Related Experiment Video
Updated: Jun 23, 2026
09:07
Fluorescent Calcium Imaging and Subsequent In Situ Hybridization for Neuronal Precursor Characterization in Xenopus laevis
Published on: February 18, 2020
A lethal convergence of dopamine and calcium
1Department of Physiology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. j-surmeier@northwestern.edu
Neuron
|May 5, 2009
Summary
Calcium influx via L-type channels increases dopamine synthesis, potentially harming neurons in Parkinson's disease. This finding offers new insights into dopamine's role in neurodegeneration.
Area of Science:
- Neuroscience
- Neurobiology
- Cellular Biology
Background:
- Parkinson's disease is a neurodegenerative disorder characterized by the loss of dopaminergic neurons.
- The role of dopamine in this cell loss remains a subject of ongoing debate.
- Ventral mesencephalon neurons are particularly vulnerable in Parkinson's disease.
Discussion:
- Mosharov et al. investigated the impact of calcium (Ca2+) influx on dopamine synthesis in vulnerable neurons.
- The study demonstrates that calcium influx through L-type channels significantly elevates dopamine production.
- This elevated synthesis may reach potentially toxic levels, contributing to neuronal damage.
Key Insights:
- Calcium influx via L-type channels is a critical regulator of dopamine synthesis.
- Elevated dopamine synthesis, driven by Ca2+ influx, is implicated as a potential mechanism for neurotoxicity in Parkinson's disease.
- The findings challenge previous assumptions and offer a new perspective on dopamine's role in Parkinson's pathogenesis.
Outlook:
- Further research is needed to fully elucidate the mechanisms linking Ca2+ influx, dopamine synthesis, and neurodegeneration.
- Therapeutic strategies targeting L-type calcium channels or dopamine synthesis could be explored for Parkinson's disease treatment.
- This study opens new avenues for understanding and potentially intervening in the progression of Parkinson's disease.
More Related Videos
17:05Loading a Calcium Dye into Frog Nerve Endings Through the Nerve Stump: Calcium Transient Registration in the Frog Neuromuscular Junction
Published on: July 8, 2017
06:54Quantifying Spontaneous Ca2+ Fluxes and their Downstream Effects in Primary Mouse Midbrain Neurons
Published on: September 9, 2020
Related Concept Videos
01:27Feedback Regulation of Calcium Concentration
Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
01:30Ligand-Gated Ion Channel Receptor: Gating Mechanism
Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
01:16Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
01:26Chemical Synapses
Chemical synapses are specialized sites between two neurons or between a neuron and a non-neuronal cell like a muscle, glandular or sensory cell.
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...
01:26Chemical Synapses
Chemical synapses are specialized sites between two neurons or between a neuron and a non-neuronal cell like a muscle, glandular or sensory cell.
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...
01:26Fusion of Secretory Vesicles with the Plasma Membrane
Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...