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SPARC (osteonectin/BM40) is a secreted protein that modifies the interaction of cells with extracellular matrix (ECM). When we added SPARC to cultured rabbit synovial fibroblasts and analyzed the secreted proteins, we observed an increase in the expression of three metalloproteinases--collagenase, stromelysin, and the 92-kD gelatinase-- that together can degrade both interstitial and basement membrane matrices. We further characterized the regulation of one of these metalloproteinases, collagenase, and showed that both collagenase mRNA and protein are upregulated in fibroblasts treated with SPARC. Experiments with synthetic SPARC peptides indicated that a region in the neutral alpha-helical domain III of the SPARC molecule, which previously had no described function, was involved in the regulation of collagenase expression by SPARC. A sequence in the carboxyl-terminal Ca(2+)-binding domain IV exhibited similar activity, but to a lesser extent. SPARC induced collagenase expression in cells plated on collagen types I, II, III, and V, and vitronectin, but not on collagen type IV. SPARC also increased collagenase expression in fibroblasts plated on ECM produced by smooth muscle cells, but not in fibroblasts plated on a basement membrane-like ECM from Engelbreth-Holm-Swarm sarcoma. Collagenase was induced within 4 h in cells treated with phorbol diesters or plated on fibronectin fragments, but was induced after 8 h in cells treated with SPARC. A number of proteins were transiently secreted by SPARC-treated cells within 6 h of treatment. Conditioned medium that was harvested from cultures 7 h after the addition of SPARC, and depleted of residual SPARC, induced collagenase expression in untreated fibroblasts; thus, part of the regulation of collagenase expression by SPARC appears to be indirect and proceeds through a secreted intermediate. Because the interactions of cells with ECM play an important role in regulation of cell behavior and tissue morphogenesis, these results suggest that molecules like SPARC are important in modulating tissue remodeling and cell-ECM interactions.

Silicon photonics has great potential for mid-wave-infrared applications. The dispersion of waveguide can be manipulated by waveguide dimension and cladding materials. Simulation shows that < 3 mu m wide conversion can be achieved by tuning the pump wavelength. (C) 2010 Optical Society of America

An ultra-broadband wavelength conversion is presented and experimentally demonstrated based on nondegenerate four-wave mixing in silicon waveguides. Two idlers can be generated and their wavelengths can be freely tuned by using two pumps where the first pump is set close to the signal and the second pump is wavelength tunable. Using this scheme, a small phase-mismatch and hence an ultra-broad conversion bandwidth is realized in spite of the waveguide dispersion profile. We show that the experimental demonstrations are consistent with the theoretical estimations. Total conversion bandwidth is estimated to reach > 500 nm and it can provide a feasible approach to realize one-to-two wavelength conversion among different telecommunication bands between 1300 nm and 1800 nm. (C) 2010 Optical Society of America

The performance of wavelength conversion based on nondegenerate four-wave mixing (FWM) with two pumps is theoretically evaluated in a silicon nanowire waveguide. A theoretical model is developed to take into the limitations of nonlinear loss parameters on conversion bandwidth, efficiency, and uniformity. Analysis shows that the conversion bandwidth of two-pump nondegenerate FWM is >30\\% broader than the conversion bandwidth of the degenerate FWM without compromising the conversion efficiency under the same pump power level. Also the results indicate that the improvement originates from efficient phase matching over broader bandwidth range due to two-wavelength pumps. [ABSTRACT FROM PUBLISHER]