Virtually all the known physico-chemical and biological techniques have been explored for treatment of extremely recalcitrant dye wastewater; none, however, has emerged as a panacea. A single universally applicable end-of-pipe solution appears to be unrealistic, and combination of appropriate techniques is deemed imperative to devise technically and economically feasible options. An in-depth evaluation of wide range of potential hybrid technologies delineated in literature along with plausible analyses of available cost information has been furnished. In addition to underscoring the indispensability of hybrid technologies, this paper also endorses the inclusion of energy and water reuse plan within the treatment scheme, and accordingly proposes a conceptual hybrid dye wastewater treatment system. Keywords GeoQUEST

We describe here the involvement of calciumactivated neutral protease (CANP or calpain, EC 3.4.22.17) in calcium-dependent proteolytic processing of the precursor of human interleukin la (IL-la) into mature IL-la. Calcium ionophore ionomycin enhanced proteolytic processing of pre-IL-la and the release of mature IL-la either from lipopolysaccharide (LPS)-activated human adherent mononuclear cells or from a human bladder carcinoma cell line (HTB9 5637) that constitutively produces human IL-la and -P. The proteolytic processing of pre-IL-la was completely inhibited by EGTA. Similar calcium-dependent proteolytic processing of pre-IL-la was also observed with lysates of either LPS-activated human adherent mononuclear cells or HTB9 5637 cells. Since the optimal pH for processing was between 7 and 8, and E-64 (a cysteine protease inhibitor) and leupeptin (a serine and cysteine protease inhibitor) both inhibited this processing by cell lysates, we hypothesized that a calcium-activated neutral protease, CANP, might be responsible for this processing. This hypothesis was supported by data showing that the specific CANP inhibitor peptide inhibited this proteolysis in cell lysates in a dose-dependent fashion (IC50 = 0.05 IM) and that treatment of pre-IL-la with purified CANP yielded the 17-kDa mature form of IL-la, which has an amino terminus identical with that reported for mature human IL-la. Taken together, these findings indicate that calcium-dependent proteolytic processing of pre-IL-la is selectively mediated by CANP.Interleukin 1 (IL-1), produced by a variety of cells, is widely known to manifest multiple biological activities on various types of target cells (1). Two biochemically distinct forms of IL-1, IL-la and -/3, have been genetically cloned (2-4). Although both types of IL-1 are lacking in a signal peptide, they have been reported to be present not only in the cytosol (5) but also in the cell membrane (6) and extracellularly. Since mature IL-1 has a molecular mass of 17 kDa, precursor IL-1 (pre-IL-1; molecular mass of 33-35 kDa) presumably is processed by an as-yet-unidentified proteolytic enzyme(s) to generate mature IL-1.A calcium ionophore has been reported to augment production of extracellular IL-1 by lipopolysaccharide (LPS)-stimulated human adherent mononuclear cells through the entry of exogenous calcium into cells (7). LPS also has been shown to increase intracellular calcium in macrophages (8).On the other hand, there are some cell types, such as HTB9 5637, which constitutively produce pre-IL-1 but do not generate and release mature IL-1 effectively (ref. 9; unpublished results). We, therefore, decided to test the possibility that calcium plays some roles in release and/or processing of IL-1 by comparative studies of this cell line and human adherent mononuclear cells. We examined the effects of calcium ionophore on the release and processing of IL-1 in detail, and we identified a major calcium-dependent proteolytic processing enzyme of pre-IL-la as calcium-activated neutral protease (CANP ...

Killer cell lectin-like receptor G1 (KLRG1) is an inhibitory receptor expressed on subsets of natural killer (NK) cells and T cells, for which no endogenous ligands are known. Here, we show that KLRG1 binds three of the classical cadherins (E-, N-, and R-), which are ubiquitously expressed in vertebrates and mediate cell–cell adhesion by homotypic or heterotypic interactions. By expression cloning using the mouse KLRG1 tetramer as a probe, we identified human E-cadherin as a xenogeneic ligand. We also identified a syngeneic interaction between mouse KLRG1 and mouse E-cadherin. Furthermore, we show that KLRG1 binds N- and R-cadherins. Finally, we demonstrate that E-cadherin binding of KLRG1 prevents the lysis of E-cadherin–expressing targets by KLRG1+ NK cells. These results suggest that KLRG1 ligation by E-, N-, or R-cadherins may regulate the cytotoxicity of killer cells to prevent damage to tissues expressing the cadherins.

Methylglyoxal (MG) is one of the side-products in glycolysis, and it reacts with proteins under physiological conditions. Here, we identified heat-shock protein 27 (Hsp27) as a major MG-modified protein in cells. MG modification of Hsp27 selectively occurs at Arg-188 to form argpyrimidine, and mutation in the residue represses the formation of a large oligomer. This modification process is essential to its repressing activity for cytochrome c-mediated caspase activation. Inhibition of MG modification of Hsp27 causes sensitization of the cells to anti-tumor drug-induced apoptosis. Thus, MG is a novel modulator of cell survival by directly incorporating with the specific protein residue.