69 research outputs found

    Middle Eastern mothers in Sweden, their experiences of the maternal health service and their partner's involvement

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    <p>Abstract</p> <p>Background</p> <p>Traditional patterns relating to how to handle pregnancy and birth are often challenged due to migration. The purpose of this study was to describe Middle Eastern mothers' experiences of the maternal health care services in Sweden and the involvement of their male partner.</p> <p>Methods</p> <p>Thirteen immigrant mothers from the Middle East who had used the maternal health services in Sweden were interviewed using focus group discussions and individual interviews. These were taped, transcribed and analysed according to Content analysis.</p> <p>Results</p> <p>The four main categories that developed were:</p> <p>• Access to the professional midwife</p> <p>• Useful counselling</p> <p>• Stable motherhood in transition</p> <p>• Being a family living in a different culture</p> <p>Conclusion</p> <p>According to the respondents in this study, understanding the woman's native language or her culture was not vital to develop a good relationship with the midwife. Instead the immigrant woman developed trust in the midwife based on the knowledge and the empathy the midwife imparted.</p> <p>Increasing the amount of first trimester antenatal visits could avoid spontaneous visits to the emergency clinic. There was a greater need for involvement and support by the father during the perinatal period, such as caring for older children and carrying out household chores since the mothers' earlier female network was often lost.</p> <p>Clinical implications</p> <p>There is a need to involve immigrant parents in the available parental education in order to prepare them for parenthood in their new country as well as to explore their altered family situation. Collecting immigrant women and their partner's, experiences of maternal health care services offers a possibility to improve the existing care, both in content, access and availability where the timing of visits and content require further evaluation.</p

    Phosphatidylinositol 4-kinases in plasma membranes and Affinity partitioning of liposomes: a model system for membrane purification

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    Polyphosphoinositides, the different phosphorylated variants of the phospholipid phosphatidylinositol (PtdIns), are used in a wide array of intracellular mechanisms in eukaryotic cells. The phosphorylation of PtdIns at carbon D4, catalyzed by phosphatidylinositol 4-kinase, is an important step in the synthesis of several of these molecules. The presence of different isoenzymes of PtdIns 4-kinase in rat liver plasma membranes and their further distribution in plasma membrane domains was examined. The wortmannin-sensitive kinase PI4K230 was located in blood sinusoidal plasma membrane domains (ca 25% of the total cell content), while PI4K92, also wortmannin-sensitive, could not be detected in plasma membranes. Together with earlier observations of the wortmannin sensitivity of the PtdIns 4,5-P2 synthesis during agonist stimulation, this indicates that PI4K230 is involved in transmembrane signaling. The presence of wortmannin-sensitive PtdIns 4-kinase activity in plasma membranes was confirmed by experiments on rabbit lacrimal glands. A third isoenzyme, PI4K55, was mainly found in exocytic vesicles, but a small part (less than 10%) was located in lateral plasma membrane domains. Such a distribution might suggest a role in intracellular membrane transport, but possibly also in the maintenance of cell-cell adhesion complexes. PtdIns 4-kinase activity was examined in spinach plasma membranes as well. Two different fractions containing PtdIns 4-kinase activity were resolved by chromatography. The molecular weights of the corresponding isoenzymes were determined to be 120 and 65 kDa respectively, and they were shown to differ in their sensitivity to wortmannin and the response to divalent cations. Both isoenzymes reacted with an antibody directed against mammalian a isoforms thereby implicating a relation to the mammalian PI4K230. Affinity partitioning in poly(ethylene glycol)/dextran two-phase systems using wheat germ agglutinin coupled to dextran as affinity ligand is an efficient and highly specific method to purify plasma membranes from different sources, as shown, for instance, in the work concerning PtdIns 4-kinase. In order to extend the method to be of general use in the purification of membranes, it was necessary to explore basic requirements for the affinity partitioning of subcellular membranes. To this end, biotinylated liposomes were used as model membranes. Such liposomes could be specifically redistributed to the dextran-rich bottom phase by avidin-dextran, but only if millimolar concentrations of Li2SO4 was included in the system. As little as 1 or 2 biotin residues per liposome was sufficient to cause this redistribution. Furthermore, negative surface charges affected the redistribution by interfering with the biotin-avidin binding, but not with the partitioning of the liposome/dextran conjugate per se. Thus, basic knowledge was gained setting the stage for future development of affinity partitioning as a tool for the purification of biological membranes

    Plasma Membranes: Methods for Preparation

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    Purifications of plasma membranes by affinity partioning.

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    This chapter describes the purification of rat liver plasma membranes by affinity partitioning in an aqueous polymer two-phase system using the lectin wheat germ agglutinin (WGA) as affinity ligand. Affinity partitioning is advantageous for conventional membrane fractionation techniques in being highly selective, allowing the rapid and high-yield purification of membranes. In addition, the aqueous polymer environment is gentle to membrane structure and function, which is of importance when studying labile structures and components. A two-phase system will form when aqueous solutions of two structurally different polymers are mixed at sufficiently high concentrations (1). A commonly used polymer pair is polyethylene glycol 3350 (PEG) and Dextran T500. These polymers will form a two-phase system at concentrations above 5.4% (w/w) of each, the top phase being enriched in PEG and the bottom phase in Dextran. A conventional two-phase system like this may be used for the fractionation of biological material, including membranes. The distribution of material between the phases is modulated by altering polymer concentration and salt contents of the system (2), but the selectivity is often insufficient for the ready separation of membranes

    Cetuximab sensitivity associated with oxaliplatin resistance in colorectal cancer.

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    BACKGROUND: Clinical studies have suggested that the epidermal growth factor receptor (EGFR)-inhibiting antibody cetuximab may have better effect in the third-line treatment of metastatic colorectal cancer, after failure of standard chemotherapy including oxaliplatin, compared to using it up-front in the first line. The reason behind this suggestion is unclear. MATERIALS AND METHODS: The effect of cetuximab on cell growth was investigated in five isogenic colon cancer cell lines with increasing level of acquired oxaliplatin resistance. The expression of EGFR and the activity of down-stream signalling molecules were measured by western blot analyses. RESULTS: A marked increase in sensitivity to cetuximab, accompanied by an up-regulation of EGFR, was observed in the oxaliplatin-resistant cell lines. CONCLUSION: The connection between oxaliplatin resistance and cetuximab sensitivity has not been previously reported in the literature. Such a connection could be of clinical importance and constitutes a substantial an argument for saving cetuximab until later treatment lines, when the tumours have become chemotherapy resistant

    Coomassie Staining as Loading Control in Western Blot Analysis

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    In Western blotting, immunodetection of housekeeping proteins is routinely performed to detect differences in electrophoresis loading. The present work describes a much faster and simpler protein staining method, which is compatible with ordinary blocking conditions. In addition, the method can be used after immunodetection with superior linearity compared to ordinary staining methods. After immunoblotting and staining, protein bands can be further identified using peptide mass fingerprinting

    Localization of phosphatidylinositol 4-kinase isoenzymes in rat liver plasma membrane domains

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    The presence of different isoenzymes of phosphatidylinositol 4-kinase in isolated rat liver plasma membranes and their further distribution in plasma membrane domains was examined. Both wortmannin-sensitive and -insensitive PtdIns 4-kinase activities were detected in highly purified plasma membranes obtained by aqueous two-phase affinity partitioning. The wortmannin-sensitive enzyme was identified as the 230 kDa isoform by Western blotting, whereas the 92 kDa isoform was not detected in plasma membranes. The apparent molecular weights of these isoforms were 205 and 105 kDa on SDS polyacrylamide gel electrophoresis, but approximately 500 and 230 kDa respectively on gel filtration, suggesting that both enzymes either are dimers or composed of heterologous subunits. Approximately 25% of the total 230 kDa isoenzyme present in liver, and only ca 5% of the wortmannin-insensitive one, was associated with the plasma membrane fraction. Plasma membrane domains were isolated by a combination of sucrose and Nycodenz gradient centrifugations. The 230 kDa isoform was identified in the blood sinusoidal domain, but not in the bile canalicular one, and was also found in lateral plasma membranes. The wortmannin-insensitive isoenzyme was present only in this latter material. The functional implications of this distribution of PtdIns 4-kinase isoenzymes in plasma membrane regions are discussed

    Purification of plasma membranes by affinity partitioning

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    This chapter describes the purification of rat liver plasma membranes by affinity partitioning in an aqueous polymer two-phase system using the lectin wheat germ agglutinin (WGA) as affinity ligand. Affinity partitioning is advantageous for conventional membrane fractionation techniques in being highly selective, allowing the rapid and high-yield purification of membranes. In addition, the aqueous polymer environment is gentle to membrane structure and function, which is of importance when studying labile structures and components. A two-phase system will form when aqueous solutions of two structurally different polymers are mixed at sufficiently high concentrations (1). A commonly used polymer pair is polyethylene glycol 3350 (PEG) and Dextran T500. These polymers will form a two-phase system at concentrations above 5.4% (w/w) of each, the top phase being enriched in PEG and the bottom phase in Dextran. A conventional two-phase system like this may be used for the fractionation of biological material, including membranes. The distribution of material between the phases is modulated by altering polymer concentration and salt contents of the system (2), but the selectivity is often insufficient for the ready separation of membranes
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