Characterization of CMOS metal based dielectric loaded surface plasmon waveguides at telecom wavelengths.

Dielectric loaded surface plasmon waveguides (DLSPPWs) comprised of polymer ridges deposited on top of CMOS compatible metal thin films are investigated at telecom wavelengths. We perform a direct comparison of the properties of copper (Cu), aluminum (Al), titanium nitride (TiN) and gold (Au) based waveguides by implementing the same plasmonic waveguiding configuration for each metal. The DLSPPWs are characterized by leakage radiation microscopy and a fiber-to-fiber configuration mimicking the cut-back method. We introduce the ohmic loss rate (OLR) to analyze quantitatively the properties of the CMOS metal based DLSPPWs relative to the corresponding Au based waveguides. We show that the Cu, Al and TiN based waveguides feature extra ohmic loss compared to Au of 0.027 dB/µm, 0.18 dB/µm and 0.52 dB/µm at 1550nm respectively. The dielectric function of each metal extracted from ellipsometric spectroscopic measurements is used to model the properties of the DLSP-PWs. We find a fairly good agreement between experimental and modeled DLSPPWs properties except for Al featuring a large surface roughness. Finally, we conclude that TiN based waveguides sustaining intermediate effective index (in the range 1.05-1.25) plasmon modes propagate over very short distances restricting the the use of those modes in practical situations.

Active reduction of fluctuations in fourth-order modulation instability.

We experimentally study the fluctuation properties of a scalar fourth-order modulation instability (MI) process obtained by pumping a photonic crystal fiber in the normal dispersion region. We observe large wavelength-dependent pulse-to-pulse fluctuations that cannot be significantly reduced by stimulating the process with a single seed. Their reduction requires two seeds slightly detuned from the maximum gain frequency in order to also stimulate the second-order MI process cascaded from the fourth-order one. This concept is validated by experiments and numerical simulations.

Spectral dynamics of modulation instability described using Akhmediev breather theory.

The Akhmediev breather formalism of modulation instability is extended to describe the spectral dynamics of induced multiple sideband generation from a modulated continuous wave field. Exact theoretical results describing the frequency domain evolution are compared with experiments performed using single mode fiber around 1550 nm. The spectral theory is shown to reproduce the depletion dynamics of an injected modulated continuous wave pump and to describe the Fermi-Pasta-Ulam recurrence and recovery towards the initial state. Realistic simulations including higher-order dispersion, loss, and Raman scattering are used to identify that the primary physical factors that preclude perfect recurrence are related to imperfect initial conditions.

NF-Y and Sp1 cooperate for the transcriptional activation and cAMP response of human tissue inhibitor of metalloproteinases-2.

The balance between matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs (TIMPs) is a key determinant in the homeostasis of the extracellular matrix. We have identified two cis-acting elements involved in the transcriptional regulation of TIMP-2. The first is an inverted CCAAT box located at position -73 to -69 in the TIMP-2 promoter that binds the transcription factor NF-Y. The second is a GAGGAGGGGG motif located at position -107 to -98, that binds the transcription factors Sp1 and Sp3. NF-Y and Sp1 cooperate for the basal transcription activity of the promoter. We then determined that TIMP-2 is transcriptionally up-regulated by cAMP analogs. Up-regulation of TIMP-2 by dibutyryl cAMP is a delayed response that requires de novo protein synthesis and does not affect RNA stability. The NF-Y and the Sp1 binding site are both involved in cAMP-dependent up-regulation of TIMP-2. Whereas NF-Y is essential for cAMP mediated regulation, Sp1 alone is not sufficient but enhances the activity of NF-Y. Dibutyryl cAMP has no effect on the expression of MMP-2 and MMP-9 and switches the MMP-TIMP balance in favor of the inhibitor.

Differential regulation of MMP-13 (collagenase-3) and MMP-3 (stromelysin-1) in mouse calvariae.

Bone resorption in mice involves the degradation of extracellular matrix. Whereas several proteases seem to be implicated in this process, it becomes increasingly clear that matrix metalloproteinases (MMPs), amongst them especially MMP-13 and MMP-3, play an essential role. We have purified MMP-13 and MMP-3 from mouse calvariae-conditioned media by differential fractionation and analyzed their collagenolytic, caseinolytic, gelatinolytic and proteoglycanolytic activities. It could be shown that in mouse calvariae-conditioned media most of the measured enzyme activities were due to MMP-13, although zymographies revealed that MMP-3, MMP-2, MMP-9 as well as TIMPs were present too. MMP-13 and MMP-3 proteins were detected and their enzyme activities were neutralized by specific polyclonal antisera. Furthermore, it was demonstrated that in cultures of mouse calvariae the production of MMP-13 was induced by the potent MMP-stimulator heparin and by parathyroid hormone (PTH), whereas the levels of MMP-3 remained unchanged. Although PTH-induced bone resorption was inhibited by calcitonin treatment, MMP-13 mRNA and protein expression were not significantly altered by this hormone. Together with previous observations, these results indicate that PTH regulates bone resorption through MMP-13, but not by MMP-3, and that its reversion by calcitonin involves neither of the two enzymes.

Structure and characterization of the human tissue inhibitor of metalloproteinases-2 gene.

We report here the characterization of the human tissue inhibitor of metalloproteinases-2 (TIMP-2) gene. The gene is 83 kilobase pairs (kb) long with exon-intron splicing sites located in preserved positions among the three members of the TIMP family. A 2.6-kb genomic DNA fragment flanking the 5'-end of the gene contains several regulatory elements including five Sp1, two AP-2, one AP-1, and three PEA-3 binding sites. Despite the presence of a complete AP-1 consensus at position -281, the promoter did not respond to 12-O-tetradecanoylphorbol-13-acetate treatment. However, 12-O-tetradecanoylphorbol-13-acetate response was generated by insertion of a similar AP-1 consensus at position -71, indicating the importance of the positioning of this motif. The promoter contains a typical CpG island; however, methylation of this island did not seem to influence gene expression. Analysis of the 3'-end of the gene revealed that the two mRNAs for TIMP-2 (1.2 and 3.8 kb) differ by the selection of their polyadenylation signal sites, but selection of these sites does not affect RNA stability. In summary, the TIMP-2 gene has several features observed in housekeeping genes, and differs significantly from TIMP-1 and TIMP-3 genes. These differences are likely to explain the specific roles that these inhibitors play in the regulation of matrix metalloproteinases.

Cloning and partial structure of the gene encoding human tissue inhibitor of metalloproteinases-3.

Using a cDNA probe, two genomic clones were obtained encoding the human tissue inhibitor of metalloproteinases-3 (TIMP-3). Analysis of these clones showed that they contained four distal exons and three introns of the gene. Although the intron-exon structure is similar to that of the timp1 gene, the first intron of the timp3 gene is much longer, being at least 17.5 kb in size.

Cloning and sequencing of a cDNA encoding mouse stromelysin 1.

A cDNA encoding mouse stromelysin 1 was cloned and the 1740-bp sequence was determined. The deduced amino acid (aa) sequence was compared with stromelysin 1 sequences of other mammals. Comparison with a previously published incomplete aa sequence of mouse stromelysin 1 revealed three single aa differences.