Localisation des activités de la p-nitrophénylphosphatase et de la phosphatase alcaline dans les cellules de transfert du noeud cotylédonaire du pois nain

1983 ◽  
Vol 61 (5) ◽  
pp. 1476-1490
Author(s):  
A. Nougarède ◽  
P. Landré ◽  
J. Rembur
Keyword(s):  
Alkaline Phosphatase ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Cotyledonary Node ◽  
Ultrastructural Localization ◽  
Transfer Cells ◽  
The Other ◽  
Reaction Products ◽  
Weak Reaction ◽  
Phosphatase Alcaline

The ultrastructural localization of the K+-dependent nitrophenylphosphatase (NPPase) and alkaline phosphatase (ALPase) activities were determined in the transfer cells of the pea cotyledonary node. These two types of activities were generally associated and located essentially on the plasma membrane. NPPase and ALPase activities were also detected along the nuclear membrane of the xylem and phloem transfer cells and along the endoplasmic reticulum profiles (internal face) of phloem transfer cells. Mitochondrial NNPase activity was confined to the outer membrane and cristae. The partial inhibition of the NPPase reaction products by L-p-bromotetramisole and cysteine, the weak reaction observed after deletion of K+, and the suppression of the reaction in the presence of L-p-bromotetramisole are best explained by the concomitant activity of a K+-dependent NPPase and of an ALPase partially inhibited by K+. On the basis of sensitivity to inhibitors, two plasma membrane ALPase isoenzymes were detected. One, extramembranous, was bromotetramisole and cysteine insensitive but inhibited by L-phenylalanine; the other, intramembranous, was bromotetramisole and cysteine sensitive, but insensitive to L-phenylalanine. The other sites of ALPase activities were substantially inhibited by all treatments.

scholarly journals Compartmentalization of intracellular membrane glycocomponents is revealed by fracture-label.

1984 ◽  
Vol 98 (1) ◽  
pp. 29-34 ◽  
Author(s):  
M R Torrisi ◽  
P Pinto da Silva
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Binding Sites ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Secretory Granules ◽  
The Other ◽  
Rat Tissues ◽  
Intracellular Membrane ◽  
Definition Of

We used thin-section fracture-label to determine the distribution of wheat-germ agglutinin binding sites in intracellular membranes of secretory and nonsecretory rat tissues as well as in human leukocytes. In all cases, analysis of the distribution of wheat germ agglutinin led to the definition of two endomembrane compartments: one, characterized by absence of the label, includes the membranes of mitochondria and peroxisomes as well as those of the endoplasmic reticulum and nuclear envelope; the other, strongly labeled, comprises the membrane of lysosomes, phagocytic vacuoles, and secretory granules, as well as the plasma membrane. The Golgi apparatus was weakly labeled in all studied tissues.

scholarly journals Ultrastructural localization of alkaline phosphatase in rat eosinophil leucocytes.

1978 ◽  
Vol 26 (10) ◽  
pp. 862-864 ◽  
Author(s):  
D M Williams ◽  
J E Linder ◽  
M W Hill ◽  
R Gillett
Keyword(s):  
Alkaline Phosphatase ◽  
Plasma Membrane ◽  
Electron Microscope ◽  
Outer Surface ◽  
Human Neutrophil ◽  
Osmium Tetroxide ◽  
Diazonium Salt ◽  
Ultrastructural Localization ◽  
Microscope Examination ◽  
Membrane Location

The ultrastructural localization of alkaline phosphatase in eosinophil leucocytes, obtained from experimentally-induced peritoneal exudates in rats, has been studied using an osmiophilic technique with 2-naphthylthiolphosphoryl dichloride as substrate, fast Blue BBN as diazonium salt and postosmication with 1% aqueous osmium tetroxide. With this method identical incubation procedures could be used for both light and electron microscope examination. Eosinophils were the only cells which contained alkaline phosphatase. The enzyme was predominantly associated with the outer surface of the plasma membrane, being present in much lower concentrations in cytoplasmic cisternae. Eosinophil granules only rarely showed reaction product. The plasma membrane location of alkaline phosphatase in eosinophil leucocytes is identical to that recently demonstrated in the human neutrophil.

Des variations d'activités de la 5′-nucléotidase et de l’adénylate-cyclase sont-elles des composantes de la levée d'inhibition du bourgeon cotylédonaire du pois?

1985 ◽  
Vol 63 (2) ◽  
pp. 309-323 ◽  
Author(s):  
Arlette Nougarède ◽  
Pierre Landré ◽  
Jacques Rembur ◽  
Mercedes Niebla Hernandez
Keyword(s):  
Cell Cycle ◽  
Alkaline Phosphatase ◽  
Plasma Membrane ◽  
Adenylate Cyclase ◽  
Sodium Fluoride ◽  
Shoot Apex ◽  
Cotyledonary Node ◽  
Ultrastructural Level ◽  
Meristematic Cells ◽  
Plant Enzyme

Adenylate cyclase and 5′-nucleotidase activities were localized at the ultrastructural level. Variations of these activities were checked in the transfer cells of the cotyledonary node in the intact or decapitated plant. They were also studied in the shoot apex of both inhibited (G0 state) and released cotyledonary buds, during the transitions G1–S orG2–M. The adenylate cyclase activity is mainly associated with the exterior side of the plasma membrane and it is identical in both specialized and meristematic cells, no matter what the phase of the cell cycle is. Sodium fluoride did not appear as an activator of the plant enzyme adenylate cyclase. The 5′-nuelcotidase activity was predominant on the outside of the plasma membrane and in the plasmodesmata with no variation of intensity in the meristematic cells of the bud in relation to the cell cycle phases. Use of inhibitors of alkaline phosphatase (L-p-bromotetramisole and L-phenylalanine) and 5′-nucleotidase activities (α-β-methylene adenosine 5′-diphosphate) demonstrated the specificity of the reaction along the plasma membrane. The constancy of adenylate cyclase and 5′-nucleotidase activities in both inhibited and released buds suggests that if the optimization of the pool of polynucleotides is a component of the release from inhibition in the cotyledonary bud of pea, it is not due to the variation of activities of enzymes which release adenosine from ATP.

Freeze-Fracture Replication of Rough Endoplasmic Reticulum of Mouse Liver Cells

1972 ◽  
Vol 11 (2) ◽  
pp. 477-489
Author(s):  
A. S. BREATHNACH ◽  
C. STOLINSKI ◽  
M. GROSS
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Rough Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Mouse Liver ◽  
Freeze Fracture ◽  
The Other ◽  
Fracture Face ◽  
Mitochondrial Membranes ◽  
En Face

Fresh, chemically unfixed, glycerinated specimens of mouse liver were examined by the technique of freeze-fracture replication without sublimation (i.e. they were not ‘etched’). Where extensive areas of fractured lamellar membranes of the rough endoplasmic reticulum are revealed en face, 2 types of fracture face are distinguishable. One of these fracture faces (A) is directed towards the cytoplasm, and the other (B) towards the cisternal cavity. A characteristic mosaic, or patchwork pattern of flat areas circumscribed by particles, is evident on both faces, and more clearly so on face B, due to a greater number of more prominent particles. Similar mosaic patterns are revealed on convex faces of the nuclear membrane, and on concave fracture faces of mitochondrial membranes, but are not evident on fracture faces of the plasma membrane. Uncertainty in establishing the exact plane of fracture of membranes in this material, since glycerol is virtually non-sublimable, makes it difficult to assess the significance of these mosaic patterns. The fact that ribosomes are not identifiable on either face of fractured endoplasmic reticulum membranes, gives no certain indication of the plane of fracture.

scholarly journals UNE FORME MICROTUBULAIRE ET PARACRISTALLINE DE RETICULUM ENDOPLASMIQUE DANS LES PHOTOCYTES DES ANNELIDES POLYNOINÆ

1966 ◽  
Vol 31 (1) ◽  
pp. 135-158 ◽  
Author(s):  
J. M. Bassot
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Fine Structure ◽  
Nuclear Envelope ◽  
Contact Surface ◽  
Special Kind ◽  
The Other ◽  
Cytoplasmic Organelle ◽  
Specialized Form

Luminous cells of polynoid worm elytra have been examined by methods of electron microscopy, with special attention focused on the fine structure of photogenic grains. These cells send apical prolongations into the mid-part of the elytra. The plasma membrane is very sinuous, and a special kind of desmosome links two portions of the same membrane. In addition to all the organelles which can be found in nonluminescent epithelial cells of the elytra, numerous photogenic grains are contained in their cytoplasm. These grains are composed of undulating microtubules measuring 200 A in diameter; their disposition in the grain is highly regular, and the grains appear as paracrystals. At the borders of the grains, the walls of the microtubules are often in continuity with those of the endoplasmic reticulum and with the external membrane of the nuclear envelope. Because of this fact, the microtubules of the grains may be considered a cytoplasmic organelle, representing a specialized form of the endoplasmic reticulum. The microtubules permit the repartition, inside and outside their walls, of two different products, one being forty-three times more abundant than the other; thus, the contact surface, in comparison to the volume, is greatly increased. The induction of the luminous reaction by change in the permeability of the microtubule walls, allowing contact between the two substances, is suggested as a working hypothesis. There is an evolution of the grains along the axis of the photocytes. The grains are often surrounded by progressively increasing amounts of glycogen. Their paracrystalline disposition is altered at the apex of the luminous cells.

scholarly journals An Association between Mitochondria and the Endoplasmic Reticulum in Cells of the Pseudobranch Gland of a Teleost

1959 ◽  
Vol 5 (3) ◽  
pp. 393-396 ◽  
Author(s):  
D. E. Copeland ◽  
A. J. Dalton
Keyword(s):  
Endothelial Cells ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Carbonic Anhydrase ◽  
Basement Membrane ◽  
The Other ◽  
Secretory Cells ◽  
Specific Cell ◽  
Primary Products ◽  
In Cells

An elaborate and apparently unique specialization of the endoplasmic reticulum having the form of tubules and a precise orientation with respect to the mitochondria has been described for the specific cell of the pseudobranch gland. The tubules also are concentrated near the vascular border of the cell where they show continuity with the plasma membrane and open directly against the basement membrane. On the other side of the basement membrane, the endothelial cells of the sinusoid show openings or discontinuities characteristically associated with secretory cells. The pseudobranch gland is presumed to have carbonic anhydrase as one of its primary products, if not its only one, and the elaborate ultrastructure is thought to be associated with the special problems of secreting this enzyme.

scholarly journals Immunocytochemical demonstration of intracytoplasmic alkaline phosphatase in HeLa TCRC-1 cells.

1981 ◽  
Vol 29 (9) ◽  
pp. 1080-1087 ◽  
Author(s):  
S Tokumitsu ◽  
K Tokumitsu ◽  
W H Fishman
Keyword(s):  
Alkaline Phosphatase ◽  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Cell Surface ◽  
Distribution Patterns ◽  
Ultrastructural Localization ◽  
Surface Plasma ◽  
Membrane Glycoproteins ◽  
Perinuclear Space ◽  
Ectopic Gene Expression

The ultrastructural localization of alkaline phosphatase has been examined in cells of a HeLa subline (TCRC-1) that are monophenotypic for Regan isoenzyme expression. Enzyme activity was demonstrated at the cell surface plasma membrane and in certain lysosomes as revealed by the lead citrate method. The regular direct immunoperoxidase procedure utilizing antibodies in IgG or Fab' form showed the same distribution patterns of alkaline phosphatase. However, when the cell surface antigen was blocked in advance with specific unlabeled antibodies and direct immunocytochemistry performed in the presence of saponin, intracellular alkaline phosphatase antigen was observed in the perinuclear space, endoplasmic reticulum, and Golgi apparatus. The results appeared to be concordant with the current concept that membrane glycoproteins are formed in the endoplasmic reticulum, modified in the Golgi apparatus and then transported to the cell surface. Intracellular alkaline phosphatase was observed predominantly in some cell populations especially mitotic cells, suggesting that the enzyme protein was synthesized in and around the mitotic phase. Accordingly, this technique of differential membrane immunocytochemistry appears to provide an opportunity to follow ectopic gene expression as a function of cell cycle and enzyme induction.

scholarly journals Ultrastructural localization of adenylate cyclase in chicken bone cells.

1989 ◽  
Vol 37 (11) ◽  
pp. 1705-1709 ◽  
Author(s):  
T Yamamoto ◽  
C V Gay
Keyword(s):  
Plasma Membrane ◽  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Bone Cells ◽  
Ultrastructural Localization ◽  
Product Distribution ◽  
The Other ◽  
Long Bone ◽  
Chicken Bone ◽  
Regulatory Systems

We investigated adenylate cyclase distribution in 6-day-and 3-week-old calvariae and in 6-day-old long bone metaphyses from chickens. Reaction product distribution was on the plasma membrane of osteoblasts, pre-osteoblasts, and forming osteocytes which contacted one another. Osteoclasts and mature osteocytes lacked reaction product. Six-day calvariae reacted less intensely than the other two tissues. In controls, reaction product was markedly diminished or eliminated by removal of forskolin or substrates, or by addition of the inhibitor 2',5'-dideoxyadenosine. The results indicate the importance of cyclic AMP in osteoblast regulation. Osteocytes and osteoclasts may involve alternate mechanisms as major regulatory systems.

Activités ATPasiques du nœud cotylédonaire et du bourgeon cotylédonaire du pois inhibé, réactivé ou soumis à la fusicoccine

1983 ◽  
Vol 61 (1) ◽  
pp. 119-134 ◽  
Author(s):  
Arlette Nougarède ◽  
Pierre Landré ◽  
Jacques Rembur
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Outer Surface ◽  
Cotyledonary Node ◽  
Transfer Cells ◽  
Intact Plant ◽  
High Concentration ◽  
Sieve Elements ◽  
Cell Specificity ◽  
Activity Of Enzymes

The activity of enzymes which hydrolyse ATP at neutral pH was demonstrated cytochemically in the cotyledonary node and in three types of cotyledonary buds (inhibited, released from dominance, treated with fusicoccin). In the intact plant, the transfer cells of the cotyledonary node showed a very strong Mg2+-dependent, ouabaïne-insensitive ATPase activity, essentially located on the outer surface of the plasmalemma. A high concentration of K+ stimulated the ATPase activity of the plasmalemma of transfer cells and sieve elements. ATPase activity was even more specifically detected along mitochondrial cristae and the tonoplast of the phloem transfer cells and along the reticular membranes of the xylem transfer cells. All these activities which were not modified by decapitation increased after a fusicoccin treatment. In the inhibited bud the same pattern of ATPase activity occurred along the plasma membrane but with a lesser intensity. At the base of the first-bud internodes the phloem transfer cells were the only ones with a high ATPase activity. Decapitation induced, without cell specificity, an increase in the ATPase activity of the plasmalemma for the entire bud, while after fusicoccin treatment, the increase extended to the tonoplast. Proper controls eliminate the possibility of artifactual reactions or interactions with other enzymes.

Two different mutants blocked in synthesis of dolichol-phosphoryl-mannose do not add glycophospholipid anchors to membrane proteins: quantitative correction of the phenotype of a CHO cell mutant with tunicamycin

1991 ◽  
Vol 11 (1) ◽  
pp. 391-400
Author(s):  
N Singh ◽  
A M Tartakoff
Keyword(s):  
Alkaline Phosphatase ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Membrane Proteins ◽  
Rough Endoplasmic Reticulum ◽  
Essential Role ◽  
Placental Alkaline Phosphatase ◽  
Cho Cell ◽  
Cell Mutant

The addition of glycophospholipid (GPL) anchors to certain membrane proteins occurs in the rough endoplasmic reticulum and is essential for transport of the proteins to the plasma membrane. Limited circumstantial evidence suggests that dolichol-phosphoryl-mannose (DPM) is a donor of mannose residues of these anchors. We here report studies of a CHO cell mutant (B421) transfected to express the GPL-anchored protein, placental alkaline phosphatase (AP). Only a few transfectants were found to express GPL-anchored AP on their surface, and these clones synthesized DPM. Moreover, and most strikingly, when surface AP-negative transfectants were treated with tunicamycin to cause accumulation of DPM, these cells expressed lipid-anchored AP. Fusion of a cloned surface AP-negative transfectant of B421 with the Thy-1-class E mutant thymoma, which is also deficient in DPM synthesis, produced hybrids that synthesized DPM and expressed AP and Thy-1. Thus, two mutations can interrupt DPM synthesis, and three sets of observations point to an essential role of DPM for addition of GPL anchors.

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