Two-Photon Absorption Light-Induced Self-Written Waveguide for Single-Mode Optical Interconnection

International audienceWe propose two-photon absorption light-induced self-written (LISW) waveguide formation using short-wavelength infrared pulse laser light. It is suitable and efficient for single-mode optical interconnection, and also promising for small-core single-mode optical interconnection. The approach offers the possibility of not only decreasing the insertion loss, but also reducing the interconnection task time. We assessed this approach for single-mode optical interconnection. We obtained an LISW waveguide loss of about 0.06 dB for an LISW waveguide length of 100 μm and a connection loss per facet of about 0.37 dB. We also presented the results on the interconnection between high-numerical-aperture small-core thermally-diffused expanded-core single-mode fibers having the mode field diameters of about 3 μm by using the same approach. The results showed the present approach to be a promising alternative route for efficient interconnection of small-core single-mode optical devices, such as silicon nanowires with appropriate configurations

Supplementary document for Solid -state optical scanning device using beam -combiner and switch array - 6572022.pdf

Supplement

Identification of sites in apolipoprotein A-I susceptible to chymase and carboxypeptidase A digestion

Synopsis MCs (mast cells) adversely affect atherosclerosis by promoting the progression of lesions and plaque destabilization. MC chymase cleaves apoA-I (apolipoprotein A-I), the main protein component of HDL (high-density lipoprotein). We previously showed that C-terminally truncated apoA-I (cleaved at the carboxyl side of Phe 225 ) is present in normal human serum using a newly developed specific mAb (monoclonal antibody). In the present study, we aimed to identify chymase-induced cleavage sites in both lipid-free and lipid-bound (HDL 3 ) forms of apoA-I. Lipid-free apoA-I was preferentially digested by chymase, at the C-terminus rather than the N-terminus. Phe 229 and Tyr 192 residues were the main cleavage sites. Interestingly, the Phe 225 residue was a minor cleavage site. In contrast, the same concentration of chymase failed to digest apoA-I in HDL 3 ; however, a 100-fold higher concentration of chymase modestly digested apoA-I in HDL 3 at only the N-terminus, especially at Phe 33 . CPA (carboxypeptidase A) is another MC protease, colocalized with chymase in severe atherosclerotic lesions. CPA, in vitro, further cleaved C-terminal Phe 225 and Phe 229 residues newly exposed by chymase, but did not cleave Tyr 192 . These results indicate that several forms of C-terminally and N-terminally truncated apoA-I could exist in the circulation. They may be useful as new biomarkers to assess the risk of CVD (cardiovascular disease)

Effects of Myeloperoxidase-Induced Oxidation on Antiatherogenic Functions of High-Density Lipoprotein

High-density lipoprotein (HDL) has protective effects against the development of atherosclerosis; these effects include reverse cholesterol transport, antioxidant ability, and anti-inflammation. Myeloperoxidase (MPO) secreted by macrophages in atherosclerotic lesions generates tyrosyl radicals in apolipoprotein A-I (apoA-I) molecules, inducing the formation of apoA-I/apoA-II heterodimers through the tyrosine-tyrosine bond in HDL. Functional characterization of HDL oxidized by MPO could provide useful information about the significance of apoA-I/apoA-II heterodimers measurement. We investigated the effects of MPO-induced oxidation on the antiatherogenic functions of HDL as described above. The antioxidant ability of HDL, estimated as the effect on LDL oxidation induced by copper sulfate, was not significantly affected after MPO oxidation. HDL reduced THP-1 monocyte migration by suppressing the stimulation of human umbilical vein endothelial cells induced by lipopolysaccharide (LPS). MPO-oxidized HDL also showed inhibition of THP-1 chemotaxis, but the extent of inhibition was significantly attenuated compared to intact HDL. MPO treatment did not affect the cholesterol efflux capacity of HDL from [3H]-cholesterol-laden macrophages derived from THP-1 cells. The principal effect of MPO oxidation on the antiatherogenic potential of HDL would be the reduction of anti-inflammatory ability, suggesting that measurement of apoA-I/apoA-II heterodimers might be useful to estimate anti-inflammatory ability of HDL

Light-induced self-written waveguide fabrication using 1550 nm laser light

International audienceLight-induced self-written (LISW) optical waveguides were fabricated for the first time, to the best of our knowledge, using a photopolymerizable resin system formed by 1550 nm pulse laser light. A two-photon absorption (TPA) chromophore with a TPA cross section of several hundred Goeppert-Mayer (GM) at 1550 nm was used. Furthermore, the optical interconnection between a single-mode fiber and a fiber Bragg grating was demonstrated by the present technique, using one-way irradiation of 1550 nm laser light through the single-mode fiber. The LISW waveguide formation using 1550 nm laser light offers a new and promising alternative route for optical interconnection in silicon photonics technology

Identification of sites in apolipoprotein A-I susceptible to chymase and carboxypeptidase A digestion

MCs (mast cells) adversely affect atherosclerosis by promoting the progression of lesions and plaque destabilization. MC chymase cleaves apoA-I (apolipoprotein A-I), the main protein component of HDL (high-density lipoprotein). We previously showed that C-terminally truncated apoA-I (cleaved at the carboxyl side of Phe225) is present in normal human serum using a newly developed specific mAb (monoclonal antibody). In the present study, we aimed to identify chymase-induced cleavage sites in both lipid-free and lipid-bound (HDL3) forms of apoA-I. Lipid-free apoA-I was preferentially digested by chymase, at the C-terminus rather than the N-terminus. Phe229 and Tyr192 residues were the main cleavage sites. Interestingly, the Phe225 residue was a minor cleavage site. In contrast, the same concentration of chymase failed to digest apoA-I in HDL3; however, a 100-fold higher concentration of chymase modestly digested apoA-I in HDL3 at only the N-terminus, especially at Phe33. CPA (carboxypeptidase A) is another MC protease, co-localized with chymase in severe atherosclerotic lesions. CPA, in vitro, further cleaved C-terminal Phe225 and Phe229 residues newly exposed by chymase, but did not cleave Tyr192. These results indicate that several forms of C-terminally and N-terminally truncated apoA-I could exist in the circulation. They may be useful as new biomarkers to assess the risk of CVD (cardiovascular disease)