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Spatio-temporal expression of a novel neuron-derived neurotrophic factor (NDNF) in mouse brains during development.

Kuang XL, Zhao XM, Xu HF, Shi YY, Deng JB, Sun GT - BMC Neurosci (2010)

Bottom Line: Cajal-Retzius cells, cortex neurons, hippocampus neurons, olfactory mitral cells, cerebellar purkinje cells, cerebellar granular cells and spinal neurons were found to be NDNF-positive.NDNF expression was observed in the neurons during development.The results of this study indicated that NDNF is a novel neurotrophic factor derived from neurons that may be useful in the treatment of neuronal degeneration diseases and nerve injuries.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Biochemistry and Molecular Biology, Institute of Molecular Medicine, Medical School, Henan University, KaiFeng, PR China.

ABSTRACT

Background: Neuron-derived neurotrophic factor (NDNF) is evolutionarily well conserved, being present in invertebrate animals such as the nematode, Caenorhabditis elegans, as well as in the fruit fly, Drosophila melanogaster. Multiple cysteines are conserved between species and secondary structure prediction shows that NDNF is mainly composed of beta-strands. In this study, we aimed to investigate the function of NDNF.

Results: NDNF is a glycosylated, disulfide-bonded secretory protein that contains a fibronectin type III domain. NDNF promoted migration and growth and elicited neurite outgrowth of mouse hippocampal neurons in culture. NDNF also protected cultured hippocampal neurons against excitotoxicity and amyloid beta-peptide toxicity. Western blotting showed that NDNF was exclusively expressed in the brain and spinal cord. Immunostaining indicated that NDNF was expressed by neurons and not by astrocytes. Cajal-Retzius cells, cortex neurons, hippocampus neurons, olfactory mitral cells, cerebellar purkinje cells, cerebellar granular cells and spinal neurons were found to be NDNF-positive. NDNF expression was observed in the neurons during development.

Conclusions: The results of this study indicated that NDNF is a novel neurotrophic factor derived from neurons that may be useful in the treatment of neuronal degeneration diseases and nerve injuries.

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Related in: MedlinePlus

Comparison of the protein sequence of NDNF. Identical amino acids are shaded. The signal peptide of NDNF is marked (SP), and the conserved N-linked glycosylation sites are indicated (G). The putative secondary structure is presented under the alignment. The red box represents the alpha-helix and the blue box represents the beta-sheet. In the frame, the phylogenic tree of NDNF proteins is shown.
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Figure 1: Comparison of the protein sequence of NDNF. Identical amino acids are shaded. The signal peptide of NDNF is marked (SP), and the conserved N-linked glycosylation sites are indicated (G). The putative secondary structure is presented under the alignment. The red box represents the alpha-helix and the blue box represents the beta-sheet. In the frame, the phylogenic tree of NDNF proteins is shown.

Mentions: Human NDNF gene encodes a 568 amino acid polypeptide with a calculated molecular mass of 65 kDa. Analysis using the SignalP software predicted that NDNF has a signal peptide, which indicates that it may enter the secretory pathway (Figure 1). Human NDNF contains two FnIII domains (174-325, 445-554) and belongs to a conserved protein family (Pfam10179). The fly ortholog, nord, is primarily expressed in the mushroom body and is involved in olfactory learning [6]. There are two potential consensus sites for N-linked glycosylation (322, 488), which are conserved among mammalian species. Human NDNF protein contains ten cysteines, five of which are conserved from nematodes to humans. Protein secondary structure analysis indicated that NDNF is a predominantly beta-sheet protein (about 43%) with a small amount of alpha-helix (about 5%). Prediction of the protein globularity demonstrated that NDNF appears as compact and globular domain. These findings demonstrate that NDNF is likely to be a glycosylated, disulfide-bonded, secreted protein and that it may be involved in neural function.


Spatio-temporal expression of a novel neuron-derived neurotrophic factor (NDNF) in mouse brains during development.

Kuang XL, Zhao XM, Xu HF, Shi YY, Deng JB, Sun GT - BMC Neurosci (2010)

Comparison of the protein sequence of NDNF. Identical amino acids are shaded. The signal peptide of NDNF is marked (SP), and the conserved N-linked glycosylation sites are indicated (G). The putative secondary structure is presented under the alignment. The red box represents the alpha-helix and the blue box represents the beta-sheet. In the frame, the phylogenic tree of NDNF proteins is shown.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2984559&req=5

Figure 1: Comparison of the protein sequence of NDNF. Identical amino acids are shaded. The signal peptide of NDNF is marked (SP), and the conserved N-linked glycosylation sites are indicated (G). The putative secondary structure is presented under the alignment. The red box represents the alpha-helix and the blue box represents the beta-sheet. In the frame, the phylogenic tree of NDNF proteins is shown.
Mentions: Human NDNF gene encodes a 568 amino acid polypeptide with a calculated molecular mass of 65 kDa. Analysis using the SignalP software predicted that NDNF has a signal peptide, which indicates that it may enter the secretory pathway (Figure 1). Human NDNF contains two FnIII domains (174-325, 445-554) and belongs to a conserved protein family (Pfam10179). The fly ortholog, nord, is primarily expressed in the mushroom body and is involved in olfactory learning [6]. There are two potential consensus sites for N-linked glycosylation (322, 488), which are conserved among mammalian species. Human NDNF protein contains ten cysteines, five of which are conserved from nematodes to humans. Protein secondary structure analysis indicated that NDNF is a predominantly beta-sheet protein (about 43%) with a small amount of alpha-helix (about 5%). Prediction of the protein globularity demonstrated that NDNF appears as compact and globular domain. These findings demonstrate that NDNF is likely to be a glycosylated, disulfide-bonded, secreted protein and that it may be involved in neural function.

Bottom Line: Cajal-Retzius cells, cortex neurons, hippocampus neurons, olfactory mitral cells, cerebellar purkinje cells, cerebellar granular cells and spinal neurons were found to be NDNF-positive.NDNF expression was observed in the neurons during development.The results of this study indicated that NDNF is a novel neurotrophic factor derived from neurons that may be useful in the treatment of neuronal degeneration diseases and nerve injuries.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Biochemistry and Molecular Biology, Institute of Molecular Medicine, Medical School, Henan University, KaiFeng, PR China.

ABSTRACT

Background: Neuron-derived neurotrophic factor (NDNF) is evolutionarily well conserved, being present in invertebrate animals such as the nematode, Caenorhabditis elegans, as well as in the fruit fly, Drosophila melanogaster. Multiple cysteines are conserved between species and secondary structure prediction shows that NDNF is mainly composed of beta-strands. In this study, we aimed to investigate the function of NDNF.

Results: NDNF is a glycosylated, disulfide-bonded secretory protein that contains a fibronectin type III domain. NDNF promoted migration and growth and elicited neurite outgrowth of mouse hippocampal neurons in culture. NDNF also protected cultured hippocampal neurons against excitotoxicity and amyloid beta-peptide toxicity. Western blotting showed that NDNF was exclusively expressed in the brain and spinal cord. Immunostaining indicated that NDNF was expressed by neurons and not by astrocytes. Cajal-Retzius cells, cortex neurons, hippocampus neurons, olfactory mitral cells, cerebellar purkinje cells, cerebellar granular cells and spinal neurons were found to be NDNF-positive. NDNF expression was observed in the neurons during development.

Conclusions: The results of this study indicated that NDNF is a novel neurotrophic factor derived from neurons that may be useful in the treatment of neuronal degeneration diseases and nerve injuries.

Show MeSH
Related in: MedlinePlus