Biochemical Interactions of the Neuronal Pentraxins

Kirkpatrick, Laura L.; Matzuk, Martin M.; Dodds, D'Nette C.; Perin, Mark S.

doi:10.1074/jbc.m002254200

Cited by 121 publications

(43 citation statements)

References 18 publications

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“…For NPR, the second and third exons were replaced with the same cassette. Constructs were electroporated into 129/SVJII-derived embryonic stem (ES) cells, and neomycin-resistant clones were isolated and screened for the expected restriction fragment length changes by genomic Southern blot as described (Kirkpatrick et al, 2000). For NP2, ES cell genomic DNA was digested with XhoI and ApaI.…”

Section: Generation Of Ko Micementioning

confidence: 99%

“…The generation of NP1 KO mice has been described previously (Kirkpatrick et al, 2000). The mouse genes for NP2 and NPR were identified, sequenced (GenBank accession numbers AF318618 and AF318076), and used to generate KO constructs.…”

Section: Generation Of Ko Micementioning

confidence: 99%

“…Four polyclonal antibodies against NP1 (raised to residues 42-57, 419 -432, 292-415, and 20 -432) , a polyclonal C-terminal antipeptide antibody to NP2 (residues 416 -429) (Hsu and Perin, 1995), and three polyclonal antibodies to NPR (residues 31-57, 472-494, and 31-494) (Dodds et al, 1997) were used as described previously (Kirkpatrick et al, 2000). In addition, an antibody to recombinant NP2 that recognizes NP1 and NP2 (residues 16 -429 of NP2) was used to detect and immunoprecipitate neuronal pentraxins.…”

Section: Antibodies Western Blotting and Immunofluorescencementioning

confidence: 99%

“…Taipoxin affinity columns were generated and used as described Kirkpatrick et al, 2000). For chromatographies of wild-type and KO tissue, 20 mouse brains [postnatal day 21 (P21) and older] were homogenized in 0.32 M sucrose.…”

Section: Affinity Chromatography and Immunoprecipitationmentioning

confidence: 99%

“…NP1, NP2, and NPR are 50% identical to each other, and their C-terminal halves are 20-30% identical to classic immune system pentraxins such as the acute phase proteins, C-reactive protein (Whitehead et al, 1990), serum amyloid P protein (Dowton and McGrew, 1990), and the long pentraxin, PTX3 (Breviario et al, 1992). Neuronal pentraxins form heteromultimers (Kirkpatrick et al, 2000). Although NP1 and NP2 are secreted when expressed alone, they can be tethered to the cell membrane when expressed as heteromultimers with NPR.…”

Section: Introductionmentioning

confidence: 99%

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Neuronal Pentraxins Mediate Synaptic Refinement in the Developing Visual System

Bjartmar

Huberman

Ullian

et al. 2006

Journal of Neuroscience

158

193

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Neuronal pentraxins (NPs) define a family of proteins that are homologous to C-reactive and acutephase proteins in the immune system and have been hypothesized to be involved in activity-dependent synaptic plasticity. To investigate the role of NPs in vivo, we generated mice that lack one, two, or all three NPs. NP1/2 knock-out mice exhibited defects in the segregation of eye-specific retinal ganglion cell (RGC) projections to the dorsal lateral geniculate nucleus, a process that involves activity-dependent synapse formation and elimination. Retinas from mice lacking NP1 and NP2 had cholinergically driven waves of activity that occurred at a frequency similar to that of wild-type mice, but several other parameters of retinal activity were altered. RGCs cultured from these mice exhibited a significant delay in functional maturation of glutamatergic synapses. Other developmental processes, such as pathfinding of RGCs at the optic chiasm and hippocampal long-term potentiation and long-term depression, appeared normal in NP-deficient mice. These data indicate that NPs are necessary for early synaptic refinements in the mammalian retina and dorsal lateral geniculate nucleus. We speculate that NPs exert their effects through mechanisms that parallel the known role of short pentraxins outside the CNS.

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Section: Generation Of Ko Micementioning

confidence: 99%

Section: Generation Of Ko Micementioning

confidence: 99%

Section: Antibodies Western Blotting and Immunofluorescencementioning

confidence: 99%

Section: Affinity Chromatography and Immunoprecipitationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Neuronal Pentraxins Mediate Synaptic Refinement in the Developing Visual System

Bjartmar

Huberman

Ullian

et al. 2006

Journal of Neuroscience

158

193

View full text Add to dashboard Cite

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The rapidly expanding CREC protein family: members, localization, function, and role in disease

2009

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Although many aspects of the physiological and pathophysiological mechanisms remain unknown, recent advances in our knowledge suggest that the CREC proteins are promising disease biomarkers or targets for therapeutic intervention in a variety of diseases. The CREC family of low affinity, Ca2+-binding, multiple EF-hand proteins are encoded by five genes, RCN1, RCN2, RCN3, SDF4, and CALU, resulting in reticulocalbin, ER Ca2+-binding protein of 55 kDa (ERC-55), reticulocalbin-3, Ca2+-binding protein of 45 kDa (Cab45), and calumenin. Alternative splicing increases the number of gene products. The proteins are localized in the cytosol, in various parts of the secretory pathway, secreted to the extracellular space or localized on the cell surface. The emerging functions appear to be highly diverse. The proteins interact with several different ligands. Rather well-described functions are attached to calumenin with the inhibition of several proteins in the endoplasmic or sarcoplasmic reticulum membrane, the vitamin K(1) 2,3-epoxide reductase, the gamma-carboxylase, the ryanodine receptor, and the Ca2+-transporting ATPase. Other functions concern participation in the secretory process, chaperone activity, signal transduction as well as participation in a large variety of disease processes.

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Neuronal pentraxin with chromo domain (NPCD) is a novel class of protein expressed in multiple neuronal domains

Chen

Bixby

2004

J of Comparative Neurology

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The receptor tyrosine phosphatase PTPRO is involved in axon guidance, but its intracellular signaling mechanisms are unknown. Signals generated through PTPRO must involve interaction of the intracellular domain with substrates and/or signaling proteins. By screening for proteins interacting with PTPRO's intracellular domain, we have identified a new class of cytoplasmic protein. This novel protein, NPCD (Neuronal Pentraxin with Chromo Domain), has multiple cytoplasmic isoforms generated by alternative splicing that are selectively expressed in neurons. These cytoplasmic NPCD isoforms are composed of a neuronal pentraxin domain (formerly thought exclusively extracellular) linked to a chromo domain (formerly thought exclusively nuclear); this protein motif organization is unprecedented. NPCD isoforms are expressed in numerous regions of the central nervous system, where they are present in distinct subcellular arrangements in different brain regions. NPCD isoforms are mainly associated with the inner side of the plasma membrane in brain neurons and rat PC12 cells in vitro; they are present in cell bodies, processes, and growth cones. The biochemical complexity and neuronal expression pattern of NPCD, together with its interaction with PTPRO, suggests involvement in multiple neuronal processes.

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Biochemical Interactions of the Neuronal Pentraxins

Cited by 121 publications

References 18 publications

Neuronal Pentraxins Mediate Synaptic Refinement in the Developing Visual System

Neuronal Pentraxins Mediate Synaptic Refinement in the Developing Visual System

The rapidly expanding CREC protein family: members, localization, function, and role in disease

Neuronal pentraxin with chromo domain (NPCD) is a novel class of protein expressed in multiple neuronal domains

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