Abstract
We have identified the first putative integral membrane pentraxin and named it neuronal pentraxin receptor (NPR). NPR is enriched by affinity chromatography on columns of a snake venom toxin, taipoxin, and columns of the taipoxin-binding proteins neuronal pentraxin 1 (NP1), neuronal pentraxin 2 (NP2), and taipoxin-associated calcium-binding protein 49 (TCBP49). The predominant form of NPR contains an putative NH2-terminal transmembrane domain and all forms of NPR are glycosylated. NPR has 49 and 48% amino acid identity to NP1 and NP2, respectively, and NPR message is expressed in neuronal regions that express NP1 and NP2. We suggest that NPR, NP1, NP2, and TCBP49 are involved in a pathway responsible for the transport of taipoxin into synapses and that this may represent a novel neuronal uptake pathway involved in the clearance of synaptic debris.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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C-Reactive Protein / chemistry*
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C-Reactive Protein / metabolism*
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Calcium-Binding Proteins / metabolism*
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Chromatography, Affinity
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Elapid Venoms / metabolism*
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In Situ Hybridization
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / metabolism
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / isolation & purification*
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Membrane Glycoproteins / metabolism
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Molecular Sequence Data
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Molecular Weight
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / metabolism*
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RNA, Messenger / metabolism
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Rats
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / isolation & purification*
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Receptors, Cell Surface / metabolism
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Sequence Alignment
Substances
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Calcium-Binding Proteins
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Elapid Venoms
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Membrane Glycoproteins
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Nerve Tissue Proteins
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RNA, Messenger
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Receptors, Cell Surface
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neuronal pentraxin
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neuronal pentraxin receptor
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taipoxin-associated calcium-binding protein 49
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taipoxin
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C-Reactive Protein
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase