Analysis on Water Environment Capacity of the Poyang Lake

AbstractA proper model was selected in this paper for analyzing the capacities of water environment of Poyang Lake for accommodating the several main pollutants quantitatively on the basis of the existing data. The results show that the maximum annual capacities of COD, TP and TN are 768288.5t, 7161.2t and 143224t respectively by taking the second-class national water standard as reference and they are 1576982.5t, 14322.4t and 286448t respectively by taking the third-class national water standard as reference. The paper further analyzed the system adjusting capacity of water environment of Poyang Lake with the following results: The flood adjusting amount for the five upper rivers of Poyang Lake at their maximum inflow reaches 74 to 246×108m3. The flood-adjustment rate is about 16 to 60 percent with its annual average adjustment rate of 34%. The occurrence of serious flooding disaster of Poyang Lake is 16%. The carrying capacity of the flooding-proof system of the lake region is relatively low. About 29.9 to 53×108 m3 water in the dry season are needed for maintaining ecological functions of the lake. Water and soil erosion, and land desertification in the lake region are not under control currently. Annual ecological and environmental cost reaches 19.85×108 RMB occupying 10.56 percent of the total GDP of the Poyang Lake region. In a word, the economic, social and environmental development coordinating level of the Poyang Lake region is low

Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain

Phagocyte recognition and clearance of bacteria play essential roles in the host response to infection. In an on-going forward genetic screen, we identify the Drosophila melanogaster scavenger receptor Croquemort as a receptor for Staphylococcus aureus, implicating for the first time the CD36 family as phagocytic receptors for bacteria. In transfection assays, the mammalian Croquemort paralogue CD36 confers binding and internalization of Gram-positive and, to a lesser extent, Gram-negative bacteria. By mutational analysis, we show that internalization of S. aureus and its component lipoteichoic acid requires the COOH-terminal cytoplasmic portion of CD36, specifically Y463 and C464, which activates Toll-like receptor (TLR) 2/6 signaling. Macrophages lacking CD36 demonstrate reduced internalization of S. aureus and its component lipoteichoic acid, accompanied by a marked defect in tumor necrosis factor-α and IL-12 production. As a result, Cd36−/− mice fail to efficiently clear S. aureus in vivo resulting in profound bacteraemia. Thus, response to S. aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain, which initiates TLR2/6 signaling

A MCP1 fusokine with CCR2-specific tumoricidal activity

<p>Abstract</p> <p>Background</p> <p>The CCL2 chemokine is involved in promoting cancer angiogenesis, proliferation and metastasis by malignancies that express CCR2 receptor. Thus the CCL2/CCR2 axis is an attractive molecular target for anticancer drug development.</p> <p>Methods</p> <p>We have generated a novel fusion protein using GMCSF and an N-terminal truncated version of MCP1/CCL2 (6-76) [hereafter GMME1] and investigated its utility as a CCR2-specific tumoricidal agent.</p> <p>Results</p> <p>We found that distinct to full length CCL2 or its N-truncated derivative (CCL2 5-76), GMME1 bound to CCR2 on mouse lymphoma EG7, human multiple myeloma cell line U266, or murine and human medulloblastoma cell lines, and led to their death by apoptosis. We demonstrated that GMME1 specifically blocked CCR2-associated STAT3 phosphorylation and up-regulated pro-apoptotic BAX. Furthermore, GMME1 significantly inhibited EG7 tumor growth in C57BL/6 mice, and induced apoptosis of primary myeloma cells from patients.</p> <p>Conclusion</p> <p>Our data demonstrate that GMME1 is a fusokine with a potent, CCR2 receptor-mediated pro-apoptotic effect on tumor cells and could be exploited as a novel biological therapy for CCR2⁺malignancies including lymphoid and central nervous system malignancies.</p

Maltose-binding protein fusion allows for high level bacterial expression and purification of bioactive mammalian cytokine derivatives.

Fusokines are chimeric proteins generated by the physical coupling of cytokines in a single polypeptide, resulting in proteins with highly pleiotropic activity and the potential to treat cancer and autoimmune ailments. For instance, the fusokine GIFT15 (GM-CSF and Interleukin 15 Fusion Transgene) has been shown to be a powerful immunosuppressive protein able to convert naïve B cells into IL-10-producing B cells. To date, the mammalian cell systems used for the expression of GIFT15 allow for secretion of the protein in the culturing media, an inefficient system for producing GMP-compliant fusokines. In this study we report the bacterial expression of bioactive recombinant GIFT15 (rGIFT15). Indeed, there is a constant demand to improve the expression systems for therapeutic proteins. Expression of a maltose-binding protein (MBP) fusion protein efficiently allowed the accumulation of soluble protein in the intracellular milieu. Optimizing the bacterial culture significantly increased the yield of recombinant protein. The biological activity of rGIFT15 was comparable to that of fusokine derived from a mammalian source. This approach led to the production of soluble, endotoxin-free functional protein, averaging 5 mg of rGIFT15 per liter of culture. This process is amenable to scale up for the development of Food and Drug Administration (FDA)-compliant immune-modulatory rGIFT15

Combination of serum lipids and cancer antigens as a novel marker for colon cancer diagnosis

Abstract Background Colon cancer is a malignancy of the large intestine with high mortality and economic burden. Recent studies reveal a new relationship between blood lipids and the risk of cancer. The presents study aims to investigate the combination of serum lipids with cancer antigens as a novel diagnostic marker for colon cancer. Methods Two hundred of colon cancer patients or healthy subjects were recruited. Serum lipids and cancer antigens such as total cholesterol (TC), high-density lipoprotein (HDL), carcinoembryonic antigen (CEA) and carbohydrate antigen 19–9 (CA19–9) were measured. Results There were significantly lower level of serum TC or HDL, and significantly higher level of serum CEA or CA19–9 in patients than in healthy subjects. Serum TC or HDL in patients with advanced colon cancer was significantly lower than the ones with early stage disease. The level of serum TC or HDL in patients after surgical removal of colon cancer was significantly higher compared to the ones before surgery, but serum CEA or CA19–9 after surgery was significantly reduced in comparison with the ones before surgery. Combined TC, HDL, CEA and CA19–9 as a diagnostic marker for colon cancer had the highest positive predictive rate in comparison with individual, two or three of the parameters. Conclusions The combination of serum TC, HDL, CEA and CA19–9 can be used as an effective marker for colon cancer, and offers a novel strategy for clinical diagnosis and monitoring the disease

Purification of rGIFT15.

<p>Purification of His-MBP-GIFT15 on Nickel-Sepharose (A) and on DEAE-Sepharose (B) after cleavage with TEV protease. Black traces are the absorbance readings recorded at 280 nm and red traces represent the elution gradient. (C) SDS-PAGE following His-MBP-GIFT15 purification. (1) cell-free extract before induction with IPTG, (2) cell-free extract after induction with IPTG, (3) His-MBP-GIFT15 after Ni-Sepharose, (4) rGIFT15 after TEV protease treatment and isolation on DEAE-Sepharose, (5) molecular weight markers.</p

Schematic representation of the plasmid vector constructs tested for expression of mouse GIFT15 in <i>E. coli</i>.

<p>1. pET20b: expression of GIFT15 without any tag, GM-CSF domain (lacking the signal peptide, green box) and IL-15 domain (blue box). The linker between the two domains is formed from the signal peptide and propeptide of IL-15 (grey box). 2. pET16b: expression of GIFT15 with an additional His-tag (6x-His) at the N-terminus of the fusokine. 3. pET32b: expression of GIFT15 downstream of thioredoxin (TRX, red box) followed by a His-tag. 4. pET42b: expression of GIFT15 in fusion with glutathione S-transferase (GST, yellow box). 5. pMALc4x: expression of GIFT15 in fusion with the maltose-binding protein (MBP, white box). 6. pHisMBP: expression of GIFT15 with the addition of a His-tag at the N-terminus of the MBP domain and replacement of the Factor Xa protease recognition site with that of the TEV protease.</p

Western blot analysis of purified rGIFT15.

<p>Immunodetection was conducted with anti-mouse IL-15 antibody.</p