Ultrastructure of 30–40 million year old leaflets from Dominican amber (Hymenaea protera,Fabaceae: Angiospermae)

Hymenaea protera leaflet fossils entombed in amber, dated at 30 to 40 million years (mine strata and exomethylene dating) were observed by both light and transmission electron microscopy. Ultrastructure preservation in these leaflets shows the presence of chloroplasts with thylakoid membranes, cell walls, mitochondria with associated endoplasmic reticulum, nuclei, and xylem tissue. Tissues show varying degrees of degradation; however, natural resin, which has perfused the cells, seems to maintain the structural integrity of the membranes and walls. We conclude that preservation of amber entombed organisms results from dehydration and slow fixative properties leaving the ultrastructure in excellent condition. These findings parallel reports on the exceptional preservation of amino acids and of DNA in amber-entombed organisms.     

Cytologie fine des cellules interstitielles du testicule du poissonLebistes reticulatus R.

Summary The active interstitial cells of the testis ofLebistes reticulatus R. have numerous, big, dense mitochondria of tubular structure and a developed endoplasmic reticulum. The formation of lipochrome pigment granules corresponds to a degenerative evolution of these cells.     

Développement cyclique du réticulum endoplasmique agranulaire dans les glandes thoraciques (glandes ecdysiales) deRhodnius prolixus Stäl (Insecte: Hétéroptère) aux deux derniers stades larvaires

Summary Ultrastructural study of the thoracic glands ofRhodnius prolixus at the 2 last larval instars demonstrates the cyclic differentiation of meshed networks of agranular endoplasmic reticulum. At the time of abdomen apolysis the ecdysial cells are compartmentalized into a peripheral array of agranular reticulum with sparsely mitochondria. The close association of agranular reticulum and mitochondria is interpreted as indicative of functional coupling in relation with steroid like ecdysone synthesis.

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Les auteurs tiennent à remercier le Dr J.-M. Pinet (I.N.A., Paris) pour l'envoi de la souche deRhodnius utilisée dans nos élevages.     

Signaling pathways between the plasma membrane and endoplasmic reticulum calcium stores

This review discusses multiple ways in which the endoplasmic reticulum participates in and is influenced by signal transduction pathways. The endoplasmic reticulum provides a Ca2+ store that can be mobilized either by calcium-induced calcium release or by the diffusible messenger inositol 1,4,5-trisphosphate. Depletion of endoplasmic reticulum Ca2+ stores provides a signal that activates surface membrane Ca2+ channels, a process known as capacitative calcium entry. Depletion of endoplasmic reticulum stores can also signal long-term cellular responses such as gene expression and programmed cell death or apoptosis. In addition to serving as a source of cellular signals, the endoplasmic reticulum is also functionally and structurally modified by the Ca2+ and protein kinase C pathways. Elevated cytoplasmic Ca2+ causes a rearrangement and fragmentation of endoplasmic reticulum membranes. Protein kinase C activation reduces the storage capacity of the endoplasmic reticulum Ca2+ pool. In some cell types, protein kinase C inhibits capacitative calcium entry. Protein kinase C activation also protects the endoplasmic reticulum from the structural effects of high cytoplasmic Ca2+. The emerging view is one of a complex network of pathways through which the endoplasmic reticulum and the Ca2+ and protein kinase C signaling pathways interact at various levels regulating cellular structure and function.     

A single tryptophan residue of endomannosidase is crucial for Golgi localization and <Emphasis Type="Italic">in vivo</Emphasis> activity

Golgi-endomannosidase provides an alternate glucosidase-independent pathway of glucose trimming. Activity for endomannosidase is detectable in various tissues and cell lines but not in CHO cells. Cloning of CHO cell endomannosidase revealed that the highly conserved Trp188 and Arg177 of vertebrate endomannosidase were both substituted by Cys. The Trp188Cys substitution was functionally important since it alone resulted in endoplasmic reticulum (ER) mislocalization of endomannosidase and caused the greatly reduced in vivo activity. These effects could be reversed in cells with a back-engineered Cys188Trp CHO cell endomannosidase, in particular N-glycans of α1-antitrypsin became fully processed. The intramolecular disulfide bridge of CHO cell endomannosidase formed with the additional Cys188 was not solely responsible for the reduced enzyme activity since endomannosidase with engineered Cys188Ala or Ser substitutions did not restore enzyme activity and was ER mislocalized. Thus, the conserved Trp188 residue in endomannosidases is of critical importance for correct subcellular localization and in vivo activity of the enzyme. Received 7 May 2007; received after revision 31 May 2007; accepted 11 June 2007     

Effect of praseodymium on drug metabolism in rat liver smooth and rough endoplasmic reticulum

Summary A small i.v. dose (3 mg/kg) of a light lanthanon, praseodymium, impairs the drug metabolizing capacity of both the smooth and rough fractions of rat liver endoplasmic reticulum. This decrease in the activity of drug metabolizing enzymes and in the amount of cytochromes P-450 and b₅ is more pronounced in the rough endoplasmic reticulum fraction.     

Licht- und elektronenmikroskopische Befunde an den Geschmacksknospen der Axolotlzunge

Summary The investigation of the taste buds in the tongue of the neotene Mexican axolotl (Siredon mexicanum) by light and electron microscopy demonstrates 4 different cell types: 1) R-cells, marginal cells of less differentiated character. 2) G-cells, granulated cells in basal position. 3) Cells of type A with fibrills, vesicular elements, and dark bodies, showing supporting and secretory function. 4) Cells of type B with an agranular endoplasmic reticulum in stripe like arrangement, supposed to be receptor cells.     

Morphological differentiation of the growing oocyte of Ctenomys torquatus (Rodentia, Octodontidae)

The ultrastructural changes observed during the growth phase of oocytes of Ctenomys torquatus (Rodentia, Octodontidae) are reported. Interest was particularly centered on the transformation and/or distribution of the components of the endoplasmic reticulum. According to the observations made it is suggested that the endoplasmic reticulum stores some kind of material which may support early stages of development.     

Role of <Emphasis Type="Italic">N</Emphasis>-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation

Misfolded or incompletely assembled multisubunit glycoproteins undergo endoplasmic reticulum-associated degradation (ERAD) regulated in large measure by their N-linked polymannose oligosaccharides. In this quality control system lectin interaction with Glc₃Man₉GlcNAc₂ glycans after trimming with endoplasmic reticulum (ER) -glucosidases and -mannosidases sorts out persistently unfolded glycoproteins for N-deglycosylation and proteolytic degradation. Monoglucosylated (Glc₁Man₉GlcNAc₂) glycoproteins take part in the calnexin/calreticulin glucosylation-deglucosylation cycle, while the Man₈GlcNAc₂ isomer B product of ER mannosidase I interacts with EDEM. Proteasomal degradation requires retrotranslocation into the cytosol through a Sec61 channel and deglycosylation by peptide: N-glycosidase (PNGase); in alternate models both PNGase and proteasomes may be either free in the cytosol or ER membrane-imbedded/attached. Numerous proteins appear to undergo nonproteasomal degradation in which deglycosylation and proteolysis take place in the ER lumen. The released free oligosaccharides (OS) are transported to the cytosol as OS-GlcNAc₂ along with similar components produced by the hydrolytic action of the oligosaccharyltransferase, where they together with OS from the proteasomal pathway are trimmed to Man₅GlcNAc₁ by the action of cytosolic endo--N-acetylglucosaminidase and -mannosidase before entering the lysosomes. Some misfolded glycoproteins can recycle between the ER, intermediate and Golgi compartments, where they are further processed before ERAD. Moreover, properly folded glycoproteins with mannose-trimmed glycans can be deglucosylated in the Golgi by endomannosidase, thereby releasing calreticulin and permitting formation of complex OS. A number of regulatory controls have been described, including the glucosidase-glucosyltransferase shuttle, which controls the level of Glc₃Man₉GlcNAc₂-P-P-Dol, and the unfolded protein response, which enhances synthesis of components of the quality control system.Received 26 January 2004; accepted 25 February 2004     

Morphometrische Untersuchungen an der Rattenleber — Parenchymzelle nach Anwendung verschiedener Fixationspuffer

Summary The effect of 2 fixatives, (1) s-Collidin buffered OsO₄, (2) phosphate buffered OsO₄, on the liver cell was studied by morphometric analysis. After fixation with solution 2, large areas of smooth endoplasmic reticulum were covered by electron-opaque deposits of glycogen. No such masking was noticed by using solution 1. Other cell organelles showed no significant differences in their relative volumes. By using fixative solution 2, decrease in glycogen can simulate relative volume increase of the smooth endoplasmic reticulum.

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Wesentliche Teile der vorliegenden Arbeit wurden von Frl. F.Stockmann der Medizinischen Fakultät der Universität Basel als Inaugural-Dissertation vorgelegt.     

Réticulum endoplasmique et progression centripète du septum interconidien chez un mutant morphologique deNeurospora crassa

Summary Preceding the infolding of the cross wall separating pseudoconidial units in the aschizogenous, amyc mutant ofNeurospora crassa is the development of an electron-dense ring seen in section as 2 spots on opposite sides of the cell wall. Vesiculated elements of the endoplasmic reticulum are seen in close proximity to the centripetally progressing edge of the interconidial septum.

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Nous remercions le Fonds national de la Recherche scientifique de son appui.     

A metabolic scenario for the evolutionary origin of peroxisomes from the endomembranous system

A novel model for the evolutionary origin of peroxisomes and related organelles from within the endoplasmic reticulum is proposed.     

Colchicine-induced appearance (proliferation) of smooth sarcoplasmic reticulum in arterial smooth muscle cells

Summary Colchicine treatment resulted in the appearance and proliferation of smooth sarcoplasmic reticulum in some smooth muscle cells of the aortic and pulmonary trunk walls in the rabbit. The significance of cytoplasmic microtubules and/or membrane-bound tubulin for the morphogenesis, functioning and control of smooth endoplasmic reticulum in different kinds of cells is discussed.     

Functions of reticulons in plants: What we can learn from animals and yeasts

Reticulons (RTNs) are membrane-spanning proteins sharing a typical domain named reticulon homology domain (RHD). RTN genes have been identified in all eukaryotic organisms examined so far, and the corresponding proteins have been found predominantly associated to the endoplasmic reticulum membranes. In animal and yeast, in which knowledge of the protein family is more advanced, RTNs are involved in numerous cellular processes such as apoptosis, cell division and intracellular trafficking. Up to now, a little attention has been paid to their plant counterparts, i.e., RTNLBs. In this review, we summarize the data available for RTNLB proteins and, using the data obtained with animal and yeast models, several functions for RTNLBs in plant cells are proposed and discussed. Received 01 July 2008; received after revision 08 September 2008; accepted 30 September 2008     

Colchicine-induced appearance (proliferation) of smooth sarcoplasmic reticulum in arterial smooth muscle cells

Colchicine treatment resulted in the appearance and proliferation of smooth sarcoplasmic reticulum in some smooth muscle cells of the aortic and pulmonary trunk walls in the rabbit. The significance of cytoplasmic microtubules and/or membrane-bound tubulin for the morphogenesis, functioning and control of smooth endoplasmic reticulum in different kinds of cells is discussed.     

Plakorin,a potent Ca2+-ATPase activator from the Okinawan marine spongePlakortis sp.

Summary A new cyclic peroxide, plakorin, which is a potent sarcoplasmic reticulum (SR) Ca^a+-ATPase activator has been isolated from the Okinawan marine spongePlakortis sp., its structure was elucidated on the basis of spectral data.Acknowledgments. We thank Ms M. Hamashima and Ms A. Muroyama for their technical assistance.     

Similar paracrystals of endoplasmic reticulum in the photoemitters and the photoreceptors of scale-worms

Summary Paracrystals of tubular endoplasmic reticulum are the characteristic of the luminous cells in the elytra of polynoïd worms, and they are the sources of luminescence as well as of fluorescence. Structurally similar paracrystals are now found to be the main constituent of the lens in the eyes of all the Aphroditidae.     

Symbioramide,a novel Ca2+-ATPase activator from the cultured dinoflagellateSymbiodinium sp.

Summary A novel sphingosine derivative, symbioramide, has been isolated from the laboratory-cultured dinoflagellateSymbiodinium sp. as a sarcoplasmic reticulum (SR) Ca²⁺-ATPase activator, and its structure elucidated to be1 on the basis of spectral and chemical means.Acknowledgments. We thank Ms M. Hamashima and Ms A. Muroyama for their technical assistance.