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Chlorine is a harmful constituent in coal, contributing to severe high temperature corrosion on the super-heater and re-heater tubes in utility boiler firing high-chlorine coal (more than 0.3 wt.%). Characteristics of the corrosion contain not only the formed products on the metal surface, but also intergranular attack inner the alloy, resulting in great potential safety hazard and economic loss. The prevailing Cl-related mechanisms of high temperature corrosion involve active oxidation and fluxing, which mean both corrosive elements in the flue gas and deposits on the boiler metal surface can accelerate the corrosion. Cl2 as a catalyst in active oxidation can be released by sulfuration of alkali metal chlorides or reactivity by alkali metal chlorides with chromium/chromium oxide and iron/iron oxide or oxidation of HCl. However, the formation of low-melting eutectics (such as NaCl-Na2CrO4) in mechanism of fluxing can be an induction of severe corrosion because the rate of molten corrosion is much higher than chemical corrosion. Lab-scale experiments simulating the flue gas species, temperature gradient from hot flue gas (950 °C) to cold metal (610 °C), and deposit (four various Cl-containing coal ash) on the specimens were conducted in a tube furnace to investigate the corrosion of three common boiler steels (12Cr1MoVG, T91, TP347H). Furthermore, with the aid of the scanning electronic microscope associated with energy dispersive spectrometer (SEM-EDX) and X-ray diffraction instrument (XRD), the appearance and microstructure, the element contents, and composition of corrosion products on the specimens after corrosion have been analyzed. For high-chlorine coal, there existed white crystal on the surface of specimens (T91, TP347H) after corrosion test, and the XRD result showed NaCl, which can be explained by evaporation-condensation mechanism. However, no white crystal was detected for 12Cr1MoVG and it can be inferred that thick corrosion product layer with high thermal resistance was formed and 12Cr1MoVG suffered severe degradation. Through comparisons of alloy elements corroded in various oxidizers (Cl2, O2, and S), it can be seen that as the metal temperature increases, the negative value of Gibbs free energy for alloy elements corroded in Cl2 becomes higher, but the value is less corroded in O2 or S. Thus, alloy elements tend to be easier combined with Cl2, and Cl-induced corrosion is aggravated with the temperature increases. Similar results can be obtained by increased equilibrium vapor pressures of metal chlorides, evaporating easily and diffusing towards further to be oxidation. In comparison with high-chlorine coal, the corrosivity of low-chlorine coals on specimens were weak, especially for TP347H characterized with higher contents of Cr and Ni. Furthermore, the higher the ratio of Cl/2S or Cl/Na in the coal ash is, the more severe corrosion the specimens suffer.

Based on the demand of the admission control of softswitch-based clustered media server, this paper proposed a new dynamic quota-based admission control algorithm that has a sub-negotiation process. The strongpoint of quota-based algorithm had been inherited in the algorithm and at the same time some new ideas had also been introduced into it. Simulations of the algorithm had been conducted on the Petri net model and the results show that this algorithm has excellent performance. In order to find the optimal resource quota setting in real time, the paper proposed two approximation analysis methods. It can be seen from analysis results that these two methods can be used to get sub-optimal quota values quickly and effectively. These two approximation analysis methods will play important roles in implementation of the algorithm in system.

Based on the system feature of softswitch-based heterogeneous clustered media server, this paper proposed a limited resource vector load-balancing algorithm. The purpose of the algorithm was to balance the load of clusters by utilizing all system resources effectively and to avoid violent shaking of the system performance. A lot of simulations on the Petri net model of load balance system are conducted and the algorithm is compared with some traditional algorithms on balancing ability for heterogeneity, system throughput, request response time and performance stability. The results of simulations show that the algorithm achieves system higher performance and it has excellent ability to deal with the heterogeneity of clustered media server.

The present studies examined the effects of acidic fibroblast growth factor (aFGF) on 5-ene-3 beta-hydroxysteroid dehydrogenase-isomerase (3 beta-HSD) and 5 alpha-reductase activities and [125I]human chorionic gonadotrophin ([125I]hCG) binding in cultured immature rat Leydig cells. Increasing concentrations of aFGF (0.1-20 ng/ml) progressively decreased basal 3 beta-HSD activity from 0.474 +/- 0.0335 to 0.093 +/- 0.0004 nmol progesterone/30 min/10(5) cells. This inhibition by aFGF (10 ng/ml) was partially reversed by 1 micrograms/ml insulin or 100 ng/ml insulin-like growth factor-I. Increasing aFGF concentrations (0.1-10 ng/ml) also inhibited hCG-stimulated 5 alpha-reductase activity in a dose-dependent manner, but had only a modest effect on basal enzyme activity. Increasing aFGF (0.1-200 ng/ml) also progressively inhibited [125I]hCG binding in cultured immature Leydig cells. These studies demonstrate a similarity in the inhibitive effects of aFGF with bFGF effects on 3 beta-HSD and 5 alpha-reductase activities and [125I]hCG binding to LH receptors, although, generally, higher aFGF concentrations were required to elicit maximal inhibitive effects. However, a FGF differed from the actions of bFGF on 3 beta-HSD activity and LH receptor levels in that a secondary increase with higher growth factor concentrations was not observed.

Previous studies have shown that basic fibroblast growth factor (bFGF) can modulate basal and luteinizing hormone/human chorionic gonadotropin (LH/hCG)-stimulated Leydig cell functions. It has not been ascertained whether these actions are due to direct or indirect effects on Leydig cells. To resolve this question, a multi-step procedure was used to isolate highly-purified Leydig cells from immature rats. 125I-bFGF binding studies were performed on cultured cells. Scatchard analysis of the data indicated a single binding site with an apparent Kd of 82 pM and a binding capacity of approximately 2800 sites per cell. Both bFGF and acidic FGF similarly were effective in displacing 125I-bFGF, suggesting that the receptor binds both bFGF and aFGF. However, neither hCG, follicle-stimulating hormone (FSH), insulin, insulin-like growth factor-1 (IGF-1), prolactin, platelet-derived growth factor (PDGF) or epidermal growth factor (EGF) were effective competitors. When binding studies were conducted on cultured testicular interstitial cellular fractions that are normally discarded during Leydig cell purification, bFGF receptors were identified in these fractions. These results demonstrate that bFGF can have direct effects on Leydig cells through specific receptors; however, because other interstitial cell type(s) also have bFGF receptors, they stress the importance of using highly purified cells when evaluating bFGF actions on Leydig cells.

We reported previously that coculture of immature rat Sertoli cells with Leydig cells or the addition of a concentrate from Sertoli cell-conditioned medium (SCCM) stimulated Leydig cell [(3)H]-thymidine incorporation, increased cell number, and altered Leydig cell morphology (Wu and Murono, 1994). In the present studies, the effect of various extracellular matrix proteins on immature Leydig cell binding, proliferation and response to SCCM concentrate was investigated. Pretreatment of culture wells with 50 μg/mL collagen I or 10 μg/mL laminin inhibited Leydig cell binding to culture wells about 95 and 89%, respectively; however, 5 μg/mL fibronectin did not change the level of attachment. The binding of Leydig cells to fibronectin was reduced by antifibronectin or-β1 integrin antibodies (66 and 91%, respectively). Treatment of culture wells with five or 50 μg/mL fibronectin alone increased [(3)H]thymidine incorporation about twofold. When Leydig cells were cultured in wells precoated with increasing concentrations of fibronectin and then treated with SCCM concentrate for 2 d, [(3)H]-thymidine incorporation increased progressively with the concentration of fibronectin, beyond the levels observed with SCCM concentrate alone. This response was associated with increases in both Leydig cell number and labeling indices. When Leydig cells were cultured on fibronectin, their numbers increased by 3.7-and 5.1-fold following treatment with SCCM concentrates or coculture for 6 d, respectively; whereas, they increased 2.6- and 3.9-fold, respectively, when cultured on plastic. Labeling indices of Leydig cells cultured on plastic for 2 d and treated with SCCM or cocultured were 6.9 and 11.9%, respectively, while labeling indices of Leydig cells grown on fibronectin increased further to 17.6 and 26.3%, respectively. α5β1 integrin complexes and α5 integrin mRNA were expressed in Leydig cells, suggesting that binding to fibronectin may be mediated by α5β1 integrins, a fibronectin receptor. These results suggest that Leydig cell proliferation stimulated by a Sertoli cell-secreted mitogenic factor(s) is enhanced by Leydig cell binding fibronectin, and that this binding may be mediated by α5β1 integrins.

Previous studies have shown that disruption or damage to the seminiferous tubules by radiation, antiandrogen, vitamin A deficiency or experimental cryptorchidism causes Leydig cell hypertrophy and hyperplasia, suggesting that Sertoli cells secrete a mitogenic factor(s) that stimulates Leydig cell proliferation. To study the possible paracrine regulation of Leydig cell proliferation by Sertoli cells, highly purified Leydig cells and Sertoli cells were co-cultured in a two-chambered co-culture system. Our results revealed that co-culture of immature rat Sertoli cells with Leydig cells stimulated Leydig cell DNA synthesis by 19-fold, increased cell number by about 3.9-fold and increased the labeling index from 0.5% to 15.8%. In addition to these changes, co-culture reduced Leydig cell testosterone formation and luteinizing hormone (LH) receptor levels, and dramatically altered the morphology of Leydig cells. The addition of concentrates from Sertoli cell conditioned medium (SCCM) mimicked these biological effects. The Leydig cell mitogenic activity in SCCM was trypsin sensitive and inactivated by boiling for 2 h, suggesting that it is a protein. However, it was resistant to acid and dithiothreitol. The molecular weight of this putative factor(s) is above 10 kDa. The responsiveness of Leydig cells to this mitogenic protein(s) decreased with age, whereas the secretion of this protein(s) by Sertoli cells in culture did not change with age. The addition of 10 ng/ml of follicle stimulating hormone (FSH) dramatically decreased the mitogenic activity in SCCM, indicating that the secretion of this mitogenic factor(s) is inhibited by FSH. This paracrine factor(s) may be as yet an unidentified testicular growth factor(s) because it differs in molecular weight, stability and other characteristics from all previously reported Sertoli cell-produced or expressed growth factors.

The present studies examined how 125I-labeled basic fibroblast growth factor (bFGF) bound to high affinity receptors and with lower affinity to heparan sulfate proteoglycans (HSPG) of cultured immature rat Leydig cells was processed. Following incubation for 2 h at 4°C with 125I-bFGF, cells were washed to remove unbound radioactivity. Fresh medium was added, and cells were incubated at 4° and/or 37°C. At time zero and at specific intervals over the next 6 h, the incubation medium was saved and cells washed to quantitate 125I-bFGF released into the medium, associated with HSPG of the cell surface or extracellular matrix (radioactivity released by washing cells with 2 M NaCl, pH 7.4), associated with cell surface receptors (radioactivity released by washing cells with 2 M NaCl, pH 4.0) or internalized (radioactivity resistant to high salt and acid washes, and solubilized with 0.5 M NaOH). Radioactivity released into the initial medium and the pooled washes was further divided into a trichloroacetic acid (TCA)-precipitated form (radioactivity precipitated by 10% TCA) and a TCA-soluble form (radioactivity remaining in the TCA supernatant). 125I-bFGF associated with both HSPG and surface receptors declined progressively during the first 4 h of incubation before stabilizing when cells were transferred to 37°C. These declines were associated with a corresponding increase in intracellular 125I-bFGF. These changes were blocked by maintaining cells at 4°C. The majority of internalized 125I-bFGF appeared to originate from the HSPG-bound fraction as there was a greater decline in HSPG-associated radioactivity and most of the increase in internalized radioactivity could be blocked by the inclusion of 10 μg/ml heparin (which mainly blocks 125I-bFGF binding to HSPG but not to high affinity receptors) during the initial incubation with 125I-bFGF for 2 h at 4°C. Furthermore, HSPG-mediated internalization appeared to have two components: the major fraction was blocked by the inclusion of 10 μg/ml heparin, while a heparin-resistant fraction, appeared to be closely linked both quantitatively and temporarily to receptor-mediated internalization. A minor fraction of internalized 125I-bFGF was metabolized in lysosomes, as the inclusion of 50 μM chloroquine during the 6 h incubation at 37°C inhibited most of the increase in TCA-soluble radioactivity appearing in the incubation medium. Exposure of cultured cells to increasing concentrations of bFGF (0.1–10 ng/ml) for ~ 16 h decreased bFGF receptor levels in a dose-dependent manner, suggesting that internalization, in part, is associated with down-regulation of bFGF receptors.

Previous studies have shown that basic fibroblast growth (bFGF) has a biphasic effect on 125I-hCG binding to LH receptors in cultured Leydig cells from immature rats. Low concentrations of bFGF (0.1-1.0 ng/ml) progressively decreased binding, while higher concentrations (10-100 ng/ml) progressively increased binding above nadir levels. In the present studies, treatment of cultured immature Leydig cells with heparinase I and/or heparinase III, which enzymatically remove heparan sulfate proteoglycans, had no effect on basal binding of 125I-hCG to LH receptors or the decrease in binding due to treatment with low bFGF concentrations; however, this treatment dramatically reduced the secondary increase in binding following the addition of higher bFGF concentrations. These results strongly support the idea that the secondary increase in 125I-hCG binding to LH receptors elicited by treatment with higher bFGF concentrations is mediated by bFGF binding to heparan sulfate proteoglycans associated with the plasma membrane and/or extracellular matrix.

The present studies examined the effects of basic fibroblast growth factor (bFGF or FGF-2) on 125I-human chorionic gonadotropin (hCG) binding to cultured immature rat Leydig cells. We found that low concentrations of bFGF (0.1-1.0 ng/ml) inhibited 125I-hCG binding to cultured immature Leydig cells in a dose- and time-dependent manner; however, this inhibition was reversed partially at higher bFGF concentrations (10-200 ng/ml). The decline in 125I-hCG binding by bFGF was due to a reduction in the number of binding sites per cell and not to a change in receptor affinity for the ligand. The inclusion of 10 micrograms/ml heparin (a concentration that is reported to block bFGF binding to heparan sulfate proteoglycans) with increasing bFGF concentrations had no effect on the inhibition of 125I-hCG binding by low bFGF concentrations, but completely blocked the secondary increase in binding by higher bFGF concentrations. In addition, neither varying heparin concentrations (0.1-25 micrograms/ml) nor insulin or insulin-like growth factor-I had any effect on the inhibition of 125I-hCG binding by 1 ng/ml bFGF. These studies suggest that receptor-mediated actions of bFGF (inhibition of hCG binding by low bFGF concentrations) on cultured immature Leydig cells are unaffected by heparin; however, the secondary increase in 125I-hCG binding observed with higher bFGF concentrations (mediated by bFGF binding to heparan sulfate proteoglycans) is blocked by heparin.