Abstract
We have identified, by affinity chromatography, a binding protein for the snake venom toxin taipoxin. The sequence of this 47 kDa protein is unique, is characteristic of a secreted protein, and has homology to the acute phase proteins serum amyloid P protein and C-reactive protein of the pentraxin family. We have named this protein neuronal pentraxin (NP), as Northern analysis and in situ hybridization demonstrate high message levels in neurons of cerebellum, hippocampus, and cerebral cortex. Because NP may be released synaptically and has homology to immune proteins potentially involved in uptake of lipidic, toxic, or other antigenic material, we suggest that NP may be involved in a general uptake of synaptic macromolecules.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Brain / metabolism*
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C-Reactive Protein / analysis
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C-Reactive Protein / biosynthesis*
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C-Reactive Protein / chemistry*
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Cerebellum / metabolism
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Chromatography, Affinity
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Cloning, Molecular
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Elapid Venoms / metabolism
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Elapid Venoms / toxicity
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In Situ Hybridization
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Molecular Sequence Data
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Molecular Weight
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Nerve Tissue Proteins / analysis
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Nerve Tissue Proteins / biosynthesis*
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Nerve Tissue Proteins / chemistry
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Neuroglia / drug effects
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Neuromuscular Blocking Agents / metabolism
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Neurons / metabolism*
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Organ Specificity
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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RNA, Messenger / analysis
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RNA, Messenger / biosynthesis
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Rats
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Sequence Homology, Amino Acid
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Serum Amyloid P-Component / chemistry*
Substances
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Elapid Venoms
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Nerve Tissue Proteins
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Neuromuscular Blocking Agents
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Peptide Fragments
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RNA, Messenger
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Recombinant Proteins
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Serum Amyloid P-Component
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neuronal pentraxin
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taipoxin
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C-Reactive Protein