26 research outputs found

    North South Divide of the Poor in the Staffordshire Potteries 1871-1901

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    Under the 1834 New Poor Law Act, three parishes, Stoke, Burslem, and Wolstanton, became two unions: Stoke Poor Law Union, consisting of the towns of Hanley, Stoke, Fenton and Longton, and Wolstanton and Burslem Union, consisting of the parishes of Wolstanton and Burslem. Wolstanton and Burslem Union workhouse was situated to the north of the city at Chell, and Stoke to the south, bordering the town of Newcastle-under-Lyme. Both workhouses lay within the industrial area known as the Staffordshire Potteries. However, at its broadest extent the aim of this thesis is to establish if two Poor Law Unions covering one industrial area (the Staffordshire Potteries) with similar socio-economic characteristics treated their poor identically or differently and if so, what influences, either internal or external can be attributed as the cause. This wide-ranging study covers various aspects of the experiential dynamics of welfare – vagrancy, the treatment of children and the elderly, religion, and health – none of which have received any detailed coverage in secondary literature relative to the North Midlands. With the aid of Local Government Board (LGB) correspondence and press reports, this thesis endeavours to investigate the authority of the LGB and their Circulars both locally and regionally. It asks how far, and with what variations two contiguous workhouses only six miles apart governed themselves within the framework set by the LGB and its directives. The study focuses on the policy adopted by the LGB considering the Crusade against outdoor relief, and will attempt to determine if this was stringently applied or otherwise. For a period from the inception of the LGB in 1871-1901 when workhouses became almost a refuge for the elderly and infirm – thinly covered by the burgeoning historiography of the New Poor Law, this case study will afford a detailed insight into the nature of pauper life-cycle experiences on relief whilst also considering the factors driving (and differentiating) the complexities of official practice

    CXCR7 signaling is not responsible for the apoptotic-resistace shown by clathrin-depleted DKO-R cells.

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    <p>(A) Quantitative RT-PCR for CXCR7 in both cell lines. (B) Caspase activity and percentage of apoptosis of clathrin-expressing and clathrin-repressed DKO-R cells in the presence or absence of 0.5 µM CCX771 and inactive analog CCX704. Cells were grown in standard DT40 medium with 1% chicken serum. Values are means of four determinations +/− standard deviation.</p

    DKO-S cells show a higher apoptotic response to clathrin-depletion than DKO-R cells.

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    <p>(A) The proportion of apoptotic cells and (B) caspase activity were measured as described in materials and methods for DKO-S and DKO-R cells grown with or without 0.1 µM doxycycline (dox) and in media supplemented with increasing concentrations of chicken serum are as indicated. Values are means of three measurements +/− standard deviation. Statistically significant differences, with p values, are indicated.</p

    Microarray analysis of the gene expression profiles of DKO-s and DKO-R cells.

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    <p>(A) differentially expressed genes ordered in descending significance according to the P value UK: unknown. (B) functional clusters of genes of processes implicated in cell fate. (C) depiction of the CXCR4 signalling pathway.</p

    RT-PCR for CXCR4, SDF-1 and CXCR7 in DKO-S and DKO-R cells.

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    <p>(A) standard RT-PCR as described in materials and methods followed by agarose gel migration. Controls (RNA) for genomic DNA contamination in which the RT-PCR reaction was conducted without prior treatment with reverse transcriptase are shown. (B) real time PCR from cDNA obtained from both cell-lines, results are expressed as ΔCp normalising the levels of expression to Cyclophilin A. (C) Caspase activity and percentage of apoptosis of clathrin-expressing and clathrin-repressed DKO-S cells in the presence or absence of 20 nM recombinant human SDF-1α. Values are means of four determinations +/− standard deviation. (D) Caspase activity and percentage of apoptosis of clathrin-expressing and clathrin-repressed DKO-R cells in the presence or absence of 5 µM AMD3100. In both (C) and (D), cells were grown in standard DT40 medium with 1% chicken serum. Values are means of four determinations +/− standard deviation. Statistically significant differences, with p values, are indicated.</p

    Identification of the putative chicken survival factor as transferrin.

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    <p>(A) FPLC separation of the positive fraction from the gel filtration step showing separation of the main bioactivity peak from major protein fractions. In each case, cell growth after 72 hours was determined as described in materials and methods. (B) SDS polyacrylamide gel electophoresis of the fractions from the FPLC column. Fraction 6, which contains the major bioactivity peak contains only two major proteins identified as vitamin D binding protein and transferrin. (C) Western blot of FPLC fraction 6 using anti-(chicken transferrin) monoclonal antibody.</p

    Western blot showing the complete repression of clathrin expression in DKO-S and DKO-R cells when grown in the presence of 0.1 µM doxycycline (dox).

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    <p>Cells were grown for 72 hours in media with or without doxycycline as indicated. Following development of the blot, the nitrocellulose was stained with amido black to detect total protein.</p

    Analysis of the expression of transferrin and its receptor.

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    <p>(A) Quantitative RT-PCT of the transferrin receptor in both cell lines. (B) Western blot for the transferrin receptor in DKO-R and DKO-S cells. (C) Quantitative RT-PCR of transferrin in a control hepatic human cell line (Huh7) and DKO-R and DKO-S cells. Statistically significant differences, with p values, are indicated.</p
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