TY - JOUR
T1 - Characterization of protein F1 (47 kDa, 4.5 pI)
T2 - A kinase C substrate directly related to neural plasticity
AU - Nelson, Robert B.
AU - Routtenberg, Aryeh
N1 - Funding Information:
Abbreviations: IEF-SDS-two-dimensional (isoelectric focusing and sodium dodecyl sulfate) gel electrophoresis, LTP-long-term potentiation, NEPHGE-SDS-two-dimensional (nonequilibrium pH gradient and sodium dodecyl sulfate) gel electrophoresis, PS-phosphatidyl+serine, p&isoelectric point, Mrmolecular mass. ’ This work was supported by National Institute of Mental Health grant MH 25281 and grant AFSGR 83-0335 to A.R. R.B.N. was a National Institute of Drug Abuse predoctoral fellow (grant DA 05254). We thank Dr. K. Murakami for preparing purified kinase C, D. Lovinger and R. Akers for preparing some of the tissue used in this study and for their valuable comments during preparation of the manuscript; and P. Gosling and S. Wojcik for technical assistance in preparation of two-dimensional gels.
PY - 1985/7
Y1 - 1985/7
N2 - We recently demonstrated that long-term potentiation in rat hippocampal formation leads to a selective increase in the phosphorylation of a 47-kDa protein band (F1). The present report provided evidence, using two-dimensional gel electrophoresis, that only one major phosphoprotein in rat is found at 47 kDa under conditions identical to those used in that earlier study. This protein, which we also term F1, has an isoelectric point of 4.5 and is increased in phosphorylation after long-term potentiation. In addition to this identification, we demonstrated in two-dimensional gels that protein F1 is a membrane-enriched kinase C substrate whose phosphorylation is stimulated by Ca2+ and phosphatidylserine. Protein F1 may be equivalent to several reported proteins: a brain-specific, synaptically enriched protein (B-50), a major membrane-bound growth cone protein (pp46), and a fast axonally transported "growth-associated protein" (GAP43; 44- to 49-kDa goldfish optic nerve protein). Protein F1 participation in neural plasticity may thus involve growth occurring at synaptic loci.
AB - We recently demonstrated that long-term potentiation in rat hippocampal formation leads to a selective increase in the phosphorylation of a 47-kDa protein band (F1). The present report provided evidence, using two-dimensional gel electrophoresis, that only one major phosphoprotein in rat is found at 47 kDa under conditions identical to those used in that earlier study. This protein, which we also term F1, has an isoelectric point of 4.5 and is increased in phosphorylation after long-term potentiation. In addition to this identification, we demonstrated in two-dimensional gels that protein F1 is a membrane-enriched kinase C substrate whose phosphorylation is stimulated by Ca2+ and phosphatidylserine. Protein F1 may be equivalent to several reported proteins: a brain-specific, synaptically enriched protein (B-50), a major membrane-bound growth cone protein (pp46), and a fast axonally transported "growth-associated protein" (GAP43; 44- to 49-kDa goldfish optic nerve protein). Protein F1 participation in neural plasticity may thus involve growth occurring at synaptic loci.
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U2 - 10.1016/0014-4886(85)90277-8
DO - 10.1016/0014-4886(85)90277-8
M3 - Article
C2 - 3159591
AN - SCOPUS:0021795184
SN - 0014-4886
VL - 89
SP - 213
EP - 224
JO - Experimental Neurology
JF - Experimental Neurology
IS - 1
ER -