracellular signal-regulated kinase activity increased the expression levels of SMC differentiation markers and decreased their migration and proliferation in response to serum. CONCLUSIONS: The present findings indicate that Necl-5 plays a role in the formation of intimal thickening after carotid artery ligation by regulating dedifferentiation, migration, and proliferation of SMCs in an extracellular signal-regulated kinase-dependent manner. Our results suggest that Necl-5 may represent a potential therapeutic target to limit intimal thickening after vascular injury.

FGD5 mediates proangiogenic action of vascular endothelial growth factor in human vascular endothelial cells.

OBJECTIVE: Vascular endothelial growth factor (VEGF) exerts proangiogenic action and induces activation of a variety of proangiogenic signaling pathways, including the Rho family small G proteins. However, regulators of the Rho family small G proteins in vascular endothelial cells (ECs) are poorly understood. Here we attempted to clarify the expression, subcellular localization, downstream effectors, and proangiogenic role of FGD5, a member of the FGD family of guanine nucleotide exchange factors. METHODS AND RESULTS: FGD5 was shown to be selectively expressed in cultured human vascular ECs. Immunofluorescence microscopy showed that the signal for FGD5 was observed at peripheral membrane ruffles and perinuclear regions in human umbilical vein ECs. Overexpression of FGD5 increased Cdc42 activity, whereas knockdown of FGD5 by small interfering RNAs inhibited the VEGF-induced activation of Cdc42 and extracellular signal-regulated kinase. VEGF-promoted capillary-like network formation, permeability, directional movement, and proliferation of human umbilical vein ECs and the reorientation of the Golgi complex during directional cell movement were attenuated by knockdown of FGD5. CONCLUSIONS: This study provides the first demonstration of expression, subcellular localization, and function of FGD5 in vascular ECs. The results suggest that FGD5 regulates proangiogenic action of VEGF in vascular ECs, including network formation, permeability, directional movement, and proliferation.

Necl-5/poliovirus receptor interacts with VEGFR2 and regulates VEGF-induced angiogenesis.

RATIONALE: Vascular endothelial growth factor (VEGF), a major proangiogenic agent, exerts its proangiogenic action by binding to VEGF receptor 2 (VEGFR2), the activity of which is regulated by direct interactions with other cell surface proteins, including integrin α(V)ß(3). However, how the interaction between VEGFR2 and integrin α(V)ß(3) is regulated is not clear. OBJECTIVE: To investigate whether Necl-5/poliovirus receptor, an immunoglobulin-like molecule that is known to bind integrin α(V)ß(3), regulates the interaction between VEGFR2 and integrin α(V)ß(3), and to clarify the role of Necl-5 in the VEGF-induced angiogenesis. METHODS AND RESULTS: Necl-5-knockout mice displayed no obvious defect in vascular development; however, recovery of blood flow after hindlimb ischemia and the VEGF-induced neovascularization in implanted Matrigel plugs were impaired in Necl-5-knockout mice. To clarify the mechanism of the regulation of angiogenesis by Necl-5, we investigated the roles of Necl-5 in the VEGF-induced angiogenic responses in vitro. Knockdown of Necl-5 by siRNAs in human umbilical vein endothelial cells (HUVECs) inhibited the VEGF-induced capillary-like network formation on Matrigel, migration, and proliferation, and conversely, enhanced apoptosis. Coimmunoprecipitation assays showed the interaction of Necl-5 with VEGFR2, and knockdown of Necl-5 prevented the VEGF-induced interaction of integrin α(V)ß(3) with VEGFR2. Knockdown of Necl-5 suppressed the VEGFR2-mediated activation of downstream proangiogenic and survival signals, including Rap1, Akt, and endothelial nitric oxide synthase. CONCLUSIONS: These results demonstrate the critical role of Necl-5 in angiogenesis and suggest that Necl-5 may regulate the VEGF-induced angiogenesis by controlling the interaction of VEGFR2 with integrin α(v)ß(3), and the VEGFR2-mediated Rap1-Akt signaling pathway.