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  • MICROSCOPY  (6)
  • 1
    Keywords: CELLS ; MICROSCOPY ; IMAGES ; PROTEINS ; PAIRS ; ANTIGEN ; ANTIGENS ; FIELD ; PARTICLES ; IDENTIFICATION ; US ; LOCALIZATION ; immunocytochemistry ; QUANTITATIVE-ANALYSIS ; FLUORESCENCE ; SECTIONS ; electron microscopy ; automated detection ; gold particles ; IMMUNOGOLD ; immunolabeling ; slow-scan cooled CCD camera
    Abstract: This work presents a computerized method to identify, detect, evaluate, and, by colored overlay, present gold particle pairs in electron microscopy (EM), even in wide-field views. Double gold immunolabeled specimens were analyzed in a LEO 912 electron microscope equipped with a 2k x 2k-pixel slow-scan cooled CCD camera connected to a computer with analySIS 3.1 PRO image processing software. The acquisition of a high-resolution and high-dynamic-range image by the camera allowed correct segmentation of the gold particles, separating them from other cell structures and from the substrate. Particle identification was performed by a classification module designed by us. Based on shape and size, the computer recognized the group of small particles and classified them as either singular or clustered and differentiated these from the single bigger type. The final image shows the particle types separated and colored, and indicates the total number of objects encountered in the specific region of interest. Moreover, a montage tool allowed us to obtain final representative images of large microscopic fields, which on analysis by the Gold Finder module provided information on the distribution and localization of antigens comparable to that provided by the wide-field light microscope images. (C) 2003 Elsevier Science (USA). All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 12648569
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  • 2
    Keywords: IN-VIVO ; MICROSCOPY ; VIVO ; DNA ; NUCLEI ; CLEAVAGE ; STAGE ; EMBRYO ; SECTIONS ; EMBRYOS ; Biomphalaria straminea ; CLSM ; embryonic development ; GLAND ; snail
    Abstract: Biomphalaria straminea is a freshwater snail and one of the intermediate hosts of the trematode parasite which causes schistosomiasis in Brazil. The main stages of embryonic development were analyzed with confocal laser scanning microscopy (CLSM), using the fluorescent probe DiOC and Nile Red as a vital stain in in vivo preparations. In fixed preparations nuclei were stained by the Feulgen reaction or the fluorescent DNA probe, Hoechst 33342. Results obtained from the analysis of embryos at the stages of early cleavage, morula, blastula, gastrula, early trocophore and veliger showed that these stages are similar to those described for Biomphalaria glabrata and Biomphalaria tenagophila. CLSM optical sections of early trochophore showed important morphological structures such as the blastopore, stomodeum and shell gland; and in early veliger, internal organs such as the esophagus, stomach and male and female ducts were also clearly identified
    Type of Publication: Journal article published
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  • 3
    Keywords: EXPRESSION ; tumor ; Germany ; human ; MICROSCOPY ; SUPPORT ; liver ; primary ; hepatocytes ; DOWN-REGULATION ; ASSOCIATION ; ISOFORM ; STAGE ; UP-REGULATION ; DECREASE ; MEMBRANE ; LOCALIZATION ; MULTIDRUG-RESISTANCE PROTEIN ; HUMAN LIVER ; ORGANIZATION ; ABCC2 ; CONJUGATE EXPORT PUMP ; MRP2 ; ELIMINATION ; HUMAN-LIVER ; CANALICULAR MEMBRANES ; CHOLESTATIC RAT-LIVER ; CROSS-LINKING ; OBSTRUCTIVE CHOLESTASIS ; organic anion transporters,radixin,multidrug resistance protein,primary biliary cirrhosis,immunofluo
    Abstract: Background/Aims: Expression and localization of human hepatocellular transporters and of radixin, cross-linking actin with some membrane transporters, may change in cholestatic liver diseases.Methods: We investigated the uptake transporters OATP2 (SLC21A6), OATP8 (SLC21A8), and NTCP (SLC10A1), the export pumps MRP2 (ABCC2), MRP3 (ABCC3), MRP6 (ABCC6), and P-glycoproteins (ABCB1, ABCB4, ABCB11), and radixin, in non-icteric primary biliary cirrhosis (PBC stages I-III) and control human liver needle-biopsies using immunofluorescence microscopy and semi-quantitative RT-PCR.Results: Expression and localization of all transporters were unchanged in PBC I-II. Immunostaining intensities of uptake transporters decreased in PBC III with a concomitant decrease in mRNA levels. Immunostaining intensities and mRNA levels of export pumps were similar in controls and PBC I-III, however, irregular MRP2 immunostaining suggested redistribution of MRP2 into intracellular structures in PBC III. Areas of irregular MRP2 immunostaining showed largely reduced radixin immunostaining, whereas normal hepatocytes had MRP2 and radixin confined to the canalicular membrane. Disrupted localization of radixin and MRP2 supports the concept that radixin contributes to the canalicular localization of MRP2.Conclusions: Down-regulation of uptake transporters may contribute to the impaired hepatobiliary elimination in advanced PBC, and partially altered localization of MRP2 may reflect the onset of changes leading to icteric PBC. (C) 2003 European Association for the Study of the Liver. Published by Elsevier B.V. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 14568249
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  • 4
    Keywords: CANCER ; CELLS ; GROWTH ; GROWTH-FACTOR ; tumor ; carcinoma ; Germany ; human ; MICROSCOPY ; DIAGNOSIS ; PROTEIN ; PROTEINS ; TUMORS ; COMPLEX ; COMPLEXES ; INDUCTION ; KERATINOCYTES ; SKIN ; ASSOCIATION ; immunohistochemistry ; skin cancer ; CARCINOMA-CELLS ; LOCALIZATION ; ADHESION ; intermediate filaments ; CARCINOMAS ; INVOLVEMENT ; squamous cell carcinoma ; beta-catenin ; epidermis ; human hair follicle ; HUMAN EPIDERMIS ; SKIN-CANCER ; CATENIN ; basal cell carcinoma ; HUMAN SKIN ; EPIDERMAL-GROWTH-FACTOR ; INNER-ROOT-SHEATH ; RE ; keratinocyte ; TUMORIGENESIS ; HAIR FOLLICLE ; SKIN CANCERS ; cell adhesion ; hair ; INTERCELLULAR-JUNCTIONS ; BCC ; DESMOSOMAL PLAQUE PROTEINS ; ADHERENS JUNCTIONS ; CELL-CARCINOMA ; E-CADHERIN EXPRESSION ; actin-binding protein ; INTERCELLULAR-ADHESION
    Abstract: Isoform E2 of drebrin, an actin-binding protein originally identified in neuronal cells, has recently been identified in diverse non-neuronal cells, mostly in association with cell processes and intercellular junctions. Here, we report on the presence of drebrin in normal human skin, epithelial skin cancers, and cultured keratinocytes. Keratinocytes of normal epidermis contain almost no drebrin but the protein is readily seen in hair follicles. By immunohistochemistry and immunoblot, basal cell carcinomas (BCC) are rich in drebrin, and confocal laser scanning and immunoelectron microscopy show accumulation at adhering junctions, in co-localization with actin and partially with plaque proteins. In squamous cell carcinomas, keratoacanthomas, and in epidermal precancers, drebrin is heterogeneously distributed, appearing as mosaics. Primary keratinocyte cultures contain significant amounts of drebrin enriched at adhering junctions. When epithelium-derived cells devoid of drebrin are transfected with drebrin-enhanced green fluorescent protein, constructs accumulate in the cell periphery, and immunoprecipitation shows complexes with actin. During epidermal growth factor induced formation of cell processes, drebrin retains this junction association, as observed by live cell microscopy. Our results suggest novel functions of drebrin such as an involvement in cell-cell adhesion and tumorigenesis and a potential value in diagnosis of BCC
    Type of Publication: Journal article published
    PubMed ID: 16185277
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  • 5
    Keywords: CANCER ; CELLS ; EXPRESSION ; CELL ; Germany ; MICROSCOPY ; IMAGES ; QUANTIFICATION ; SYSTEM ; TOOL ; DISEASE ; DISEASES ; GENE ; GENE-EXPRESSION ; GENES ; EFFICIENCY ; TISSUE ; gene transfer ; GENE-TRANSFER ; TISSUES ; SEQUENCE ; treatment ; FREQUENCY ; FREQUENCIES ; NUCLEI ; TARGET ; TRANSPORT ; gene expression ; EFFICIENT ; DELIVERY ; LOCALIZATION ; molecular ; review ; HELA-CELLS ; REPORTER GENE ; development ; analysis ; methods ; NUCLEAR ; cancer research ; PLASMID ; TOXICOLOGY ; DIVISION ; transfer efficiency ; German ; nuclear localization ; PLASMIDS ; scanning ; TRANSPORT-SYSTEM
    Abstract: An efficient gene transfer into target tissues and cells is needed for safe and effective treatment of genetic diseases like cancer. In this paper, we describe the development of a transport system and show its ability for transporting plasmids. This non-viral peptide-based BioShuttle-mediated transfer system consists of a nuclear localization address sequence realizing the delivery of the plasmid phNIS-IRES-EGFP coding for two independent reporter genes into nuclei of HeLa cells. The quantification of the transfer efficiency was achieved by measurements of the sodium iodide symporter activity. EGFP gene expression was measured with Confocal Laser Scanning Microscopy and quantified with biostatistical methods by analysis of the frequency of the amplitude distribution in the CLSM images. The results demonstrate that the "BioShuttle"-Technology is an appropriate tool for an effective transfer of genetic material carried by a plasmid.
    Type of Publication: Journal article published
    PubMed ID: 18026568
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  • 6
    Keywords: PEPTIDE ; SIMULATIONS ; CANCER ; CELLS ; INHIBITOR ; CELL ; Germany ; human ; LUNG ; MICROSCOPY ; DRUG ; DYNAMICS ; SIMULATION ; MOLECULE ; FORM ; TRANSPORT ; virus ; MEMBRANE ; LYMPHOCYTES ; bioshuttle ; DELIVERY ; MITOCHONDRIA ; PEPTIDES ; HUMAN IMMUNODEFICIENCY VIRUS ; LIVING CELLS ; 1 ; IMMUNODEFICIENCY-VIRUS ; MEMBRANES ; HUMAN-IMMUNODEFICIENCY-VIRUS ; MOLECULAR-DYNAMICS ; HIV-1 ; HUMAN-LYMPHOCYTES ; CAPACITY ; ASSEMBLIES ; assembly ; CLSM ; development ; structure ; solubility ; DRUG DEVELOPMENT ; docking ; anti-HIV ; CANDIDATE ; cancer research ; capsid ; TOXICOLOGY ; VICINITY ; DIVISION ; German ; molecular dynamics ; circular dichroism ; CIRCULAR-DICHROISM ; confocal laser scanning microscopy ; CD ; A ; AS ; Research ; DICHROISM ; HIV 1 ; HUMAN IMMUNODEFICIENCY ; IMMUNODEFICIENCY ; LA ; LASER ; LASER SCANNING MICROSCOPY ; Lead ; LYMPHOCYTE
    Abstract: The Human immunodeficiency virus 1 derived capsid assembly inhibitor peptide (HIV-1 CAI-peptide) is a promising lead candidate for anti-HIV drug development. Its drawback, however, is that it cannot permeate cells directly. Here we report the transport of the pharmacologically active CAI-peptide into human lymphocytes and Human Embryonic Lung cells (HEL) using the BioShuttle platform. Generally, the transfer of pharmacologically active substances across membranes, demonstrated by confocal laser scanning microscopy (CLSM), could lead to a loss of function by changing the molecule's structure. Molecular dynamics (MD) simulations and circular dichroism (CD) studies suggest that the CAI-peptide has an intrinsic capacity to form a helical structure, which seems to be critical for the pharmacological effect as revealed by intensive docking calculations and comparison with control peptides. This coupling of the CAI-peptide to a BioShuttle-molecule additionally improved its solubility. Under the conditions described, the HIV-1 CAI peptide was transported into living cells and could be localized in the vicinity of the mitochondria.
    Type of Publication: Journal article published
    PubMed ID: 18695744
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