Evidence map›Paper›PMID 39322833›Full record

ArticleMolecular neurobiology2025

Spinal PTP1B Regulated NMDA Receptor-mediated Nociceptive Transmission and Peripheral Inflammation-induced Pain Sensitization.

Shu-Jin Wu, Xin-Yi Lan, Yue Shi, Yan-Ni Liu, Xiao-Xi Zhang, Qi Zhang, Yu-Bo Gao, Juan Li, Xian Yang, Hu-Hu Bai

Abstract read
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Article in Molecular neurobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Shu-Jin Wu *Department of Molecular Pharmacology, School of Pharmacy, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Xin-Yi Lan *Department of Molecular Pharmacology, School of Pharmacy, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Yue Shi *Department of Molecular Pharmacology, School of Pharmacy, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Yan-Ni LiuDepartment of Molecular Pharmacology, School of Pharmacy, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Xiao-Xi ZhangDepartment of Molecular Pharmacology, School of Pharmacy, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Qi ZhangDepartment of Molecular Pharmacology, School of Pharmacy, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Yu-Bo GaoDepartment of Molecular Pharmacology, School of Pharmacy, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Juan LiDepartment of Molecular Pharmacology, School of Pharmacy, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Xian YangDepartment of Molecular Pharmacology, School of Pharmacy, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Hu-Hu BaiSchool of Life Science, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China. baihh@lzu.edu.cn.

Funding

the National Natural Science Foundation of China 32170997; 81973296; 32000703the Science and Technology Program of Gansu Province 23JRRA1106
6 · The paper itself

Abstract

Protein tyrosine phosphatases (PTPs) catalyze the dephosphorylation of several pain-related substrates in spinal cord dorsal horn and are critically involved in the modification of pain transmission. The current study demonstrated that protein tyrosine phosphatase 1B (PTP1B), a unique endoplasmic reticulum-resident member of PTP family, displayed an activity-dependent increase in its protein expression and synaptic localization in spinal dorsal horn of adult male rats. PTP1B interacted with the Src Homology 3 (SH3) domain of Synapse-Associated Protein 102 (SAP102), one of the postsynaptic scaffolding proteins that anchored PTP1B at postsynaptic sites. The SAP102-tethered PTP1B augmented the synaptic transmission mediated specifically by GluN2B subunit-containing N-methyl-D-aspartate subtype glutamate receptors. Interference with PTP1B activity or disruption of its interaction with SAP102 attenuated GluN2B-mediated nociceptive transmission and ameliorated pain sensitization induced by intraplantar injection of Complete Freund's Adjuvant. These data suggested that the activity-dependent synaptic redistribution of PTP1B served as an important mechanism regulating GluN2B receptor activity and that manipulation of PTP1B synaptic targeting might represent an effective approach for the treatment of chronic inflammatory pain.

Indexed as

InflammationNociceptionPainProtein Tyrosine Phosphatase, Non-Receptor Type 1Receptors, N-Methyl-D-AspartateSpinal CordSynaptic TransmissionAnimalsFreund's AdjuvantMaleRatsRats, Sprague-DawleyFreund's AdjuvantNR2B NMDA receptorProtein Tyrosine Phosphatase, Non-Receptor Type 1Ptpn1 protein, ratReceptors, N-Methyl-D-AspartateNMDA ReceptorPainProtein Tyrosine Phosphatase 1BSpinal cordSynapse-Associated Protein 102

Identifiers

PMID39322833

What OpenQuestion holds

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.