Source:http://linkedlifedata.com/resource/pubmed/id/12037567
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6888
|
| pubmed:dateCreated |
2002-5-30
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| pubmed:abstractText |
Myelin-derived axon outgrowth inhibitors, such as Nogo, may account for the lack of axonal regeneration in the central nervous system (CNS) after trauma in adult mammals. A 66-residue domain of Nogo (Nogo-66) is expressed on the surface of oligodendrocytes and can inhibit axonal outgrowth through an axonal Nogo-66 receptor (NgR). The IN-1 monoclonal antibody recognizes Nogo-A and promotes corticospinal tract regeneration and locomotor recovery; however, the undefined nature of the IN-1 epitope in Nogo, the limited specificity of IN-1 for Nogo, and nonspecific anti-myelin effects have prevented a firm conclusion about the role of Nogo-66 or NgR. Here, we identify competitive antagonists of NgR derived from amino-terminal peptide fragments of Nogo-66. The Nogo-66(1 40) antagonist peptide (NEP1 40) blocks Nogo-66 or CNS myelin inhibition of axonal outgrowth in vitro, demonstrating that NgR mediates a significant portion of axonal outgrowth inhibition by myelin. Intrathecal administration of NEP1 40 to rats with mid-thoracic spinal cord hemisection results in significant axon growth of the corticospinal tract, and improves functional recovery. Thus, Nogo-66 and NgR have central roles in limiting axonal regeneration after CNS injury, and NEP1-40 provides a potential therapeutic agent.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned,
http://linkedlifedata.com/resource/pubmed/chemical/GPI-Linked Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
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| pubmed:status |
MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
0028-0836
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
30
|
| pubmed:volume |
417
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
547-51
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:12037567-Amino Acid Sequence,
pubmed-meshheading:12037567-Animals,
pubmed-meshheading:12037567-Axons,
pubmed-meshheading:12037567-Binding, Competitive,
pubmed-meshheading:12037567-Central Nervous System,
pubmed-meshheading:12037567-Culture Media, Conditioned,
pubmed-meshheading:12037567-Female,
pubmed-meshheading:12037567-GPI-Linked Proteins,
pubmed-meshheading:12037567-Growth Cones,
pubmed-meshheading:12037567-Molecular Sequence Data,
pubmed-meshheading:12037567-Motor Activity,
pubmed-meshheading:12037567-Myelin Proteins,
pubmed-meshheading:12037567-Myelin Sheath,
pubmed-meshheading:12037567-Nerve Regeneration,
pubmed-meshheading:12037567-Neurites,
pubmed-meshheading:12037567-Peptide Fragments,
pubmed-meshheading:12037567-Protein Structure, Tertiary,
pubmed-meshheading:12037567-Rats,
pubmed-meshheading:12037567-Rats, Sprague-Dawley,
pubmed-meshheading:12037567-Receptors, Cell Surface,
pubmed-meshheading:12037567-Spinal Cord Injuries
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| pubmed:year |
2002
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| pubmed:articleTitle |
Nogo-66 receptor antagonist peptide promotes axonal regeneration.
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| pubmed:affiliation |
Department of Neurology and Section of Neurobiology, Yale University School of Medicine, New Haven, CT 06520, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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