Extracellular hydrolysis of diadenosine polyphosphates, ApnA, by bovine chromaffin cells in culture

During exocytosis of the chromaffin granules, ATP is released. ATP can then be hydrolyzed by the ecto-ATPases of the plasma membrane to provide adenosine for reuptake or for activation of P1 purinoceptors. Chromaffin granule membranes also possess ATPase activity. This activity is linked to the uptake of catecholamines from the cytoplasm into the membrane-bound granule compartment.In this report we combine EM cytochemistry and immunogold labelling to provide further evidence for the presence of ATPase on both the plasma membrane and granule membranes of bovine chromaffin cells in culture.

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Bovine chromaffin cells in culture show carboxylesterase activities sensitive to organophosphorus compounds

The International Journal of Biochemistry & Cell Biology ◽

10.1016/1357-2725(96)00045-3 ◽

1996 ◽

Vol 28 (9) ◽

pp. 983-989 ◽

Cited By ~ 5

Author(s):

Miguel A. Sogorb ◽

Eugenio Vilanova ◽

JoséL. Quintanar ◽

Salvador Viniegra

Keyword(s):

Chromaffin Cells ◽

Organophosphorus Compounds ◽

Cells In Culture ◽

Bovine Chromaffin Cells

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Use of Fluorogenic Substrates for Detection and Investigation of Ectoenzymatic Hydrolysis of Diadenosine Polyphosphates: A Fluorometric Study on Chromaffin Cells

Analytical Biochemistry ◽

10.1006/abio.1995.1317 ◽

1995 ◽

Vol 228 (1) ◽

pp. 74-82 ◽

Cited By ~ 23

Author(s):

A. Ramos ◽

J. Pintor ◽

M.T. Mirasportugal ◽

P. Rotllan

Keyword(s):

Chromaffin Cells ◽

Fluorogenic Substrates ◽

Diadenosine Polyphosphates ◽

Hydrolysis Of ◽

Fluorometric Study

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Bovine Chromaffin Cells in Culture, a Promising Model for the Study of Neuropathy Target Esterase and Related Esterases

Toxicology Letters ◽

10.1016/03784-2749(59)4937c- ◽

1995 ◽

Vol 78 ◽

pp. 75

Author(s):

M Sogorb

Keyword(s):

Chromaffin Cells ◽

Neuropathy Target Esterase ◽

Cells In Culture ◽

Bovine Chromaffin Cells

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Bovine adrenal chromaffin cells contain an inositol 1,4,5-trisphosphate-insensitive but caffeine-sensitive Ca2+ store that can be regulated by intraluminal free Ca2+

Biochemical Journal ◽

10.1042/bj2750697 ◽

1991 ◽

Vol 275 (3) ◽

pp. 697-701 ◽

Cited By ~ 59

Author(s):

T R Cheek ◽

V A Barry ◽

M J Berridge ◽

L Missiaen

Keyword(s):

Chromaffin Cells ◽

Ruthenium Red ◽

Release Mechanism ◽

High Dose ◽

Permeabilized Cells ◽

Transient Rise ◽

Bovine Chromaffin Cells ◽

Releasing Effect ◽

Adrenal Chromaffin ◽

Hydrolysis Of

We have characterized some properties of the caffeine-sensitive Ca2+ store in bovine chromaffin cells. Addition of 10 mM-caffeine to permeabilized cells that were allowed to sequester Ca2+ in the presence of the precipitating anion pyrophosphate induced a transient rise in free Ca2+ concentration that was blocked by 10 microM-Ruthenium Red. Caffeine was able to release Ca2+ after the InsP3-sensitive Ca2+ pool had been completely emptied, and 10 microM-InsP3 still released Ca2+ in the presence of a high dose (50 mM) of caffeine, indicating that there are selectively sensitive Ca2+ pools in these cells. The progressive hydrolysis of pyrophosphate by a cytosolic pyrophosphatase induced a spontaneous Ca2+ release after a latency. Caffeine prevented this spontaneous Ca2+ release, indicating that the pyrophosphate-sensitive Ca2+ pool was caffeine-sensitive. On varying the free Ca2+ concentration within the caffeine-sensitive pool (by using methylenediphosphonic acid, pyrophosphate or no precipitating anion), we observed that the Ca(2+)-releasing effect of caffeine was dependent on an elevated intraluminal free Ca2+ concentration. In conclusion, the caffeine-sensitive Ca2+ store in bovine chromaffin cells is largely distinct from the InsP3-sensitive Ca2+ store, and its release mechanism shares characteristics with the ryanodine receptor of muscle cells.

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