Biochemical Characterization of Netrin-synergizing Activity
The netrin-1 protein elicits spinal commissural axon outgrowth and turning in vitro and has been shown to be required for commissural axon guidance in vivo in the developing spinal cord. Biochemical observations made during the purification of netrin-1 suggest that this ligand and its receptor, DCC,...
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Published in | The Journal of biological chemistry Vol. 275; no. 11; pp. 7832 - 7838 |
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Main Authors | , |
Format | Journal Article |
Language | English |
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17.03.2000
American Society for Biochemistry and Molecular Biology |
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Abstract | The netrin-1 protein elicits spinal commissural axon outgrowth and turning in vitro and has been shown to be required for commissural axon guidance in vivo in the developing spinal cord. Biochemical observations made during the purification of netrin-1 suggest that this ligand and its receptor, DCC, may not function alone in directing commissural axon guidance. Recombinant netrin-1 protein is ∼10 times more active in eliciting axon outgrowth from embryonic day (E) 13 rat dorsal spinal cord explants than from E11 rat dorsal spinal cord explants (Serafini, T., Kennedy, T. E., Galko, M. J., Mirzayan, C., Jessell, T. M., and Tessier-Lavigne, M. (1994) Cell 78, 409–424) even though the starting material for the netrin purification, a high salt extract of E10 chicken brain membranes, is equally active on E13 and E11 explants. We previously reported an activity termed netrin-synergizing activity (NSA) that can potentiate the outgrowth-promoting activity of netrin-1 on E11 explants (Serafiniet al.). Here we report a biochemical characterization of NSA in netrin-depleted high salt extracts of E10 chicken brain membranes. We provide evidence that NSA is composed of a denaturation-resistant basic protein(s) in the 25–35-kDa size range. We also provide evidence that the activity may be heterogeneous, splitting into three species that may be distinct or related. The results reported here should facilitate purification of this activity from a more abundant source or identification of the activity based on similarity to known proteins that share its distinctive biochemical properties. |
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AbstractList | The netrin-1 protein elicits spinal commissural axon outgrowth and turning in vitro and has been shown to be required for commissural axon guidance in vivo in the developing spinal cord. Biochemical observations made during the purification of netrin-1 suggest that this ligand
and its receptor, DCC, may not function alone in directing commissural axon guidance. Recombinant netrin-1 protein is â¼10
times more active in eliciting axon outgrowth from embryonic day (E) 13 rat dorsal spinal cord explants than from E11 rat
dorsal spinal cord explants (Serafini, T., Kennedy, T. E., Galko, M. J., Mirzayan, C., Jessell, T. M., and Tessier-Lavigne,
M. (1994) Cell 78, 409â424) even though the starting material for the netrin purification, a high salt extract of E10 chicken brain membranes,
is equally active on E13 and E11 explants. We previously reported an activity termed netrin-synergizing activity (NSA) that
can potentiate the outgrowth-promoting activity of netrin-1 on E11 explants (Serafini et al. ). Here we report a biochemical characterization of NSA in netrin-depleted high salt extracts of E10 chicken brain membranes.
We provide evidence that NSA is composed of a denaturation-resistant basic protein(s) in the 25â35-kDa size range. We also
provide evidence that the activity may be heterogeneous, splitting into three species that may be distinct or related. The
results reported here should facilitate purification of this activity from a more abundant source or identification of the
activity based on similarity to known proteins that share its distinctive biochemical properties. The netrin-1 protein elicits spinal commissural axon outgrowth and turning in vitro and has been shown to be required for commissural axon guidance in vivo in the developing spinal cord. Biochemical observations made during the purification of netrin-1 suggest that this ligand and its receptor, DCC, may not function alone in directing commissural axon guidance. Recombinant netrin-1 protein is approximately 10 times more active in eliciting axon outgrowth from embryonic day (E) 13 rat dorsal spinal cord explants than from E11 rat dorsal spinal cord explants (Serafini, T., Kennedy, T. E., Galko, M. J., Mirzayan, C., Jessell, T. M., and Tessier-Lavigne, M. (1994) Cell 78, 409-424) even though the starting material for the netrin purification, a high salt extract of E10 chicken brain membranes, is equally active on E13 and E11 explants. We previously reported an activity termed netrin-synergizing activity (NSA) that can potentiate the outgrowth-promoting activity of netrin-1 on E11 explants (Serafini et al.). Here we report a biochemical characterization of NSA in netrin-depleted high salt extracts of E10 chicken brain membranes. We provide evidence that NSA is composed of a denaturation-resistant basic protein(s) in the 25-35-kDa size range. We also provide evidence that the activity may be heterogeneous, splitting into three species that may be distinct or related. The results reported here should facilitate purification of this activity from a more abundant source or identification of the activity based on similarity to known proteins that share its distinctive biochemical properties. The netrin-1 protein elicits spinal commissural axon outgrowth and turning in vitro and has been shown to be required for commissural axon guidance in vivo in the developing spinal cord. Biochemical observations made during the purification of netrin-1 suggest that this ligand and its receptor, DCC, may not function alone in directing commissural axon guidance. Recombinant netrin-1 protein is ∼10 times more active in eliciting axon outgrowth from embryonic day (E) 13 rat dorsal spinal cord explants than from E11 rat dorsal spinal cord explants (Serafini, T., Kennedy, T. E., Galko, M. J., Mirzayan, C., Jessell, T. M., and Tessier-Lavigne, M. (1994) Cell 78, 409–424) even though the starting material for the netrin purification, a high salt extract of E10 chicken brain membranes, is equally active on E13 and E11 explants. We previously reported an activity termed netrin-synergizing activity (NSA) that can potentiate the outgrowth-promoting activity of netrin-1 on E11 explants (Serafiniet al.). Here we report a biochemical characterization of NSA in netrin-depleted high salt extracts of E10 chicken brain membranes. We provide evidence that NSA is composed of a denaturation-resistant basic protein(s) in the 25–35-kDa size range. We also provide evidence that the activity may be heterogeneous, splitting into three species that may be distinct or related. The results reported here should facilitate purification of this activity from a more abundant source or identification of the activity based on similarity to known proteins that share its distinctive biochemical properties. |
Author | Tessier-Lavigne, Marc Galko, Michael J. |
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Cites_doi | 10.1523/JNEUROSCI.06-12-03576.1986 10.1016/0003-9861(69)90042-3 10.1038/336775a0 10.1016/S0092-8674(00)80588-7 10.1016/S0021-9258(18)62040-X 10.1016/0076-6879(95)48032-3 10.1146/annurev.neuro.22.1.351 10.1016/0092-8674(94)90421-9 10.1002/bies.950151207 10.1016/0092-8674(90)90223-2 10.1016/0896-6273(90)90148-9 10.1016/S0092-8674(00)81336-7 10.1038/386796a0 10.1016/0092-8674(93)80064-L 10.1146/annurev.ne.19.030196.002013 10.1002/j.1460-2075.1982.tb01207.x 10.1016/S0896-6273(00)80241-X 10.1016/S0092-8674(00)81795-X 10.1016/0092-8674(94)90420-0 |
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SubjectTerms | Animals Axons - drug effects Brain Chemistry Cell Communication Chromatography, Affinity Drug Synergism Heparin In Vitro Techniques Nerve Growth Factors - pharmacology Nerve Tissue Proteins - isolation & purification Nerve Tissue Proteins - pharmacology Netrin-1 Protein Binding Protein Denaturation Rats Spinal Cord - drug effects Spinal Cord - embryology Tumor Suppressor Proteins |
Title | Biochemical Characterization of Netrin-synergizing Activity |
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