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  • 1.
    Dreier, Jes
    et al.
    KTH, School of Engineering Sciences (SCI), Applied Physics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
    Castello, Marco
    Ist Italiano Tecnol, Mol Microscopy & Spect, Via Morego 30, I-16136 Genoa, Italy..
    Coceano, Giovanna
    KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Engineering Sciences (SCI), Applied Physics.
    Caceres, Rodrigo
    PSL Res Univ, CNRS, Inst Curie, Lab Phys Chim Curie, F-75005 Paris, France.;Sorbonne Univ, F-75005 Paris, France.;Univ Paris 05, F-75005 Paris, France..
    Plastino, Julie
    PSL Res Univ, CNRS, Inst Curie, Lab Phys Chim Curie, F-75005 Paris, France.;Sorbonne Univ, F-75005 Paris, France..
    Vicidomini, Giuseppe
    Ist Italiano Tecnol, Mol Microscopy & Spect, Via Morego 30, I-16136 Genoa, Italy..
    Testa, Ilaria
    KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Engineering Sciences (SCI), Applied Physics.
    Smart scanning for low-illumination and fast RESOLFT nanoscopy in vivo2019In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 10, article id 556Article in journal (Refereed)
    Abstract [en]

    RESOLFT fluorescence nanoscopy can nowadays image details far beyond the diffraction limit. However, signal to noise ratio (SNR) and temporal resolution are still a concern, especially deep inside living cells and organisms. In this work, we developed a non-deterministic scanning approach based on a real-time feedback system which speeds up the acquisition up to 6-fold and decreases the light dose by 70-90% for in vivo imaging. Also, we extended the information content of the images by acquiring the complete temporal evolution of the fluorescence generated by reversible switchable fluorescent proteins. This generates a series of images with different spatial resolution and SNR, from conventional to RESOLFT images, which combined through a multi-image deconvolution algorithm further enhances the effective resolution. We reported nanoscale imaging of organelles up to 35 Hz and actin dynamics during an invasion process at a depth of 20-30 mu m inside a living Caenorhabditis elegans worm.

  • 2.
    Masullo, Luciano A.
    et al.
    KTH, School of Engineering Sciences (SCI), Applied Physics.
    Boden, Andreas
    KTH, School of Engineering Sciences (SCI), Applied Physics.
    Pennacchietti, Francesca
    KTH, School of Engineering Sciences (SCI), Applied Physics.
    Coceano, Giovanna
    KTH, School of Engineering Sciences (SCI), Applied Physics.
    Ratz, Michael
    Karolinska Inst, Dept Cell & Mol Biol, S-17176 Stockholm, Sweden..
    Testa, Ilaria
    KTH, School of Engineering Sciences (SCI), Applied Physics.
    Enhanced photon collection enables four dimensional fluorescence nanoscopy of living systems2018In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 9, article id 3281Article in journal (Refereed)
    Abstract [en]

    The theoretically unlimited spatial resolution of fluorescence nanoscopy often comes at the expense of time, contrast and increased dose of energy for recording. Here, we developed MoNaLISA, for Molecular Nanoscale Live Imaging with Sectioning Ability, a nanoscope capable of imaging structures at a scale of 45-65 nm within the entire cell volume at low light intensities (W-kW cm(-2)). Our approach, based on reversibly switchable fluorescent proteins, features three distinctly modulated illumination patterns crafted and combined to gain fluorescence ON-OFF switching cycles and image contrast. By maximizing the detected photon flux, MoNaLISA enables prolonged (40-50 frames) and large (50 x 50 mu m(2)) recordings at 0.3-1.3 Hz with enhanced optical sectioning ability. We demonstrate the general use of our approach by 4D imaging of organelles and fine structures in epithelial human cells, colonies of mouse embryonic stem cells, brain cells, and organotypic tissues.

  • 3. Richter, Katharina N.
    et al.
    Revelo, Natalia H.
    Seitz, Katharina J.
    Helm, Martin S.
    Sarkar, Deblina
    Saleeb, Rebecca S.
    D'Este, Elisa
    Eberle, Jessica
    Wagner, Eva
    Vogl, Christian
    Lazaro, Diana F.
    Richter, Frank
    Coy-Vergara, Javier
    Coceano, Giovanna
    KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Engineering Sciences (SCI), Applied Physics.
    Boyden, Edward S.
    Duncan, Rory R.
    Hell, Stefan W.
    Lauterbach, Marcel A.
    Lehnart, Stephan E.
    Moser, Tobias
    Outeiro, Tiago F.
    Rehling, Peter
    Schwappach, Blanche
    Testa, Ilaria
    KTH, School of Engineering Sciences (SCI), Applied Physics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
    Zapiec, Bolek
    Rizzoli, Silvio O.
    Glyoxal as an alternative fixative to formaldehyde in immunostaining and super-resolution microscopy2018In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 37, no 1, p. 139-159Article in journal (Refereed)
    Abstract [en]

    Paraformaldehyde (PFA) is the most commonly used fixative for immunostaining of cells, but has been associated with various problems, ranging from loss of antigenicity to changes in morphology during fixation. We show here that the small dialdehyde glyoxal can successfully replace PFA. Despite being less toxic than PFA, and, as most aldehydes, likely usable as a fixative, glyoxal has not yet been systematically tried in modern fluorescence microscopy. Here, we tested and optimized glyoxal fixation and surprisingly found it to be more efficient than PFA-based protocols. Glyoxal acted faster than PFA, cross-linked proteins more effectively, and improved the preservation of cellular morphology. We validated glyoxal fixation in multiple laboratories against different PFA-based protocols and confirmed that it enabled better immunostainings for a majority of the targets. Our data therefore support that glyoxal can be a valuable alternative to PFA for immunostaining.

  • 4. Terriac, Emmanuel
    et al.
    Coceano, Giovanna
    KTH, School of Engineering Sciences (SCI), Applied Physics, Cellular Biophysics.
    Mavajian, Zahra
    KTH, School of Engineering Sciences (SCI), Applied Physics.
    Hageman, Tijmen A. G.
    Christ, Andreas F.
    Testa, Ilaria
    KTH, School of Engineering Sciences (SCI), Applied Physics, Cellular Biophysics.
    Lautenschlaeger, Franziska
    Gad, Annica K. B.
    Vimentin Levels and Serine 71 Phosphorylation in the Control of Cell-Matrix Adhesions, Migration Speed, and Shape of Transformed Human Fibroblasts2017In: CELLS, ISSN 2073-4409, Vol. 6, no 1, article id 2Article in journal (Refereed)
    Abstract [en]

    Metastasizing tumor cells show increased expression of the intermediate filament (IF) protein vimentin, which has been used to diagnose invasive tumors for decades. Recent observations indicate that vimentin is not only a passive marker for carcinoma, but may also induce tumor cell invasion. To clarify how vimentin IFs control cell adhesions and migration, we analyzed the nanoscale (30-50 nm) spatial organization of vimentin IFs and cell-matrix adhesions in metastatic fibroblast cells, using three-color stimulated emission depletion (STED) microscopy. We also studied whether wild-type and phospho-deficient or -mimicking mutants of vimentin changed the size and lifetime of focal adhesions (FAs), cell shape, and cell migration, using live-cell total internal reflection imaging and confocal microscopy. We observed that vimentin exists in fragments of different lengths. Short fragments were mostly the size of a unit-length filament and were mainly localized close to small cell-matrix adhesions. Long vimentin filaments were found in the proximity of large FAs. Vimentin expression in these cells caused a reduction in FAs size and an elongated cell shape, but did not affect FA lifetime, or the speed or directionality of cell migration. Expression of a phospho-mimicking mutant (S71D) of vimentin increased the speed of cell migration. Taken together, our results suggest that in highly migratory, transformed mesenchymal cells, vimentin levels control the cell shape and FA size, but not cell migration, which instead is linked to the phosphorylation status of S71 vimentin. These observations are consistent with the possibility that not only levels, but also the assembly status of vimentin control cell migration.

1 - 4 of 4
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