TY - JOUR
T1 - Vesicular Transmitter Content in Chromaffin Cells Can Be Regulated via Extracellular ATP
AU - Larsson, Anna
AU - Majdi, Soodabeh
AU - Borges, Ricardo
AU - Ewing, Andrew
N1 - Funding Information:
We acknowledge funding from the European Research Council (Advanced Grant), the Knut and Alice Wallenberg Foundation, the Swedish Research council (VR), the National Institutes of Health, and the Spanish MINECO-FEDER BFU2017-82618-P.
Publisher Copyright:
Copyright © 2019 American Chemical Society.
PY - 2019/11/20
Y1 - 2019/11/20
N2 - The energy carrying molecule adenosine triphosphate (ATP) has been implicated for its role in modulation of chemical signaling for some time. Despite this, the precise effects and mechanisms of action of ATP on secretory cells are not well-known. Here, bovine chromaffin cells have been used as a model system to study the effects of extracellular ATP in combination with the catecholamine transmitter norepinephrine (NE). Both transmitter storage and exocytotic release were quantified using complementary amperometric techniques. Although incubation with NE alone did not cause any changes to either transmitter storage or release, coincubation with NE and ATP resulted in a significant increase that was concentration dependent. To probe the potential mechanisms of action, a slowly hydrolyzable version of ATP, ATP-γ-S, was used either alone or together with NE. The result implicates two different behaviors of ATP acting on both the purinergic autoreceptors and as a source of the energy needed to load chromaffin cell vesicles.
AB - The energy carrying molecule adenosine triphosphate (ATP) has been implicated for its role in modulation of chemical signaling for some time. Despite this, the precise effects and mechanisms of action of ATP on secretory cells are not well-known. Here, bovine chromaffin cells have been used as a model system to study the effects of extracellular ATP in combination with the catecholamine transmitter norepinephrine (NE). Both transmitter storage and exocytotic release were quantified using complementary amperometric techniques. Although incubation with NE alone did not cause any changes to either transmitter storage or release, coincubation with NE and ATP resulted in a significant increase that was concentration dependent. To probe the potential mechanisms of action, a slowly hydrolyzable version of ATP, ATP-γ-S, was used either alone or together with NE. The result implicates two different behaviors of ATP acting on both the purinergic autoreceptors and as a source of the energy needed to load chromaffin cell vesicles.
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U2 - 10.1021/acschemneuro.9b00494
DO - 10.1021/acschemneuro.9b00494
M3 - Article
C2 - 31637911
AN - SCOPUS:85074637945
SN - 1948-7193
VL - 10
SP - 4735
EP - 4740
JO - ACS Chemical Neuroscience
JF - ACS Chemical Neuroscience
IS - 11
ER -