Cysteine String Protein
Cysteine string proteins (CSP) are discovered very recently and they belong to the class of cysteine-rich proteins.
They play significant role in neurotransmitter release.
They are secreted by the secretory vesicles and possess a "J-Domain" and a palmitoylated cysteine-rich 'string'.
These two regions are very much essential for the release of neurotransmitter.
The exact role of CSPs in neurotransmission is under debate.
One of the research studies identify this protein to be interacting with receptor coupled trimeric GTP binding proteins and N-type calcium channels.
The alpha subunit of G-protein is known to interact with J-Domain of CSP in the presence of ATP.
The beta and gamma subunits of G-protein are found to be interacting with C-terminus of CSP with and without the help of ATP molecules.
The binding affinity between G-protein and N-type calcium channel with CSP results in inhibition of the channels by the G-protein.
As the N-type calcium channels are important in pre-synaptic vesicle release, the study describes the role of CSP in neurotransmission.
To find out the activity of CSPs and their exact function, an experiment was conducted for identifying this protein in the CNS of rat brain.
The presence of CSP and its immuno-reactivity was identified using a technique called immunohistochemistry.
This technique was performed using affinity purified anti-CSP antibodies.
The immunoreactivity of CSPs was found to be more at synapse rich regions.
Neuromuscular joints were found to be exhibiting strong immunoreactivity for CSP.
It is proved that CSPs are involved in pre-synaptic events in several synapses by the discovery of CSP immunoreactivity.
The CSPs are also observed to be present in adrenal medulla which indicates that these proteins are involved in events related to secretion in some non-neural cells.
They play significant role in neurotransmitter release.
They are secreted by the secretory vesicles and possess a "J-Domain" and a palmitoylated cysteine-rich 'string'.
These two regions are very much essential for the release of neurotransmitter.
The exact role of CSPs in neurotransmission is under debate.
One of the research studies identify this protein to be interacting with receptor coupled trimeric GTP binding proteins and N-type calcium channels.
The alpha subunit of G-protein is known to interact with J-Domain of CSP in the presence of ATP.
The beta and gamma subunits of G-protein are found to be interacting with C-terminus of CSP with and without the help of ATP molecules.
The binding affinity between G-protein and N-type calcium channel with CSP results in inhibition of the channels by the G-protein.
As the N-type calcium channels are important in pre-synaptic vesicle release, the study describes the role of CSP in neurotransmission.
To find out the activity of CSPs and their exact function, an experiment was conducted for identifying this protein in the CNS of rat brain.
The presence of CSP and its immuno-reactivity was identified using a technique called immunohistochemistry.
This technique was performed using affinity purified anti-CSP antibodies.
The immunoreactivity of CSPs was found to be more at synapse rich regions.
Neuromuscular joints were found to be exhibiting strong immunoreactivity for CSP.
It is proved that CSPs are involved in pre-synaptic events in several synapses by the discovery of CSP immunoreactivity.
The CSPs are also observed to be present in adrenal medulla which indicates that these proteins are involved in events related to secretion in some non-neural cells.
