Ontogénie des laticifères du système primaire de l’Hevea brasiliensis: une étude ultrastructurale et cytochimique

1981 ◽  
Vol 59 (6) ◽  
pp. 974-985 ◽  
Author(s):  
Charles Hébant
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Surface Film ◽  
Secretory Cells ◽  
Primary System ◽  
Parenchyma Cells ◽  
Rubber Particles ◽  
Specialized Form ◽  
Hydrolysis Of

The development of the laticifers of the primary system in the roots of young seedlings of Hevea is investigated. The nucleus of the maturing secretory cells progressively diminishes in size, thus giving rise to a dense "pycnotic" body. Plastids of primary laticifers show an organization intermediate between that of plastids of neighbouring parenchyma cells and that of the Frey-Wyssling complexes of the secondary laticifers. The continuity of the vacuome sensu lato is underlined. The lutoids, a specialized form of "polydisperse vacuome," show a relationship with the endoplasmic reticulum; these lutoïds can also incorporate rubber particles. The ontogeny of cell wall perforations is described; a progressive hydrolysis of the wall results in its gradual thinning followed by its disruption. Rubber particles are initiated as discrete inclusions within the protoplasm. A thin surface film is identifiable on them, the staining properties of which change during the maturation of the particles. The protoplasm of adult laticifers is densely packed with rubber particles.

Certain aspects of xylem differentiation in corn

1972 ◽  
Vol 50 (9) ◽  
pp. 1795-1804 ◽  
Author(s):  
L. M. Srivastava ◽  
A. P. Singh
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Wall Thickening ◽  
Xylem Differentiation ◽  
Cytoplasmic Protein ◽  
Wall Deposition ◽  
Vessel Elements ◽  
Parenchyma Cells ◽  
Vacuolar Membranes

Differentiation of vessel elements in corn is accompanied by marked changes in nearly all organelles except plastids. The young cells increase in volume and apparently synthesize new cytoplasmic protein. The initiation of wall thickening is accompanied by an aggregation of microtubules in specific locations and an increase in the number of mitochondria and dictyosomes. During the period of active wall deposition, the endoplasmic reticulum (ER) shows a highly elaborate form, harbors intralamellar tubules, and nearly blankets those parts of the wall which remain unthickened. Dictyosomes seem to produce at least two types of vesicles, one of which may serve as a carrier of lignin precursors. The final autolysis involves a progressive removal of vacuolar membranes, plastids, dictyosomes, vesicles associated with secretion of noncellulosic polysaccharides, microtubules, and finally plasmalemma, parts of cell wall, and cytoplasm. Mitochondria and ribosomes are degenerated. The ER probably plays an important role in this autolysis. The parenchyma cells associated with vessel elements are rich in mitochondria.

Nectary structure and nectar presentation in the Mediterranean geophyte, Urginea maritima (Hyacinthaceae)

Botany ◽  
2008 ◽  
Vol 86 (10) ◽  
pp. 1194-1204 ◽  
Author(s):  
Sharaf Al-Tardeh ◽  
Thomas Sawidis ◽  
Barbara-Evelin Diannelidis ◽  
Stylianos Delivopoulos
Keyword(s):  
Intermediate Stage ◽  
Secretory Cells ◽  
Urginea Maritima ◽  
Floral Nectary ◽  
Hydrolysis Process ◽  
Septal Nectary ◽  
Parenchyma Cells ◽  
Subsidiary Cells ◽  
Hydrolysis Of ◽  
Anatomy And Ultrastructure

The morphology, anatomy, and ultrastructure of the floral nectary of Urginea maritima (L.) Baker were investigated at three stages of nectary development. The plant possesses a typical gynopleural (septal) nectary with secondary presentation. The nectary consists of one layer of epithelium secretory cells and one to four layers of subsidiary cells subtended by two to six layers of parenchyma (subnectary) cells. The nectary releases the nectar at a point two-thirds towards the summit of the ovary by means of carpellary sutures. Nectar secretion appears to depend largely on the hydrolysis of starch grains stored in amyloplasts at the intermediate stage. The hydrolysis process most likely commences in the epithelium layer followed by the subsidiary tissue and then the parenchyma cells of the ovary wall. A symplastic transfer of the secreted nectar occurs by plasmodesmata connecting the subsidiary cells to the parenchyma and the epithelial secretory cells. However, microchannels in the cell wall of the epithelial cells may facilitate the apoplastic transfer of the nectar into the nectary cavity. The old stage of nectary development is characterized by a crystallized form of nectar, collapse of the parenchyma cells, complete starch hydrolysis, and disappearance of the amyloplasts and endoplasmic reticulum.

Analysis of the Anterior Secretory Cells of Onchidohs Muricata (Nudibranchia)

1981 ◽  
Vol 39 ◽  
pp. 614-615
Author(s):  
Roy Skidmore
Keyword(s):  
Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Golgi Body ◽  
The Body ◽  
Secretory Cells ◽  
Secretory Vesicles ◽  
High Magnification ◽  
Large Numbers ◽  
Membrane Bound ◽  
Sole Of The Foot

The long-necked secretory cells in Onchidoris muricata are distributed in the anterior sole of the foot. These cells are interspersed among ciliated columnar and conical cells as well as short-necked secretory gland cells. The long-necked cells contribute a significant amount of mucoid materials to the slime on which the nudibranch travels. The body of these cells is found in the subepidermal tissues. A long process extends across the basal lamina and in between cells of the epidermis to the surface of the foot. The secretory granules travel along the process and their contents are expelled by exocytosis at the foot surface.The contents of the cell body include the nucleus, some endoplasmic reticulum, and an extensive Golgi body with large numbers of secretory vesicles (Fig. 1). The secretory vesicles are membrane bound and contain a fibrillar matrix. At high magnification the similarity of the contents in the Golgi saccules and the secretory vesicles becomes apparent (Fig. 2).

scholarly journals Characterization of Glycoside Hydrolase Family 5 Proteins in Schizosaccharomyces pombe

2010 ◽  
Vol 9 (11) ◽  
pp. 1650-1660 ◽  
Author(s):  
Encarnación Dueñas-Santero ◽  
Ana Belén Martín-Cuadrado ◽  
Thierry Fontaine ◽  
Jean-Paul Latgé ◽  
Francisco del Rey ◽  
...  
Keyword(s):  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Protein Characterization ◽  
Wall Material ◽  
Glycoside Hydrolase Family ◽  
Content Type ◽  
Hydrolysis Of ◽  
Controlled Hydrolysis ◽  
Hydrolase Family

ABSTRACT In yeast, enzymes with β-glucanase activity are thought to be necessary in morphogenetic events that require controlled hydrolysis of the cell wall. Comparison of the sequence of the Saccharomyces cerevisiae exo-β(1,3)-glucanase Exg1 with the Schizosaccharomyces pombe genome allowed the identification of three genes that were named exg1 + (locus SPBC1105.05), exg2 + (SPAC12B10.11), and exg3 + (SPBC2D10.05). The three proteins have different localizations: Exg1 is secreted to the periplasmic space, Exg2 is a membrane protein, and Exg3 is a cytoplasmic protein. Characterization of the biochemical activity of the proteins indicated that Exg1 and Exg3 are active only against β(1,6)-glucans while no activity was detected for Exg2. Interestingly, Exg1 cleaves the glucans with an endohydrolytic mode of action. exg1 + showed periodic expression during the cell cycle, with a maximum coinciding with the septation process, and its expression was dependent on the transcription factor Sep1. The Exg1 protein localizes to the septum region in a pattern that was different from that of the endo-β(1,3)-glucanase Eng1. Overexpression of Exg2 resulted in an increase in cell wall material at the poles and in the septum, but the putative catalytic activity of the protein was not required for this effect.

scholarly journals Optimization of a minimal synergistic enzyme system for hydrolysis of raw cassava pulp

RSC Advances ◽  
2017 ◽  
Vol 7 (76) ◽  
pp. 48444-48453 ◽  
Author(s):  
Benjarat Bunterngsook ◽  
Thanaporn Laothanachareon ◽  
Suda Natrchalayuth ◽  
Sirithorn Lertphanich ◽  
Tatsuya Fujii ◽  
...  
Keyword(s):  
Cell Wall ◽  
Enzyme System ◽  
Starch Granules ◽  
Cell Wall Polysaccharides ◽  
Cassava Pulp ◽  
Lignocellulosic Wastes ◽  
Hydrolysis Of

Cassava pulp is an underused agricultural by-product comprising residual starch granules entrapped in cell wall polysaccharides, making it unique from other lignocellulosic wastes in terms of enzymatic processing.

scholarly journals Resynthesis of phosphatidylinositol in permeabilized neutrophils following phospholipase Cβ activation: transport of the intermediate, phosphatidic acid, from the plasma membrane to the endoplasmic reticulum for phosphatidylinositol resynthesis is not dependent on soluble lipid carriers or vesicular transport

1999 ◽  
Vol 341 (2) ◽  
pp. 435-444 ◽  
Author(s):  
Jacqueline WHATMORE ◽  
Claudia WIEDEMANN ◽  
Pennti SOMERHARJU ◽  
Philip SWIGART ◽  
Shamshad COCKCROFT
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Vesicular Transport ◽  
Human Neutrophils ◽  
Permeabilized Cells ◽  
Transfer Protein ◽  
Membrane Contact ◽  
Phosphatidylinositol Transfer ◽  
Pi Hydrolysis ◽  
Hydrolysis Of

Receptor-mediated phospholipase C (PLC) hydrolysis of phosphoinositides is accompanied by the resynthesis of phosphatidylinositol (PI). Hydrolysis of phosphoinositides occurs at the plasma membrane, and the resulting diacylglycerol (DG) is converted into phosphatidate (PA). Two enzymes located at the endoplasmic reticulum (ER) function sequentially to convert PA back into PI. We have established an assay whereby the resynthesis of PI could be followed in permeabilized cells. In the presence of [γ-32P]ATP, DG generated by PLC activation accumulates label when converted into PA. The 32P-labelled PA is subsequently converted into labelled PI. The formation of labelled PI reports the arrival of labelled PA from the plasma membrane to the ER. Cytosol-depleted, permeabilized human neutrophils are capable of PI resynthesis following stimulation of PLCβ (in the presence of phosphatidylinositol-transfer protein), provided that CTP and inositol are also present. We also found that wortmannin, an inhibitor of endocytosis, or cooling the cells to 15 °C did not stop PI resynthesis. We conclude that PI resynthesis is dependent neither on vesicular transport mechanisms nor on freely diffusible, soluble transport proteins. Phosphatidylcholine-derived PA generated by the ADP-ribosylation-factor-stimulated phospholipase D pathway was found to accumulate label, reflecting the rapid cycling of PA to DG, and back. This labelled PA was not converted into PI. We conclude that PA derived from the PLC pathway is selected for PI resynthesis, and its transfer to the ER could be membrane-protein-mediated at sites of close membrane contact.

scholarly journals The Endoplasmic Reticulum and the Golgi Structures in Maize Root Cells

1959 ◽  
Vol 5 (3) ◽  
pp. 501-506 ◽  
Author(s):  
W. Gordon Whaley ◽  
Hilton H. Mollenhauer ◽  
Joyce E. Kephart
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Electron Microscope ◽  
Nuclear Envelope ◽  
Epoxy Resin ◽  
Maize Root ◽  
Root Tips ◽  
Animal Cells ◽  
Root Cells ◽  
Vesicular Structure

Maize root tips were fixed in potassium permanganate, embedded in epoxy resin, sectioned to show silver interference color, and studied with the electron microscope. All the cells were seen to contain an endoplasmic reticulum and apparently independent Golgi structures. The endoplasmic reticulum is demonstrated as a membrane-bounded, vesicular structure comparable in many aspects to that of several types of animal cells. With the treatment used here the membranes appear smooth surfaced. The endoplasmic reticulum is continuous with the nuclear envelope and, by contact at least, with structures passing through the cell wall. The nuclear envelope is characterized by discontinuities, as previously reported for animal cells. The reticula of adjacent cells seem to be in contact at or through the plasmodesmata. Because of these contacts the endoplasmic reticulum of a given cell appears to be part of an intercellular system. The Golgi structures appear as stacks of platelet-vesicles which apparently may, under certain conditions, produce small vesicles around their edges. Their form changes markedly with development of the cell.

scholarly journals Pectin methylesterase, metal ions and plant cell-wall extension. Hydrolysis of pectin by plant cell-wall pectin methylesterase

1991 ◽  
Vol 279 (2) ◽  
pp. 343-350 ◽  
Author(s):  
J Nari ◽  
G Noat ◽  
J Ricard
Keyword(s):  
Cell Wall ◽  
Metal Ions ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Direct Interaction ◽  
Enzyme Reaction ◽  
Pectin Methylesterase ◽  
High Concentrations ◽  
Enzyme Molecules ◽  
Hydrolysis Of

The hydrolysis of p-nitrophenyl acetate catalysed by pectin methylesterase is competitively inhibited by pectin and does not require metal ions to occur. The results suggest that the activastion by metal ions may be explained by assuming that they interact with the substrate rather than with the enzyme. With pectin used as substrate, metal ions are required in order to allow the hydrolysis to occur in the presence of pectin methylesterase. This is explained by the existence of ‘blocks’ of carboxy groups on pectin that may trap enzyme molecules and thus prevent the enzyme reaction occurring. Metal ions may interact with these negatively charged groups, thus allowing the enzyme to interact with the ester bonds to be cleaved. At high concentrations, however, metal ions inhibit the enzyme reaction. This is again understandable on the basis of the view that some carboxy groups must be adjacent to the ester bond to be cleaved in order to allow the reaction to proceed. Indeed, if these groups are blocked by metal ions, the enzyme reaction cannot occur, and this is the reason for the apparent inhibition of the reaction by high concentrations of metal ions. Methylene Blue, which may be bound to pectin, may replace metal ions in the ‘activation’ and ‘inhibition’ of the enzyme reaction. A kinetic model based on these results has been proposed and fits the kinetic data very well. All the available results favour the view that metal ions do not affect the reaction through a direct interaction with enzyme, but rather with pectin.

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