Fusion images and intramembrane particle aggregates during the action of antidiuretic hormone

1985 ◽  
Vol 240 (2) ◽  
Author(s):  
RichardM. Hays ◽  
Jacques Chevalier ◽  
Ren�e Gobin ◽  
Jacques Bourguet
Keyword(s):  
Antidiuretic Hormone ◽  
Intramembrane Particle ◽  
Particle Aggregates ◽  
Fusion Images

scholarly journals Role of osmotic forces in exocytosis: studies of ADH-induced fusion in toad urinary bladder.

1981 ◽  
Vol 91 (2) ◽  
pp. 584-588 ◽  
Author(s):  
W A Kachadorian ◽  
J Muller ◽  
A Finkelstein
Keyword(s):  
Plasma Membrane ◽  
Urinary Bladder ◽  
Antidiuretic Hormone ◽  
Basic Mechanism ◽  
Toad Urinary Bladder ◽  
Bathing Medium ◽  
Intramembrane Particle ◽  
Luminal Membrane ◽  
Particle Aggregates

Antidiuretic hormone (ADH) treatment of toad urinary bladder activates an exocytotic-like process by which intramembrane particle aggregates are transferred from membranes of elongated cytoplasmic tubules to the luminal-facing plasma membrane. We find that the number of these ADH-induced fusion events, and the number of aggregates appearing in the luminal membrane, are reduced when the luminal bathing medium is made hyperosmotic. As an apparent consequence of the inhibition of their fusion with the luminal membrane, the elongated cytoplasmic tubules become enormously swollen into large, rounded vesicles. These results are consistent with the view that osmotic forces are essential to the basic mechanism of exocytosis.

scholarly journals Appearance and distribution of surface proteins of the human erythrocyte membrane. An electron microscope and immunochemical labeling study.

1978 ◽  
Vol 76 (2) ◽  
pp. 512-531 ◽  
Author(s):  
D Shotton ◽  
K Thompson ◽  
L Wofsy ◽  
D Branton
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Indirect Evidence ◽  
Surface Proteins ◽  
Human Erythrocyte Membrane ◽  
Intramembrane Particle ◽  
Translational Movement ◽  
Cytoplasmic Surface ◽  
Particle Aggregates ◽  
Before And After

We have used freeze-etching, before and after immunoferritin labeling, to visualize spectrin molecules and other surface proteins of the human erythrocyte membrane. After intramembrane particle aggregation was induced, spectrin molecules, identified by labeling with ferritin-conjugated antispectrin, were clustered on the cytoplasmic surface of the membrane in patches directly underlying the particle clusters. This labeling pattern confirms the involvement of spectrin in such particle aggregates, as previously inferred from indirect evidence. Ferritin-conjugated antihapten molecules, directed against external and cytoplasmic surface proteins of the erythrocyte membrane which had been covalently labeled nonspecifically with the hapten p-diazoniumphenyl-beta-D-lactoside, were similarly found in direct association with such intramembrane particle aggregates. This indicates that when spectrin and the intramembrane particles are aggregated, all the major proteins of the erythrocyte membrane are constrained to coaggregate with them. Although giving no direct information concerning the freedom of translational movement of proteins in the unperturbed erythrocyte membrane, these experiments suggest that a close dynamic association may exist between the integral and peripheral protein components of the membrane, such that immobilization of one component can restrict the lateral mobility of others.

Antidiuretic hormone moves membranes

1988 ◽  
Vol 255 (3) ◽  
pp. F375-F382 ◽  
Author(s):  
J. S. Handler
Keyword(s):  
Plasma Membrane ◽  
Antidiuretic Hormone ◽  
Water Permeability ◽  
Apical Membrane ◽  
Collecting Duct ◽  
Toad Bladder ◽  
Cell Swelling ◽  
Apical Plasma Membrane ◽  
Principal Cells ◽  
Particle Aggregates

This review focuses on events at the apical plasma membrane of toad urinary bladder and mammalian collecting duct as their permeability to water changes in response to antidiuretic hormone (ADH) and to its withdrawal. The major marker of the permeability change is observed in freeze-fracture electron microscopy of the apical plasma membrane and consists of a dramatic increase in membrane particle aggregates and, in toad bladder but not in collecting duct, in fused vesicles (aggrephores) that contain particle aggregates in their limiting membranes. Withdrawal of ADH is accompanied by endocytosis at the apical membrane, reflecting retrieval of water-permeable, particle aggregate-containing membrane. Covalent labeling of the external surface of the apical membrane of toad bladder identifies specific proteins that are present in the apical membrane only during the response to ADH. Proteins of the same molecular weights are also present in the retrieved membrane when ADH is withdrawn. Several controversial areas are considered, including the extent of cell swelling as water flows across the epithelium from dilute apical solution to isotonic basal solution, whether only principal cells or principal cells and intercalated cells participate in the water permeability response of the collecting duct, the role of the cytoskeleton in the water permeability response, and the proposed second water permeability barrier that is affected by ADH, but not by adenosine 3',5'-cyclic monophosphate.

scholarly journals Retention of antidiuretic hormone-induced particle aggregates by luminal membranes separated from toad bladder epithelial cells.

1982 ◽  
Vol 92 (1) ◽  
pp. 237-241 ◽  
Author(s):  
R M Hays ◽  
J Bourguet ◽  
B H Satir ◽  
N Franki ◽  
J Rapoport
Keyword(s):  
Antidiuretic Hormone ◽  
Intact Cell ◽  
Collecting Duct ◽  
Freeze Fracture ◽  
High Yield ◽  
Starting Point ◽  
Particle Aggregates ◽  
Fracture Study ◽  
Bladder Cells ◽  
Membrane Components

Aggregates of intramembrane particles appear in the luminal membranes of renal collecting duct and amphibian bladder cells after stimulation by antidiuretic hormone (ADH). We undertook this freeze-fracture study to determine whether particle aggregates, once in place, remain in the luminal membrane of the amphibian bladder after the membrane is physically separated from the rest of the cell. We found that the aggregates do remain in high yield in isolated membranes stabilized with a bifunctional imidoester (DTBP) followed by fixation with glutaraldehyde, or unfixed but stabilized with DTBP. These findings support the view that the particles are intrinsic membrane components and that their organization in the form of aggregates does not depend on the presence of the intact cell. In addition, the availability of isolated membranes containing particle aggregates provides a starting point for the isolation of the water-conducting proteins.

scholarly journals Evidence that ADH-stimulated intramembrane particle aggregates are transferred from cytoplasmic to luminal membranes in toad bladder epithelial cells.

1980 ◽  
Vol 85 (1) ◽  
pp. 83-95 ◽  
Author(s):  
J Muller ◽  
W A Kachadorian ◽  
V A DiScala
Keyword(s):  
Urinary Bladder ◽  
Freeze Fracture ◽  
Toad Urinary Bladder ◽  
Granular Cells ◽  
Thin Sections ◽  
Intramembrane Particle ◽  
Luminal Membrane ◽  
Particle Aggregates ◽  
Cytoplasmic Structures ◽  
Induced Changes

In freeze-fracture (FF) preparations of ADH-stimulated toad urinary bladder, characteristic intramembrane particle (IMP) aggregates are seen on the protoplasmic (P) face of the luminal membrane of granular cells while complementary parallel grooves are found on the exoplasmic (E) face. These IMP aggregates specifically correlate with ADH-induced changes in water permeability. Tubular cytoplasmic structures whose membranes contain IMP aggregates which look identical to the IMP aggregates in the luminal membrane have also been described in granular cells from unstimulated and ADH-stimulated bladders. The diameter of these cytoplasmic structures (0.11 +/- 0.004 micrometers) corresponds to that of tubular invaginations of the luminal membrane seen in thin sections of ADH-treated bladders (0.13 +/- 0.005 micrometers). Continuity between the membranes of these cytoplasmic structures (which are not granules) and the luminal membrane has been directly observed in favorable cross-fractures. In FF preparations of the luminal membrane, these apparent fusion events are seen as round, ice-filled invaginations (0.13 +/- 0.01 micrometer Diam), of which about half have the characteristic ADH-associated aggregates near the point of membrane fusion. They are less numerous than, but linearly related to, the number of aggregates counted in the same preparations (n = 78, r = 0.71, P less than 0.01). These observations suggest that the IMP aggregates seen in luminal membrane after ADH stimulation are transferred preformed by fusion of cytoplasmic with luminal membrane.

Effects of cellular acidification on ADH-induced intramembrane particle aggregates

1984 ◽  
Vol 246 (1) ◽  
pp. C157-C159 ◽  
Author(s):  
M. Parisi ◽  
J. Bourguet
Keyword(s):  
Membrane Surface ◽  
Water Flux ◽  
Medium Ph ◽  
Intramembranous Particle ◽  
Intramembrane Particle ◽  
Cyclic Monophosphate ◽  
Particle Aggregates ◽  
Camp Levels ◽  
Cellular Acidification ◽  
Intramembranous Particle Aggregates

8-Bromoadenosine 3',5'-cyclic monophosphate [an analogue of adenosine 3',5'-cyclic monophosphate (cAMP), the intracellular mediator for antidiuretic hormone (ADH) action] induces, in frog urinary bladder, an increase in water permeability that is rapidly and reversibly inhibited by cellular acidification. The effect of CO2 bubbling on the simultaneously observed intramembranous particle aggregates, which probably represent water channels, depended on the time that elapsed after changing medium pH: 3 min of CO2 bubbling depressed the water flux by 70%, whereas the membrane surface occupied by the aggregates remained unchanged. On the contrary, after 9-15 min of CO2 bubbling, both the water flux and the surface area occupied by the aggregates were strongly reduced. These results can be interpreted by accepting two post-cAMP levels of action for cellular acidification: 1) the channels themselves that, as previously suggested by ADH experiments at low temperature, would shift their structure from an "open" to a "closed" state, and 2) the mechanism that controlled the aggregates' plug in and removal.

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