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Portable power sources and grid-scale storage both require batteries combining high energy density and low cost. Zinc metal battery systems are attractive due to the low cost of zinc and its high charge-storage capacity. However, under repeated plating and stripping, zinc metal anodes undergo a well-known problem, zinc dendrite formation, causing internal shorting. Here we show a backside-plating configuration that enables long-term cycling of zinc metal batteries without shorting. We demonstrate 800 stable cycles of nickel–zinc batteries with good power rate (20 mA cm−2, 20 C rate for our anodes). Such a backside-plating method can be applied to not only zinc metal systems but also other metal-based electrodes suffering from internal short circuits.

The conduction of the bivalent magnesium cation, Mg(2+), in an inorganic solid state material, Mg(BH4)(NH2), has been demonstrated. This material exhibited a high ionic conductivity of 10(-6) S cm(-1) at 150 °C, and its electrochemical window was estimated to be approximately 3 V using cyclic voltammetry.

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The mechanism of the acceleration of the catalytic activity of factor VIIa (VIIa) in the presence of tissue factor (TF) was investigated. To explore the VIIa's site(s) that correlates with TF-mediated acceleration, zymogen VII, VIIa, and active site-modified VIIa were prepared, and dissociation constants (K d ) for their bindings to TF or soluble TF in solution were determined. We found that conversion of zymogen VII to VIIa led to an increase in affinity (⌬⌬G When one assumes that free VIIa exists in equilibrium between minor active and dominant zymogen-like inactive conformational states, preferential binding of TF to the active state leads to a shift in equilibrium. We speculate that TF traps the active conformational state of VIIa and converts its zymogen-like state into an active state, thereby accelerating the VIIa activity.

Regulation of cell surface molecules by matrix metalloproteinases (MMPs), as well as MMPs-catalyzed degradation of extracellular matrix, is important for tumor invasion and metastasis. Our previous study (Kioi, M., Yamamoto, K., Higashi, S., Koshikawa, N., Fujita, K., and Miyazaki, K. (2003) Oncogene 22, 8662-8670) demonstrated that active matrilysin specifically binds to the surface of colon cancer cells and induces notable cell aggregation due to processing of the cell membrane protein(s). Furthermore, these aggregated cells showed a dramatically enhanced metastatic potential. To elucidate the mechanism of matrilysin-induced cell aggregation, we attempted to identify the matrilysin-binding substance on the cell surface. Here, we demonstrate that cholesterol sulfate on the cell surface is a major matrilysin-binding substance. We found that active matrilysin bound to the cell membrane and cholesterol sulfate incorporated into liposomes with similar affinities. Treatment of colon cancer cells with ␤-cyclodextrin significantly reduced not only matrilysin binding to the cell surface but also matrilysin-dependent proteolysis and cell aggregation. Interestingly, replenishment of cholesterol sulfate, but not cholesterol, neutralized the effects of ␤-cyclodextrin. Taken together, it is likely that binding of matrilysin to cholesterol sulfate facilitates the matrilysin-catalyzed modulation of cell surface proteins, thus inducing the cancer cell aggregation. Matrix metalloproteinases (MMPs)2 are zinc-dependent endopeptidases that degrade components of the extracellular matrix and play essential roles in tissue remodeling in physiological and pathological processes such as morphogenesis, differentiation, angiogenesis, tissue remodeling, and tumor invasion (1, 2). The association of MMPs with cancer cell invasion and metastasis has suggested that these proteinases represent attractive targets for the development of novel anti-tumor therapies.Recently, it has been suggested that the biological functions of various cell surface proteins are proteolytically modulated by several MMPs (1, 3, 4), including MT-MMPs, gelatinase A (MMP-2), gelatinase B (MMP-9), stromelysin (MMP-3), and matrilysin (MMP-7). These metalloproteinases are thought to regulate cellular functions by activating, inactivating, or releasing membrane proteins. Such regulation of cell surface molecules as well as MMP-catalyzed degradation of the extracellular matrix is important for tumor invasion and metastasis.Matrilysin is the smallest member of the MMP family, which lacks the C-terminal hemopexin-like domain. In cancer tissues, various MMPs are overexpressed both in stromal and tumor cells. In contrast, matrilysin has been detected specifically in tumor cells but not in stromal cells (5, 6). Among many MMPs, matrilysin appears to be one of the most important MMPs in human colon cancers because it is almost always overexpressed in colon cancers. Expression of matrilysin is also correlated well with malignancy and metastasis of cancers, especially in liver me...

Matrilysin (MMP-7) is thought to contribute to invasive growth and metastasis of colon carcinoma and many other human cancers. The present study demonstrates that treatment of human colon carcinoma cells with active matrilysin induces cell aggregation in vitro and promotes liver metastasis in nude mice. When two kinds of colon carcinoma cell lines were incubated with active matrilysin, this enzyme efficiently bound to the cell surface and induced loose cell aggregation, which led to E-cadherinmediated tight cell aggregation. Synthetic MMP inhibitors inhibited both the membrane binding of matrilysin and matrilysin-induced cell aggregation, while TIMP-2 inhibited only the cell aggregation. Two other active MMPs, stromelysin and gelatinase A, neither bound to cell membrane nor induced cell aggregation. Tumor cells in loose cell aggregates could reaggregate even after they were freed from matrilysin and dispersed. When injected into the spleen of nude mice, the tumor cells in the stable aggregates produced much larger metastatic nodules in the livers than control cells and those in the loose aggregates. These results suggest that matrilysin may enhance metastatic potential of tumor cells by processing a cell surface protein(s) and thereby inducing loose and then tight aggregation of tumor cells.

It was recently found that overexpression of the trypsin gene in tumor cells stimulates their growth in culture and in nude mice. In the present study, expression of trypsin in various human cancer cell lines and tissues was studied by gelatin zymography and immunoblotting before and after enterokinase treatment and by immunohistochemistry. The analyses showed that many stomach, colon, and breast cancer cell lines secreted trypsinogens-1 and/or -2, as well as an unidentified serine proteinase of about 70 kDa, into culture medium. Lung cancer cell lines secreted 18- and 19-kDa unidentified trypsin-like proteins. Stomach cancer cell lines frequently secreted active trypsin, suggesting that they produced an endogenous activator of trypsinogen, most likely enterokinase. Active trypsin formed a complex with a soluble form of Alzheimer amyloid precursor protein (sAPP), a Kunitz-type trypsin inhibitor, which was secreted by all cell lines tested. This indicated that sAPP is a primary inhibitor of secreted trypsin. Immunohistochemical analysis showed that trypsin(ogen) was frequently expressed at high levels in stomach and colon cancers, but scarcely in breast cancers. In the stomach cancers, the trypsin immunoreactivity was higher in the malignant, non-cohesive type than in the cohesive type. These results support the hypothesis that tumor-derived trypsin is involved in the malignant growth of tumor cells, especially stomach cancer cells.