Cell Structure and Function
Online ISSN : 1347-3700
Print ISSN : 0386-7196
ISSN-L : 0386-7196
Volume 29 , Issue 2
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  • Valéria Pereira Nacife, Maria de Nazaré Correia Soeiro, ...
    2004 Volume 29 Issue 2 Pages 27-34
    Published: 2004
    Released: September 02, 2004
    JOURNALS FREE ACCESS FULL-TEXT HTML
    Macrophages are able to recognize, internalize and destroy a large number of pathogens, thus restricting the infection until adaptive immunity is initiated. In this work our aim was to analyze the surface charge of cells activated by carrageenan (CAR) and lipopolysaccharide (LPS) through light and electron microscopy approaches as well as the release of inflammatory mediators in vitro. The ultrastuctural analysis and the light microscopy data showed that in vivo administration of CAR represents a potent inflammatory stimulation for macrophages leading to a high degree of spreading, an increase in their size, in the number of the intracellular vacuoles and membrane projections as compared to the macrophages collected from untreated animals as well as mice submitted to LPS. Our data demonstrated that CAR stimulated-macrophages displayed a remarkable increase in nitric oxide production and PGE2 release as compared to the cells collected from non-stimulated and stimulated mice with LPS in vivo. On the other hand, non-stimulated macrophages as well as macrophages stimulated by LPS produce almost the same quantities of TNF-α, while in vivo stimulation by CAR leads to a 30–40% increase of cytokine release in vitro compared to the other groups.
    In conclusion, our morphological and biochemical data clearly showed that in vivo stimulation with CAR induces a potent inflammatory response in macrophages representing an interesting model to analyze inflammatory responses.
  • Guo-Yun Chen, Hisako Muramatsu, Keiko Ichihara-Tanaka, Takashi Muramat ...
    2004 Volume 29 Issue 2 Pages 35-42
    Published: 2004
    Released: September 02, 2004
    JOURNALS FREE ACCESS FULL-TEXT HTML
    We isolated a mouse cDNA encoding a protein that contains a BEACH domain, 5 WD40 repeats and a FYVE domain, which we designated as BWF1. The mRNA is approximately 10 kb in size and encodes a protein consisting of 3508 amino acids with a predicted molecular weight of 385 kDa. BWF1 has 45% homology with the Drosophila protein, blue cheese (BCHS). The BWF1 gene consists of 67 exons, which span 270 kb of genomic sequence, and has been mapped to mouse chromosome 5. Northern blot analysis revealed that it was strongly expressed in the liver, moderately in the kidney and testis, and weakly in the brain of adult mice. During the development of the mouse brain, BWF1 mRNA was abundant on embryonic day (E) 14–16; after birth, the level of BWF1 mRNA expression decreased markedly to reach the adult level at postnatal day 3. In situ hybridization analysis revealed that the expressed BWF1 mRNA was restricted to the marginal region both in E14 and E16 embryonic brain, but became diffuse after birth. Confocal microscopy studies of the epitope-tagged BWF1 protein showed that the protein was a cytoplasmic one.
  • Eiji Notsu, Akira Matsuno
    2004 Volume 29 Issue 2 Pages 43-48
    Published: 2004
    Released: September 02, 2004
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    The foot structure of molluscan (clam) catch muscle cells was studied from the structural and biochemical standpoints. In vertebrate cross striated muscle cells, foot structures are situated in the interspaces between T-tubules and sarcoplasmic reticula (SRs). By contrast, T-tubules were not observed in clam catch muscle cells, but foot structures were ultrastructurally identified in the interspaces between the SRs and cell membranes. We isolated the SR fraction from muscle cells which contained vesicles with SRs and cell membranes. Foot structures were also observed in the SR fraction by thin sectioning. The size and shape of the foot structure in both intact muscle cells and the SR fractions appeared to be slightly smaller than those of vertebrates. However, the molecular weight of the foot structures (foot proteins) as determined by SDS-PAGE (450 kD) was similar to ryanodine receptors (RyRs) which were reported previously in cross striated muscle cells from pecten and vertebrates. The protein showing the 450 kD band reacted to an anti-ryanodine receptor by Western blotting. These findings are discussed in comparison with previous studies of foot structures and RyRs of vertebrates and invertebrates.
  • Tomohiro Uemura, Takashi Ueda, Ryosuke L. Ohniwa, Akihiko Nakano, Kuni ...
    2004 Volume 29 Issue 2 Pages 49-65
    Published: 2004
    Released: September 02, 2004
    JOURNALS FREE ACCESS FULL-TEXT HTML
    In all eucaryotic cells, specific vesicle fusion during vesicular transport is mediated by membrane-associated proteins called SNAREs (soluble N-ethyl-maleimide sensitive factor attachment protein receptors).
    Sequence analysis identified a total of 54 SNARE genes (18 Qa-SNAREs/Syntaxins, 11 Qb-SNAREs, 8 Qc-SNAREs, 14 R-SNAREs/VAMPs and 3 SNAP-25) in the Arabidopsis genome. Almost all of them were ubiquitously expressed through out all tissues examined. A series of transient expression assays using green fluorescent protein (GFP) fused proteins revealed that most of the SNARE proteins were located on specific intracellular compartments: 6 in the endoplasmic reticulum, 9 in the Golgi apparatus, 4 in the trans-Golgi network (TGN), 2 in endosomes, 17 on the plasma membrane, 7 in both the prevacuolar compartment (PVC) and vacuoles, 2 in TGN/PVC/vacuoles, and 1 in TGN/PVC/plasma membrane.
    Some SNARE proteins showed multiple localization patterns in two or more different organelles, suggesting that these SNAREs shuttle between the organelles. Furthermore, the SYP41/SYP61-residing compartment, which was defined as the TGN, was not always located along with the Golgi apparatus, suggesting that this compartment is an independent organelle distinct from the Golgi apparatus. We propose possible combinations of SNARE proteins on all subcellular compartments, and suggest the complexity of the post-Golgi membrane traffic in higher plant cells.
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