scholarly journals Interaction of antimycin with cytochrome b -561: A study in secretory granules and in plasma membrane isolated from chromaffin cells of bovine adrenal medulla (1983) FEBS Letters 160, 153-158

FEBS Letters ◽  
1983 ◽  
Vol 163 (1) ◽  
pp. 153-153
Keyword(s):  
Plasma Membrane ◽  
Cytochrome B ◽  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Secretory Granules ◽  
Bovine Adrenal Medulla

Plasma membrane and vesicular glutamate transporter expression in chromaffin cells of bovine adrenal medulla

2010 ◽  
Vol 89 (1) ◽  
pp. 44-57 ◽  
Author(s):  
A.M. Oliván ◽  
R. Pérez-Rodríguez ◽  
C. Roncero ◽  
C. Arce ◽  
M.P. González ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Glutamate Transporter ◽  
Vesicular Glutamate Transporter ◽  
Bovine Adrenal Medulla ◽  
Transporter Expression

scholarly journals Glucose transporters in isolated chromaffin cells. Effects of insulin and secretagogues

1987 ◽  
Vol 243 (2) ◽  
pp. 541-547 ◽  
Author(s):  
E G Delicado ◽  
M T Miras Portugal
Keyword(s):  
Plasma Membrane ◽  
Glucose Transport ◽  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Cytochalasin B ◽  
Insulin Receptors ◽  
Neural Tissue ◽  
Glucose Transporters ◽  
High Affinity ◽  
Bovine Adrenal Medulla

1. Isolated chromaffin cells from bovine adrenal medulla were used to study glucose transport in a homogeneous neural tissue. 2. The affinity of glucose transporters was 1.20 +/- 0.52 mM by the infinite-cis technique and 1.02 +/- 0.09 mM by the direct transport experiments. 3. The affinity for 2-deoxyglucose of these transporters was 2.3 mM. 4. The glucose transporters, quantified by [3H]cytochalasin B binding, were 419,532 +/- 120,740 receptors/cell, which corresponds to about 7.2 +/- 2 pmol/mg of protein, with KD = 0.1 microM. 5. High-affinity insulin receptors with KD = 3.95 nM were present at a density of 68,400 +/- 7500 per cell. 6. Insulin and secretagogues increased glucose transport, raising the transporter number at the plasma membrane without changes in the affinity.

Interactions Between Bovine Adrenal Medulla Endothelial and Chromaffin Cells

1998 ◽  
pp. 91-107 ◽  
Author(s):  
Fernando F. Vargas ◽  
Soledad Calvo ◽  
Raul Vinet ◽  
Eduardo Rojas
Keyword(s):  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Bovine Adrenal Medulla

Diadenosine 5′,5′′′-P1,P4-tetraphosphate (Ap4A), ATP and catecholamine content in bovine adrenal medulla, chromaffin granules and chromaffin cells

Biochimie ◽  
1994 ◽  
Vol 76 (5) ◽  
pp. 404-409 ◽  
Author(s):  
M.A. Günther Sillero ◽  
M. Del Valle ◽  
E. Zaera ◽  
P. Michelena ◽  
A.G. García ◽  
...  
Keyword(s):  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Chromaffin Granules ◽  
Catecholamine Content ◽  
Bovine Adrenal Medulla

scholarly journals Restriction of Secretory Granule Motion near the Plasma Membrane of Chromaffin Cells

2001 ◽  
Vol 153 (1) ◽  
pp. 177-190 ◽  
Author(s):  
Laura M. Johns ◽  
Edwin S. Levitan ◽  
Eric A. Shelden ◽  
Ronald W. Holz ◽  
Daniel Axelrod
Keyword(s):  
Plasma Membrane ◽  
Total Internal Reflection ◽  
Chromaffin Cells ◽  
Botulinum Toxin A ◽  
Secretory Granules ◽  
Internal Reflection ◽  
Snare Proteins ◽  
Bovine Chromaffin Cells ◽  
Heterogeneous Matrix ◽  
Granule Motion

We used total internal reflection fluorescence microscopy to study quantitatively the motion and distribution of secretory granules near the plasma membrane (PM) of living bovine chromaffin cells. Within the ∼300-nm region measurably illuminated by the evanescent field resulting from total internal reflection, granules are preferentially concentrated close to the PM. Granule motion normal to the substrate (the z direction) is much slower than would be expected from free Brownian motion, is strongly restricted over tens of nanometer distances, and tends to reverse directions within 0.5 s. The z-direction diffusion coefficients of granules decrease continuously by two orders of magnitude within less than a granule diameter of the PM as granules approach the PM. These analyses suggest that a system of tethers or a heterogeneous matrix severely limits granule motion in the immediate vicinity of the PM. Transient expression of the light chains of tetanus toxin and botulinum toxin A did not disrupt the restricted motion of granules near the PM, indicating that SNARE proteins SNAP-25 and VAMP are not necessary for the decreased mobility. However, the lack of functional SNAREs on the plasma or granule membranes in such cells reduces the time that some granules spend immediately adjacent to the PM.

Recycling of a secretory granule membrane protein after stimulated secretion

1993 ◽  
Vol 106 (2) ◽  
pp. 649-655 ◽  
Author(s):  
S.M. Hurtley
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Secretory Granule ◽  
Chromaffin Cells ◽  
Secretory Granules ◽  
Primary Cultures ◽  
Dopamine Beta Hydroxylase ◽  
Granule Membrane ◽  
Antibody Complex ◽  
Adrenal Chromaffin

Recycling of a secretory granule membrane protein, dopamine-beta-hydroxylase, was examined in primary cultures of bovine adrenal chromaffin cells. Cells were stimulated to secrete in the presence of antibodies directed against the luminal domain of dopamine-beta-hydroxylase. The location of the antibodies after various times of reincubation and after a second secretory stimulus was assessed using immunofluorescence microscopy. Stimulation led to the exposure of dopamine-beta-hydroxylase at the plasma membrane, which could be detected by a polyclonal antibody in living and fixed cells. The plasma membrane dopamine-beta-hydroxylase, either alone or complexed with antibody, was rapidly internalized after removal of the secretagogue. Internalized protein-antibody complex remained stable for at least 24 hours of reculture. Twenty four hours after stimulation the cells with internalized antibody could respond to further stimulation and some of the antibody was re-exposed at the plasma membrane. These findings were confirmed using FACS analysis. This suggests that the antibody-protein complex had returned to secretory granules that could respond to further secretagogue stimulation.

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