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Neuronal Pentraxin Receptor, a Novel Putative Integral Membrane Pentraxin That Interacts with Neuronal Pentraxin 1 and 2 and Taipoxin-associated Calcium-binding Protein 49
Open accessAbstract
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.
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“The complex can also interact with NPTXR, which is anchored in the post-synaptic membrane through its N-terminal domain (Dodds et al. 1997)”
From Neuronal pentraxins as biomarkers of synaptic activity: from physiological functions to pathological changes in neurodegeneration (2022) · cites this paper as Dodds et al. 1997
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“clearance of synaptic debris and toxins from neurons (Dodds et al. 1997)”
From Neuronal pentraxins as biomarkers of synaptic activity: from physiological functions to pathological changes in neurodegeneration (2022) · cites this paper as Dodds et al. 1997
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Metadata
- Authors
- Dodds, D. C., Omeis, I. A., Cushman, S. J., Helms, J. A., & Perin, M. S.
- Affiliations
- Baylor College of Medicine (US)
- University of California, San Francisco (US)
- Corresponding author
- Perin, Mark S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-08
- Volume
- 272
- Issue
- 34
- Pages
- 21488-21494
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2162193325
- Cited by
- 170
- References
- 26
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 6 · 2023: 1 · 2022: 5 · 2021: 6 · 2020: 18 · 2019: 2 · 2018: 5 · 2017: 4 · 2016: 3 · 2015: 5 · 2014: 7 · 2013: 5 · 2012: 3
- FWCI
- 2.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Biomarkers in Disease Mechanisms
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Venomous Animal Envenomation and Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Keywords
- NPTX2, taipoxin, transmembrane domain, glycosylation, snake venom toxins, protein-protein interaction, neuronal expression
- MeSH terms
- Pentraxins, Amino Acid Sequence, Animals, Base Sequence, C-Reactive Protein, Calcium-Binding Proteins, Chromatography, Affinity, Elapid Venoms, Membrane Glycoproteins, Molecular Sequence Data, Molecular Weight, Nerve Tissue Proteins, Receptors, Cell Surface, RNA, Messenger, Sequence Alignment, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, In Situ Hybridization, Rats
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