Conceptualizing resistance

The 1990s saw a proliferation of sociological work applying Foucault's ideas on governmentality to health promotion and public health. This work characterized public health discourses as regimes of power and knowledge employed in the regulation and surveillance of individuals and populations. This article is concerned with the question of how and to what extent those who are subject to such regimes are able to resist them. We seek to identify the various forms in which resistance to such regimes of power have been manifest in empirical studies of health and illness. Our aims are threefold. The first is to alert empirical researchers who wish to examine resistance in the context of health and health care to the subtle and nuanced ways in which such resistance can be manifested both within and outside encounters with health professionals. This is achieved through tracing both the evolution of Foucault's own concepts around resistance and the way in which these ideas have been mobilized in empirical studies. The second, and related, aim is to demonstrate the complex forms which such resistance takes, problematizing the simplistic assumptions that adherence to health promotion advice necessarily implies the collapse of agency, and that resistance necessarily involves the rejection of advice and interventions. The third is to highlight the potentially problematic normative qualities that may be assigned to resistance

SNO proteins from HepG2 cells as identified via SNO-RAC proteomic analysis.

<p>SNO proteins from HepG2 cells as identified via SNO-RAC proteomic analysis.</p

Myocardial perfusion protocols.

<p>Perfusion protocols for <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0111448#pone-0111448-g002" target="_blank">Figure 2</a> (<b>A</b>) and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0111448#pone-0111448-t001" target="_blank">Table 1</a> (<b>B</b>).</p

Age criteria for cervical screening in England: qualitative study of women’s views

The age criteria applied in the NHS Cervical Screening Programme have been much debated at policy and professional levels, but little is known about women’s views on appropriate age criteria. Our objective is to provide insight into women’s views on age criteria for the NHS Cervical Screening Programme in England. We present data collected as part of a qualitative interview study conducted in the East Midlands of England. Thirty-five women, representing a range of ages and ethnic groups, were interviewed. Analysis was based on the constant comparative method. Women’s views about the age criteria that should appropriately be applied to cervical cancer screening diverged considerably from the technical principles and criteria upon which policy decisions are based. Women called for screening to be extended at both the upper and the lower ends of the age range. However, there was little explicit acknowledgement in women’s accounts of the risks posed by screening or of the relative effectiveness and cost-effectiveness of screening in women of different ages. Policy decisions about screening programmes often face problems of legitimacy and acceptability. There is an increasingly pressing need to ensure that the criteria used to make decisions about who will be offered screening are made explicit and communicated effectively, so that people’s views can be well-informed

Mitochondrial GAPDH and total GAPDH levels following cardioprotection.

<p>(<b>A</b>) GAPDH protein levels in the mitochondrial fraction of hearts subjected to control or an IPC-I/R protocol were assessed via liquid chromatography-tandem mass spectrometry, followed by label-free peptide quantification (*p<0.05 vs. control, n = 3). (<b>B</b>) Total GAPDH protein levels in hearts subjected to control or an IPC-I/R protocol were assessed via western blot analysis. Representative western blots are shown for total GAPDH (upper) and enolase (lower) in whole heart homogenates together with the densitometry of GAPDH normalized to enolase (n = 3).</p

GAPDH and SNO-GAPDH are imported into the matrix of heart mitochondria.

<p>Mitochondrial GAPDH protein levels were assessed after the addition of purified GAPDH or SNO-GAPDH to isolated mitochondria from control and IPC hearts. (<b>A</b>) Representative western blots for GAPDH (upper), TOM20 (center), and the α subunit of F₁F₀-ATPase (lower) in control heart and IPC heart mitochondria. Control: non-treated mitochondrial control; GAPDH: purified GAPDH treated mitochondria; SNO-GAPDH: SNO-GAPDH treated mitochondria. (<b>B</b>) GAPDH import into control and IPC heart mitochondria as assessed via the percentage of GAPDH following trypsin digestion compared to GAPDH levels prior to the addition of trypsin. GAPDH levels were assessed via densitometry (n = 3).</p

GAPDH acts as a mitochondrial trans-S-nitrosylase.

<p>GAPDH and SNO-GAPDH can be imported into the mitochondria, where SNO-GAPDH targets Hsp60, ACAT1, and VDAC1 as a mitochondrial trans-<i>S</i>-nitrosylase.</p

HepG2 cell line as a model system for examining GAPDH as a trans-S-nitrosylase.

<p>(<b>A</b>) Expression of neuronal and endothelial isoforms of NO synthase in HepG2 cells. Representative western blots are shown for neuronal (top right) and endothelial (top left) NO synthase and β-actin (lower). (<b>B</b>) Mitochondrial GAPDH protein levels were assessed after the addition of purified GAPDH to isolated HepG2 mitochondria. Representative western blots for GAPDH (upper), TOM20 (center), and the α subunit of F₁F₀-ATPase (lower) in HepG2 mitochondria. Control: non-treated mitochondrial control; GAPDH: purified GAPDH treated mitochondria; (n = 3). (<b>C</b>) and (<b>D</b>) Hep2G cells were transfected with either a control GFP plasmid or siRNA scramble, a plasmid encoding DDK-tagged GAPDH for overexpression, a GAPDH siRNA for knock-down, or a plasmid encoding DDK-tagged GAPDH_C150S for overexpression. Representative western blots are shown together with the densitometry of GAPDH normalized to β-actin for total GAPDH (upper; GAPDH, GAPDH-DDK, GAPDH_C150S-DDK) and β-actin (lower; *p<0.05 vs. control; n = 6).</p

SNO-GAPDH increases mitochondrial SNO levels.

<p>A representative gel is shown for mitochondrial SNO levels measured via DyLight800 fluorescence after the addition of purified GAPDH or SNO-GAPDH. MW: molecular weight marker; GSNO (+): GSNO treatment was used as a positive control for mitochondrial SNO; Control: non-treated mitochondrial control; GSNO: filtered GSNO treated mitochondria; GAPDH: purified GAPDH treated mitochondria; SNO-GAPDH: SNO-GAPDH treated mitochondria. <i>Please note</i>: the filtration procedure serves to remove excess GSNO following the incubation of purified GAPDH with GSNO (n = 3).</p

GAPDH overexpression increases in SNO-Hsp60, but not SNO-DHRS2 levels.

<p>SNO-Hsp60 (<b>A</b>) and SNO-DHRS2 (<b>B</b>) levels from Hep2G cells transfected with either a control GFP plasmid or siRNA scramble, a plasmid encoding DDK-tagged GAPDH for overexpression, a GAPDH siRNA for knock-down, or a plasmid encoding DDK-tagged GAPDH_C150S were assessed via SNO-RAC proteomic analysis, followed by label-free peptide quantification (n = 6).</p