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  • 1.
    Akner, Gunnar
    et al.
    Örebro University, School of Health and Medical Sciences.
    Mossberg, K.
    Sundqvist, K. G.
    Gustafsson, J. A.
    Wikström, A. C.
    Evidence for reversible, non-microtubule and non-microfilament-dependent nuclear translocation of hsp90 after heat shock in human fibroblasts1992In: European Journal of Cell Biology, ISSN 0171-9335, E-ISSN 1618-1298, Vol. 58, no 2, p. 356-364Article in journal (Refereed)
    Abstract [en]

    A monoclonal antibody (29A) directed against rat liver heat shock protein M(r) 90,000 (hsp90) was produced. By Western immunoblotting of cytosols prepared from several different tissues and species, 29A was shown to specifically recognize only one band with M(r) approximately 90,000. Localization of hsp90 in human gingival fibroblasts was studied using the 29A antibody by indirect mono- and double-staining immunofluorescence and confocal laser scanning microscopy. The distribution was compared to that of the glucocorticoid receptor (GR) and various cytoskeletal structures. Cells were analyzed in interphase and mitosis under basal culture conditions, after heat shock and after microtubule and microfilament depolymerization, sometimes combined with heat shock. A major part of hsp90 immunoreactivity was diffusely distributed throughout the interphase cytoplasm, but a weak nuclear staining with non-stained nucleoli was also present, however, only detectable after methanol and not after formaldehyde/Triton X-100 fixation. Heat shock induced a time-dependent translocation of hsp90 from the cytoplasm to the cell nucleus reaching a plateau after 15 h. This compartment shift was reversible and also occurred in the absence of intact microtubules or intact microfilaments.

  • 2.
    Akner, Gunnar
    et al.
    Örebro University, School of Health and Medical Sciences.
    Sundqvist, K. G.
    Denis, M.
    Wikström, A. C.
    Gustafsson, J. A.
    Immunocytochemical localization of glucocorticoid receptor in human gingival fibroblasts and evidence for a colocalization of glucocorticoid receptor with cytoplasmic microtubules1990In: European Journal of Cell Biology, ISSN 0171-9335, E-ISSN 1618-1298, Vol. 53, no 2, p. 390-401Article in journal (Refereed)
    Abstract [en]

    The cellular distribution of the glucocorticoid receptor (GR) in relation to various intracellular and plasma membrane structures in human fibroblasts was studied using indirect immunofluorescence techniques with monoclonal and polyclonal antibodies. During interphase, GR was located predominantly in the cytoplasm, showing a similar pattern as tubulin. In mitotic cells, GR and tubulin were localized in mitotic spindles and in telophase midbodies. Colchicine and vinblastine induced a similar redistribution of GR and tubulin to the cell periphery. This redistribution was reversible for colchicine but not for vinblastine. Vinblastine also induced paracrystals containing GR and tubulin. These results support the hypothesis that GR interacts in vivo with cytoplasmic microtubules.

  • 3.
    Kälvegren, Hanna
    et al.
    Örebro University, School of Health and Medical Sciences. Fac Hlth Sci, Dept Med & Hlth Sci, Div Cardiovasc Med, Linköping Univ, Linköping, Sweden.
    Fridfeldt, Jonna
    Fac Hlth Sci, Dept Med & Hlth Sci, Div Drug Res, Linköping Univ, Linköping, Sweden.
    Bengtsson, Torbjörn
    Örebro University, School of Health and Medical Sciences. Fac Hlth Sci, Dept Med & Hlth Sci, Div Drug Res, Linköping Univ, Linköping, Sweden.
    The role of plasma adenosine deaminase in chemoattractant-stimulated oxygen radical production in neutrophils2010In: European Journal of Cell Biology, ISSN 0171-9335, E-ISSN 1618-1298, Vol. 89, no 6, p. 462-467Article in journal (Refereed)
    Abstract [en]

    Objectives: Adenosine deaminase (ADA) has a role in many immunity mediated disorders, such as asthma, tuberculosis and coronary artery disease. This study aims to investigate the ability of plasma ADA to modulate reactive oxygen species (ROS) production in neutrophils, and examine the involvement of adenosine and the cyclic AMP signaling pathway in this process. Methods: Neutrophils were stimulated, in the absence or presence of plasma, with the chemotactic peptide fMLP (formyl-methionyl-leucyl-phenylalanine), and the ROS production was determined with luminol-enhanced chemiluminescence. Activity of ADA was measured spectrophotometrically. Results: Plasma dose-dependently amplified the ROS generation in fMLP-stimulated neutrophils. In parallel, incubation of neutrophils in plasma elevated the total ADA-activity approximately 10 times from 1.3 U/ml to 12 U/ml. Inhibition of ADA, or type IV phosphodiesterases, significantly lowered the plasma-mediated ROS production. Furthermore, the high-affinity adenosine A(1) receptor antagonists DPCPX and 8-phenyltheophylline markedly inhibited the plasma-induced respiratory burst in neutrophils, suggesting an AI receptor-mediated mechanism. Conclusions: This study suggests that plasma ADA amplifies the release of toxic oxygen radicals from neutrophils through a downregulation of the inhibitory adenosine/cAMP-system and an enhanced activation of the stimulatory adenosine A(1)-receptor. This mechanism has probably a crucial role in regulating neutrophil function and in the defence against microbial infections. However, a sustained neutrophil activation could also contribute to inflammatory disorders such as atherosclerosis. (C) 2010 Elsevier GmbH. All rights reserved.

  • 4.
    Wigerius, Michael
    et al.
    Södertörn University, Huddinge, Sweden; Dalhousie University, Halifax, Canada.
    Asghar, Naveed
    Södertörn University, Huddinge, Sweden.
    Melik, Wessam
    Södertörn University, Huddinge, Sweden.
    Johansson, Magnus
    Örebro University, School of Health and Medical Sciences, Örebro University, Sweden.
    Scribble controls NGF-mediated neurite outgrowth in PC12 cells2013In: European Journal of Cell Biology, ISSN 0171-9335, E-ISSN 1618-1298, Vol. 92, no 6-7, p. 213-221Article in journal (Refereed)
    Abstract [en]

    Neurite outgrowth is mediated by dynamic changes of the cytoskeleton and is largely controlled by Rho GTPases and their regulators. Here, we show that the polarity protein Scribble controls PC12 cell neurite outgrowth in response to nerve growth factor. Scribble knockdown decreases neurite numbers and increases neurite length. This effect is linked to TrkA the cognate receptor for NGF as pharmacological inhibition of phosphorylated TrkA (pTrkA) reduces Scribble expression. Moreover, Scribble forms a complex with the MAPK components ERK1/2 in a growth factor dependent manner. In RNAi experiments where Scribble expression is efficiently depleted sustained ERK1/2 phosphorylation is reduced. Conversely, siRNA with intermediate Scribble silencing efficiency fails to match this effect indicating that ERK1/2 activation depends on basic Scribble protein levels. Finally, Scribble translocates to the plasma membrane in response to growth factor where it complexes with HRas and Rac1 suggesting that the phenotype activated by loss of Scribble may be a result of altered GTPase activity. Together, these results demonstrate a novel role for Scribble in neurite outgrowth of PC12 cells. (c) 2013 Elsevier GmbH. All rights reserved.

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