Characterization of protein F1 (47 kDa, 4.5 pI): A kinase C substrate directly related to neural plasticity

Robert B. Nelson; Aryeh Routtenberg

doi:10.1016/0014-4886(85)90277-8

Characterization of protein F1 (47 kDa, 4.5 pI): A kinase C substrate directly related to neural plasticity

Robert B. Nelson^*, Aryeh Routtenberg

^*Corresponding author for this work

Psychology

Research output: Contribution to journal › Article › peer-review

144 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	213-224
Number of pages	12
Journal	Experimental Neurology
Volume	89
Issue number	1
DOIs	https://doi.org/10.1016/0014-4886(85)90277-8
State	Published - Jul 1985

Funding

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.

ASJC Scopus subject areas

Neurology
Developmental Neuroscience

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10.1016/0014-4886(85)90277-8

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@article{aeed6f7d87ec4c6ea6524456b6ac2b88,

title = "Characterization of protein F1 (47 kDa, 4.5 pI): A kinase C substrate directly related to neural plasticity",

abstract = "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.",

author = "Nelson, \{Robert B.\} and Aryeh Routtenberg",

note = "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. {\textquoteright} 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.",

year = "1985",

month = jul,

doi = "10.1016/0014-4886(85)90277-8",

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journal = "Experimental Neurology",

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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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Characterization of protein F1 (47 kDa, 4.5 pI): A kinase C substrate directly related to neural plasticity

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