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Quantification of p38/synaptophysin in highly purified adrenal medullary chromaffin vesicles
p38/synaptophysin is a membrane protein present
in clear (synaptic) vesicles of neurons and endocrine
ceHs [1-4]. From the amino acid sequence
deduced from cDNAs encoding p38/synaptophysin,
a model with several membrane spanning
polypeptide segments and a carboxy-terminal
protein domain exposed to the cytoplasmic surface
has been constructed [5-7].
The function of p38/synaptophysin is not
known. It has been suggested to form a transmembrane
channel for ions, or to interact with
cytoplasmic factors via its cytoplasmic domain [7].
Since synaptophysin binds Ca2
+, it may also play
a role in the release of neurotransmitters stored in
clear (synaptic) vesicles [3].
Recently it has been reported [8] that p38/synaptophysin
also occurs in hormone containing large
dense core vesicles. This would imply that
p38/synaptophysin could fulfill similar functions
as described above in chromaffin and other
secretory ceHs containing large dense core vesicles.
In dear (synaptic) vesicles p38/synaptophysin constitutes
7.51Jfo of the vesicle membrane proteins [I].
The amount of p38/synaptophysin in large dense
core vesides is not known. Here we report on the
quantification of p38/synaptophysin in highly
purified chromaffin secretory vesides
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By Ludwig-Maximilians-Universität Münchenp38/synaptophysin is a membrane protein present
in clear (synaptic) vesicles of neurons and endocrine
ceHs [1-4]. From the amino acid sequence
deduced from cDNAs encoding p38/synaptophysin,
a model with several membrane spanning
polypeptide segments and a carboxy-terminal
protein domain exposed to the cytoplasmic surface
has been constructed [5-7].
The function of p38/synaptophysin is not
known. It has been suggested to form a transmembrane
channel for ions, or to interact with
cytoplasmic factors via its cytoplasmic domain [7].
Since synaptophysin binds Ca2
+, it may also play
a role in the release of neurotransmitters stored in
clear (synaptic) vesicles [3].
Recently it has been reported [8] that p38/synaptophysin
also occurs in hormone containing large
dense core vesicles. This would imply that
p38/synaptophysin could fulfill similar functions
as described above in chromaffin and other
secretory ceHs containing large dense core vesicles.
In dear (synaptic) vesicles p38/synaptophysin constitutes
7.51Jfo of the vesicle membrane proteins [I].
The amount of p38/synaptophysin in large dense
core vesides is not known. Here we report on the
quantification of p38/synaptophysin in highly
purified chromaffin secretory vesides
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