Calcium Extrusion from Mammalian Photoreceptor Terminals

Calcium Extrusion from Mammalian Photoreceptor Terminals

Ribbon synapses of vertebrate photoreceptors constantly release glutamate in darkness. Transmitter release is maintained by a steady influx of calcium through voltage-dependent calcium channels, implying the presence of a mechanism that is able to extrude calcium at an equal rate. The two predominan...

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Published in:The Journal of neuroscience Vol. 18; no. 7; pp. 2467 - 2474
Main Authors: Morgans, Catherine W, El Far, Oussama, Berntson, Amy, Wassle, Heinz, Taylor, W. Rowland
Format: Journal Article
Language:English
Published: United States Soc Neuroscience 01-04-1998
Society for Neuroscience
Subjects:
Animals
Biological Transport - physiology
Calcium - metabolism
Calcium-Transporting ATPases - analysis
Calcium-Transporting ATPases - metabolism
Mammals
Microscopy, Confocal
Photoreceptor Cells - chemistry
Photoreceptor Cells - metabolism
Presynaptic Terminals - chemistry
Presynaptic Terminals - enzymology
Rats
Sodium-Calcium Exchanger - analysis
Sodium-Calcium Exchanger - metabolism
Tupaiidae
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Abstract Ribbon synapses of vertebrate photoreceptors constantly release glutamate in darkness. Transmitter release is maintained by a steady influx of calcium through voltage-dependent calcium channels, implying the presence of a mechanism that is able to extrude calcium at an equal rate. The two predominant mechanisms of intracellular calcium extrusion are the plasma membrane calcium ATPase (PMCA) and the Na+/Ca2+-exchanger. Immunohistochemical staining of retina sections revealed strong immunoreactivity for the PMCA in rod and cone terminals, whereas staining for the Na+/Ca2+-exchanger was very weak. The PMCA was localized to the plasma membrane along the sides of the photoreceptor terminals and was excluded from the base of the terminals where the active zones are located. The amplitude of a calcium-activated chloride current was used to monitor the intracellular calcium concentration. An upper limit for the time required to remove intracellular free calcium is obtained from two time constants measured for the calcium-activated chloride current tail currents: one of 50 msec and a second of 190 msec. Calcium extrusion was inhibited in the absence of intracellular ATP or in the presence of the PMCA inhibitor orthovanadate, but was unaffected by replacement of external Na+ with Li+. The data indicate that the PMCA, rather than the Na+/Ca2+-exchanger, is the predominant mechanism for calcium extrusion from photoreceptor synaptic terminals.
AbstractList Ribbon synapses of vertebrate photoreceptors constantly release glutamate in darkness. Transmitter release is maintained by a steady influx of calcium through voltage-dependent calcium channels, implying the presence of a mechanism that is able to extrude calcium at an equal rate. The two predominant mechanisms of intracellular calcium extrusion are the plasma membrane calcium ATPase (PMCA) and the Na + /Ca 2+ -exchanger. Immunohistochemical staining of retina sections revealed strong immunoreactivity for the PMCA in rod and cone terminals, whereas staining for the Na + /Ca 2+ -exchanger was very weak. The PMCA was localized to the plasma membrane along the sides of the photoreceptor terminals and was excluded from the base of the terminals where the active zones are located. The amplitude of a calcium-activated chloride current was used to monitor the intracellular calcium concentration. An upper limit for the time required to remove intracellular free calcium is obtained from two time constants measured for the calcium-activated chloride current tail currents: one of 50 msec and a second of 190 msec. Calcium extrusion was inhibited in the absence of intracellular ATP or in the presence of the PMCA inhibitor orthovanadate, but was unaffected by replacement of external Na + with Li + . The data indicate that the PMCA, rather than the Na + /Ca 2+ -exchanger, is the predominant mechanism for calcium extrusion from photoreceptor synaptic terminals.
Ribbon synapses of vertebrate photoreceptors constantly release glutamate in darkness. Transmitter release is maintained by a steady influx of calcium through voltage-dependent calcium channels, implying the presence of a mechanism that is able to extrude calcium at an equal rate. The two predominant mechanisms of intracellular calcium extrusion are the plasma membrane calcium ATPase (PMCA) and the Na+/Ca2+-exchanger. Immunohistochemical staining of retina sections revealed strong immunoreactivity for the PMCA in rod and cone terminals, whereas staining for the Na+/Ca2+-exchanger was very weak. The PMCA was localized to the plasma membrane along the sides of the photoreceptor terminals and was excluded from the base of the terminals where the active zones are located. The amplitude of a calcium-activated chloride current was used to monitor the intracellular calcium concentration. An upper limit for the time required to remove intracellular free calcium is obtained from two time constants measured for the calcium-activated chloride current tail currents: one of 50 msec and a second of 190 msec. Calcium extrusion was inhibited in the absence of intracellular ATP or in the presence of the PMCA inhibitor orthovanadate, but was unaffected by replacement of external Na+ with Li+. The data indicate that the PMCA, rather than the Na+/Ca2+-exchanger, is the predominant mechanism for calcium extrusion from photoreceptor synaptic terminals.
Ribbon synapses of vertebrate photoreceptors constantly release glutamate in darkness. Transmitter release is maintained by a steady influx of calcium through voltage-dependent calcium channels, implying the presence of a mechanism that is able to extrude calcium at an equal rate. The two predominant mechanisms of intracellular calcium extrusion are the plasma membrane calcium ATPase (PMCA) and the Na super(+)/Ca super(2+)-exchanger. Immunohistochemical staining of retina sections revealed strong immunoreactivity for the PMCA in rod and cone terminals, whereas staining for the Na super(+)/Ca super(2+)-exchanger was very weak. The PMCA was localized to the plasma membrane along the sides of the photoreceptor terminals and was excluded from the base of the terminals where the active zones are located. The amplitude of a calcium-activated chloride current was used to monitor the intracellular calcium concentration. An upper limit for the time required to remove intracellular free calcium is obtained from two time constants measured for the calcium-activated chloride current tail currents: one of 50 msec and a second of 190 msec. Calcium extrusion was inhibited in the absence of intracellular ATP or in the presence of the PMCA inhibitor orthovanadate, but was unaffected by replacement of external Na super(+) with Li super(+). The data indicate that the PMCA, rather than the Na super(+)/Ca super(2+)-exchanger, is the predominant mechanism for calcium extrusion from photoreceptor synaptic terminals.
Author Wassle, Heinz
Morgans, Catherine W
Taylor, W. Rowland
Berntson, Amy
El Far, Oussama
AuthorAffiliation 2 Neurochemistry, Max-Planck-Institute für Hirnforschung, D-60528 Frankfurt, Germany
1 Departments of Neuroanatomy and
AuthorAffiliation_xml – name: 1 Departments of Neuroanatomy and
– name: 2 Neurochemistry, Max-Planck-Institute für Hirnforschung, D-60528 Frankfurt, Germany
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  fullname: Taylor, W. Rowland
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Snippet Ribbon synapses of vertebrate photoreceptors constantly release glutamate in darkness. Transmitter release is maintained by a steady influx of calcium through...
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SubjectTerms Animals
Biological Transport - physiology
Calcium - metabolism
Calcium-Transporting ATPases - analysis
Calcium-Transporting ATPases - metabolism
Mammals
Microscopy, Confocal
Photoreceptor Cells - chemistry
Photoreceptor Cells - metabolism
Presynaptic Terminals - chemistry
Presynaptic Terminals - enzymology
Rats
Sodium-Calcium Exchanger - analysis
Sodium-Calcium Exchanger - metabolism
Tupaiidae
Title Calcium Extrusion from Mammalian Photoreceptor Terminals
URI http://www.jneurosci.org/cgi/content/abstract/18/7/2467
https://www.ncbi.nlm.nih.gov/pubmed/9502807
https://search.proquest.com/docview/16325711
https://search.proquest.com/docview/79737854
https://pubmed.ncbi.nlm.nih.gov/PMC6793104
Volume 18
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