scholarly journals The Use of Confocal Laser Microscopy to Analyze Mouse Retinal Blood Vessels

10.5772/56131 ◽  
2013 ◽  
Author(s):  
David Ramos ◽  
Marc Navarro ◽  
Luisa Mendes-Jorge ◽  
Ana Carretero ◽  
Mariana Lopez-Luppo ◽  
...  
Keyword(s):  
Blood Vessels ◽  
Confocal Laser Microscopy ◽  
Confocal Laser ◽  
Laser Microscopy ◽  
Retinal Blood Vessels

125 CONFOCAL LASER MICROSCOPY FOR DIAGNOSIS OF UROTHELIAL BLADDER CANCER: A TECHNOLOGY OF THE FUTURE?

2009 ◽  
Vol 8 (4) ◽  
pp. 152
Author(s):  
C. Wiesner ◽  
A. Salzer ◽  
R. Kiesslich ◽  
C. Hampel ◽  
R. Gillitzer ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Confocal Laser Microscopy ◽  
Confocal Laser ◽  
Urothelial Bladder Cancer ◽  
Laser Microscopy ◽  
The Future ◽  
Urothelial Bladder

Dynamic in vivo Imaging of Microvasculature and Perfusion by Miniaturized Confocal Laser Microscopy

2008 ◽  
Vol 41 (3) ◽  
pp. 290-297 ◽  
Author(s):  
M. Goetz ◽  
S. Thomas ◽  
A. Heimann ◽  
P. Delaney ◽  
C. Schneider ◽  
...  
Keyword(s):  
In Vivo Imaging ◽  
Confocal Laser Microscopy ◽  
Confocal Laser ◽  
Laser Microscopy

Probe-Based Confocal Laser Microscopy Identifies Criteria Predictive of Active Celiac Sprue

2011 ◽  
Vol 57 (2) ◽  
pp. 451-457 ◽  
Author(s):  
Heiko Pohl ◽  
Barbara T. Tanczos ◽  
Birgit Rudolph ◽  
Alexander Meining ◽  
Ahmed C. Khalifa ◽  
...  
Keyword(s):  
Confocal Laser Microscopy ◽  
Celiac Sprue ◽  
Confocal Laser ◽  
Laser Microscopy

scholarly journals Internalization of prolactin receptor and prolactin in transfected cells does not involve nuclear translocation

1997 ◽  
Vol 110 (9) ◽  
pp. 1123-1132 ◽  
Author(s):  
M. Perrot-Applanat ◽  
O. Gualillo ◽  
H. Buteau ◽  
M. Edery ◽  
P.A. Kelly
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Cell Lines ◽  
Map Kinases ◽  
Nuclear Translocation ◽  
Short Form ◽  
Confocal Laser Microscopy ◽  
Confocal Laser ◽  
Laser Microscopy ◽  
Transfected Cells

Prolactin (PRL) interacts with a specific, well characterized plasma membrane receptor (PRLR) that is coupled to signal transduction pathways involving Jak2, Fyn, and MAP kinases, and signal transducers and activators of transcription (STAT). Although a few previous studies have indicated nuclear translocation of PRL in IL-2 stimulated T lymphocytes, PRL-dependent Nb2 lymphoma cell lines and 235–1 lactotrophs, the mechanisms of nuclear targeting remain unknown and conflicting results have been reported concerning the putative nuclear translocation of the PRLR. We therefore decided to investigate nuclear translocation of PRLR and PRL in various cell lines transfected with an expression plasmid encoding PRLR, using confocal laser microscopy. We have constructed various cDNAs of the long and short forms of the rat PRLR containing an oligonucleotide encoding a Flag epitope inserted either just before the N-terminal amino acid or in the C-terminal end of the mature receptor (named N-terminal or C-terminal Flag-tagged PRLR). The corresponding receptors function as the PRLR in transfected cells: they are expressed at the plasma membrane and in compartments of the secretory pathway, they bind PRL with normal affinity (Kd= 4x10(−10) M) and have the same capacity to stimulate the transcriptional activity of a milk protein (beta-casein) gene as wild-type PRLR. In addition, the tagged receptors are much more efficiently immunodetected using anti-Flag antibodies, as compared to anti-PRL antibodies (U5 or U6). Immunofluorescence combined with detailed confocal laser microscopy showed that addition of PRL (0 to 12 hours) to COS-7, CHO and NIH-3T3 transfected fibroblasts induces rapid internalization of the receptor (long form), without any translocation to the nucleus. Using PRL-R tagged both in the N-terminal or C-terminal regions of the mature receptor excludes the possibility of a cleaved fragment which could have been subsequently imported into the nucleus. An absence of nuclear translocation of PRLR was also observed in a 293 cell line stably expressing the receptor, and in physiological targets for PRL, i.e. in Nb2 lymphoma cells expressing the Nb2 form of the receptor or in BGME mammary gland epithelial cells upon overexpression of a Flag-tagged PRLR. Similarly, the short form of the PRLR was not detected in nuclei of transfected COS cells upon PRL treatment. Clearly, our results provide evidence that internalization of the plasma membrane PRLR does not lead to nuclear translocation of the receptor, or part of it, in most fibroblasts and epithelial cells at physiological concentrations of PRL. Also, in co-localization experiments, PRL was internalized without nuclear translocation. Activation of STATs transcription factors and MAP kinases, as well as translocation of these proteins to the nucleus following their phosphorylation, probably remains the intracellular mechanism coupling stimulation to nuclear events.

Confocal laser microscopy to study microcirculation on the rat brain surface in vivo

1989 ◽  
Vol 504 (1) ◽  
pp. 159-160 ◽  
Author(s):  
Arno Villringer ◽  
Roman L. Haberl ◽  
Ulrich Dirnagl ◽  
Franziska Anneser ◽  
Michael Verst ◽  
...  
Keyword(s):  
Rat Brain ◽  
Confocal Laser Microscopy ◽  
Confocal Laser ◽  
Laser Microscopy ◽  
Brain Surface

scholarly journals Suppressive Effects of Hainosan (Painongsan) against Biofilm Production by Streptococcus mutans

2020 ◽  
Vol 8 (3) ◽  
pp. 71
Author(s):  
Masaaki Minami ◽  
Hiroshi Takase ◽  
Masayo Taira ◽  
Toshiaki Makino
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Streptococcus Mutans ◽  
Biofilm Formation ◽  
Confocal Laser Microscopy ◽  
Confocal Laser ◽  
Transmission Electron Microscopy Analysis ◽  
Laser Microscopy ◽  
Dental Plaques ◽  
Scanning Electron

Streptococcus mutans, a bacterium that causes dental plaques, forms a biofilm on tooth surfaces. This biofilm can cause gingivitis by stimulating the gingival margin. However, there is no established treatment for biofilm removal. Hainosan (Painongsan), a traditional Japanese Kampo formula, has been used to treat gingivitis. Therefore, we investigated the biofilm suppressive effects of the hainosan extract (HNS) and its components on S. mutans. We conducted scanning electron microscopy and confocal laser microscopy analyses to clarify the anti-biofilm activities of HNS and its crude drugs. We also performed a quantitative RT-PCR assay to assess the biofilm-related gene expression. HNS showed a significant dose-dependent suppressive effect on biofilm formation. Both the scanning electron microscopy and confocal laser microscopy analyses also revealed the significant inhibitory effects of the extract on biofilm formation. Transmission electron microscopy analysis showed that HNS disrupted the surface of the bacterial wall. Furthermore, HNS reduced the hydrophobicity of the bacteria, and suppressed the mRNA expression of β-glucosyltransferase (gtfB), glucosyltransferase-SI (gtfC), and fructosyltransferase (ftf). Among the constituents of hainosan, the extract of the root of Platycodon grandiflorum (PG) showed the strongest biofilm suppression effect. Platycodin D, one of the constituent natural compounds of PG, inhibited S. mutans-associated biofilm. These findings indicate that hainosan eliminates dental plaques by suppressing biofilm formation by S. mutans.

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