RT Journal Article
SR Electronic
T1 Synapsin I in PC12 cells. I. Characterization of the phosphoprotein and effect of chronic NGF treatment
JF The Journal of Neuroscience
JO J. Neurosci.
FD Society for Neuroscience
SP 1294
OP 1299
DO 10.1523/JNEUROSCI.07-05-01294.1987
VO 7
IS 5
A1 C Romano
A1 RA Nichols
A1 P Greengard
A1 LA Greene
YR 1987
UL http://www.jneurosci.org/content/7/5/1294.abstract
AB PC12 cells contain a synapsin I-like molecule. Several serum and monoclonal antibodies raised against bovine brain synapsin I bind to and precipitate this molecule, demonstrating immunochemical similarity between the brain and PC12 species. PC12 synapsin I, like brain synapsin I, is a phosphoprotein: It is phosphorylated in intact cells and, when partially purified, serves as a substrate for several synapsin I kinases. PC12 cell synapsin I is structurally similar to brain synapsin I as shown by peptide mapping of 35S-methionine-and 32P- phosphate-labeled molecules from the 2 sources. Chronic NGF treatment of the cells induces a significant increase in the amount of synapsin I relative to total cell protein, measured either by immunolabeling or incorporation of 35S-methionine. The synapsin I present in untreated PC12 cells migrates predominantly as a singlet and that present in cells treated chronically with NGF as a doublet in SDS-PAGE.