Unsafe to drink? Perspectives on water quality among NGOs, commercial firms and consumers

Ensuring a reliable supply of potable water for people affected by conflicts or disasters is crucial for daily living and to prevent disease. For humanitarian NGOs and government water service providers, potability is usually defined as water free from chemical, physical and bacterial contaminants. Water consumers, however, typically define water quality from a less technical view. For the end user, the two main questions about potability are: Does the water taste good? And do my neighbours drink the same water as I do? As part of an ongoing NGO response to facilitating access to safe water by urban refugees and low income communities in Jordan and Palestine, water market assessment surveys were conducted in 2013. A key lesson emerging from both studies was the need for active engagement with local water service providers to help promote a shared understanding of the importance of safe drinking water

Dry season water strategies in Myanmar after cyclone Nargis

For many residents of the Ayeyarwady Delta of Myanmar, rainwater collection from village ponds and roof tops serves as the primary source of potable water throughout the year. In May 2008, Cyclone Nargis struck the Delta region, damaging many of these ponds by breaching their embankments or filling them with debris and saline water. Despite the efforts of the international aid community and local government to repair and rehabilitate these traditional water sources, concerns remain about a potential water crisis affecting thousands of Ayeyarwady Delta residents during the dry season from November to April. This paper examines the different water rehabilitation and supply strategies adopted by relief agencies and communities during the second half of 2008 to mitigate possible water shortages in 2009

Collagen XVI overexpression leads to an increase of ILK/kindlin-1 interaction.

<p>(<b>A</b>) Proximity ligation assay for the analysis of ILK/kindlin-1 interaction in COLXVI and mock control cells (scale bar equals 50 µm). COLXVI cell clones exhibit an increased interaction of kindlin-1 and ILK at focal adhesions compared to mock control cells (<b>A+B</b>). After inhibition of focal adhesion formation with soluble RGD peptides (c  =  100 µg/mL) ILK/kindlin-1 interaction was significantly reduced (p<0.001, n = 100) (A+<b>C</b>). (<b>D</b>) Quantitative PCR of <i>MMP9</i> gene expression in COLXVI cell clones and mocks after 24 h incubation with soluble RGD peptides. Inhibition of focal adhesions via soluble RGD-peptides resulted in a dose-dependent decrease in <i>MMP9</i> gene expression (n = 3). (<b>E</b>) Co-Immunoprecipitation of ILK and kindlin-1 of protein extracts isolated from COLXVI clones and mocks. COLXVI cell clones exhibit an increased ILK/kindlin-1 interaction depending on collagen XVI dose. Mock control cells showed least ILK/kindlin-1 interaction.</p

Collagen XVI overexpression leads to increased invasion of OSCC cells.

<p>(<b>A</b>) Quantitative PCR of <i>MMP9</i> gene expression of COLXVI and mock control cells after AP-1 inhibition with Tanshinone IIA (TIIA; c  =  100 ng/mL). The expression of <i>MMP9</i> decreased in the COLXVI cell clones after AP-1 inhibition with Tanshinone IIA. (n = 3) (<b>B</b>) 3D micromass pellets of COLXVI cells compared to mock control cells 24 h after placement. COLXVI cells (high and low expressing) show a significantly wider invasion zone (orange line) compared to mock control cells (p<0.01; n = 10). (<b>C</b>) 3D micromass pellets of mock control cells after 24 h of incubation with 500 ng/mL recombinant collagen XVI. Incubation with recombinant collagen XVI resulted in a significantly increased spreading of the invasion zone (orange line) compared to the control (p<0.001; n = 10).</p

The AP-1 binding site at –98bp is important for collagen XVI dependent MMP9 induction.

<p>(<b>A</b>) Schematic presentation of the three different MMP9 promoter fragments. MMP9a, MMP9b, and MMP9c contain 0, 1, and 2 AP-1 binding sites, respectively. (<b>B</b>) Comparison of MMP9 promoter activities of MMP9a, MMP9b, and MMP9c in COLXVI and control cells, respectively. The shortest MMP9 promoter fragment (MMP9a) exhibits the lowest activation. In general, COLXVI clones reveal a higher activation of the <i>MMP9</i> promoter than the mock control cells. The luciferase reporter shows increased activation of the <i>MMP9</i> promoter in clone high compared to clone low (n = 3). (<b>C</b>) Schematic presentation of the MMP9b promoter and the MMP9b deletion promoter, respectively. The MMP9b deletion promoter does not contain the AP-1 binding site 98 bp upstream from the start codon. (<b>D</b>) Promoter activity of the MMP9b promoter after deletion of the AP-1 binding site. After deletion of the AP-1 binding site the MMP9b promoter activity decreases significantly (n = 3).</p

Collagen XVI overexpression leads to c-Fos – dyskerin interaction and increased nuclear JunB localization.

<p>(<b>A</b>) Immunoblot analyses of JunB and c-Fos nuclear extracts from COLXVI cell clones and mock control cells. COLXVI cell clones show a higher amount of JunB compared to mock control cells. COLXVI cell clones do not differ from mock control cells in c-Fos expression. (<b>B</b>) Immunofluorescence staining of c-Fos (green) in COLXVI cell clones and mock control cells (scale bar equals 50 µm). COLXVI cell clones do not differ from mock control cells in their c-Fos expression. Quantification was performed measuring the fluorescent intensity of 100 COLXVI cells and mock controls, each. (<b>C</b>) Silver stained gel of protein lysates from COLXVI cell clones and mock control cells, respectively, after immune precipitation of c-Fos. In COLXVI cell clones a band with a size of 58 kDa was differentially expressed. Mass spectrometry revealed it as dyskerin. (<b>D</b>) Co-immunoprecipitation of c-Fos and dyskerin of protein extracts isolated from COLXVI clones and mocks. COLXVI cell clones exhibit an increased interaction of c-Fos and dyskerin compared to mock control cells. (E) Dyskerin immunoblot of nuclear extracts from COLXVI cell clones and mock control cells. COLXVI cell clones exhibit a higher protein amount of dyskerin than mock control cells. (<b>F</b>) Immunofluorescence staining of dyskerin (red) in COLXVI cell clones and mock control cells (scale bar equals 50 µm). COLXVI cell clones showed strong dyskerin staining compared to mock control cells (<b>G</b>). Immunofluorescence staining of JunB (red) in COLXVI clones and mock control cells (scale bar equals 50 µm). COLXVI cell clones exhibit stronger JunB staining compared to mock control cells. Quantification of signal intensity demonstrates significantly increased nuclear JunB expression in COLXVI cells compared to mock controls.</p

COLXVI overexpression induces MMP9 expression.

<p>(<b>A</b>) Immunoblot analysis of collagen XVI secretion in supernatants of COLXVI cell clones (clones 1-4) and mock control cells (mock 1-2). Only COLXVI cell clones secret the full-length form of COLXVI (213 kDa; black arrow). Clones 3 and 4 exhibit higher COLXVI secretion than clones 1 and 2. COLXVI cell clones also secrete collagen XVI fragments. A Coomassie Blue membrane staining was used as loading control. (<b>B</b>) Quantitative PCR of <i>MMP9</i> expression in COLXVI cell clones and mocks after 24 h incubation with/without recombinant collagen XVI. COLXVI cell clones (1-4) show a significant expression of <i>MMP9</i> that is further enhanced by the addition of recombinant collagen XVI (n = 3). (<b>C</b>) Gelatin zymography of COLXVI cell supernatant and mock controls. The COLXVI cell clones (1-4) show a clear gelatinolytic activity at 92 kDa (pro form). In contrast, the mock control cells (1-2) show very weak MMP9 bands. (<b>D</b>) Immunoblot of total ILK and phosphorylated ILK (P ILK) isolated from membrane fractions of COLXVI cell clones and mock control cells. ILK is activated in COLXVI cell clones whereas in mock control cells P-ILK is lacking. (<b>E</b>) Quantitative PCR of <i>MMP9</i> expression after ILK inhibition with Cpd 22 (ILKi). The expression of <i>MMP9</i> decreased after ILK inhibition in the COLXVI cell clones. (n = 3). (<b>F</b>) Gelatin zymography of the supernatant of the COLXVI cell clone 3 after ILK inhibition with Cpd 22 (ILKi; c  =  300nM). After ILK inhibition the COLXVI cell clone depicts decreased MMP9 secretion. (<b>G</b>) Promoter activity of the COLXVI cell clone 3 after ILK inhibition with Cpd 22 (ILKi; c  =  300 nM). ILK inhibition results in a significant decrease of the MMP9b promoter activity. (p<0.001; n = 3). (<b>H</b>) Immunoblot of total Akt/PKB and phosphorylated Akt/PKB (P-Akt/PKB) in cell lysates of COLXVI cell clones (clones 1-4) and mock control cells (1-2). Akt/PKB activation is increased in COLXVI cell clones compared to mock controls.</p

Oral acantholytic squamous cell carcinoma shares clinical and histological features with angiosarcoma-3

, ×150).<p><b>Copyright information:</b></p><p>Taken from "Oral acantholytic squamous cell carcinoma shares clinical and histological features with angiosarcoma"</p><p>http://www.head-face-med.com/content/4/1/17</p><p>Head & Face Medicine 2008;4():17-17.</p><p>Published online 31 Jul 2008</p><p>PMCID:PMC2515303.</p><p></p

Oral acantholytic squamous cell carcinoma shares clinical and histological features with angiosarcoma-6

<p><b>Copyright information:</b></p><p>Taken from "Oral acantholytic squamous cell carcinoma shares clinical and histological features with angiosarcoma"</p><p>http://www.head-face-med.com/content/4/1/17</p><p>Head & Face Medicine 2008;4():17-17.</p><p>Published online 31 Jul 2008</p><p>PMCID:PMC2515303.</p><p></p

Oral angiosarcoma: immunohistochemical demonstration of factor VIII-related antigen in a subset of the tumour cells lining the vascular spaces (×150)

<p><b>Copyright information:</b></p><p>Taken from "Oral acantholytic squamous cell carcinoma shares clinical and histological features with angiosarcoma"</p><p>http://www.head-face-med.com/content/4/1/17</p><p>Head & Face Medicine 2008;4():17-17.</p><p>Published online 31 Jul 2008</p><p>PMCID:PMC2515303.</p><p></p