Evidence map›Paper›PMID 36884214›Full record

ArticleNeuroscience bulletin2023

Neuroglobin Facilitates Neuronal Oxygenation through Tropic Migration under Hypoxia or Anemia in Rat: How Does the Brain Breathe?

Chun-Yang Li, Hai-Feng Jiang, Li Li, Xiao-Jing Lai, Qian-Rong Liu, Shang-Bin Yu, Cheng-La Yi, Xiao-Qian Chen

Open access · greenAbstract read
In one paragraph

Article in Neuroscience bulletin, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.7field-weighted citation impact, top 18% of its field
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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Observational
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

8 authors at 3 institutions in 1 country.

Chun-Yang Li *Department of Pathophysiology, Tongji Medical College; Key Laboratory of Neurological Diseases, The Ministry of Education (HUST), Huazhong University of Science and Technology, Wuhan, 430030, China.
Hai-Feng Jiang *Department of Pathophysiology, Tongji Medical College; Key Laboratory of Neurological Diseases, The Ministry of Education (HUST), Huazhong University of Science and Technology, Wuhan, 430030, China.ORCID https://orcid.org/0000-0003-3338-4808
Li LiDepartment of Pathophysiology, Tongji Medical College; Key Laboratory of Neurological Diseases, The Ministry of Education (HUST), Huazhong University of Science and Technology, Wuhan, 430030, China.
Xiao-Jing LaiSchool of Life Science and Technology, Wuhan Polytechnic University, Wuhan, 430023, China.
Qian-Rong LiuDepartment of Pathophysiology, Tongji Medical College; Key Laboratory of Neurological Diseases, The Ministry of Education (HUST), Huazhong University of Science and Technology, Wuhan, 430030, China.
Shang-Bin YuDepartment of Pathophysiology, Tongji Medical College; Key Laboratory of Neurological Diseases, The Ministry of Education (HUST), Huazhong University of Science and Technology, Wuhan, 430030, China.
Cheng-La YiDepartment of Traumatic Surgery, Tong-ji Hospital, Tong-ji Medical College, Huazhong University of Science and Technology, Wuhan, 430030, China. chenglayi@163.com.
Xiao-Qian ChenDepartment of Pathophysiology, Tongji Medical College; Key Laboratory of Neurological Diseases, The Ministry of Education (HUST), Huazhong University of Science and Technology, Wuhan, 430030, China. chenxq@mails.tjmu.edu.cn.ORCID http://orcid.org/0000-0002-2673-2977
Huazhong University of Science and Technology · CNTongji Hospital · CNWuhan Polytechnic University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The discovery of neuroglobin (Ngb), a brain- or neuron-specific member of the hemoglobin family, has revolutionized our understanding of brain oxygen metabolism. Currently, how Ngb plays such a role remains far from clear. Here, we report a novel mechanism by which Ngb might facilitate neuronal oxygenation upon hypoxia or anemia. We found that Ngb was present in, co-localized to, and co-migrated with mitochondria in the cell body and neurites of neurons. Hypoxia induced a sudden and prominent migration of Ngb towards the cytoplasmic membrane (CM) or cell surface in living neurons, and this was accompanied by the mitochondria. In vivo, hypotonic and anemic hypoxia induced a reversible Ngb migration toward the CM in cerebral cortical neurons in rat brains but did not alter the expression level of Ngb or its cytoplasm/mitochondria ratio. Knock-down of Ngb by RNA interference significantly diminished respiratory succinate dehydrogenase (SDH) and ATPase activity in neuronal N2a cells. Over-expression of Ngb enhanced SDH activity in N2a cells upon hypoxia. Mutation of Ngb at its oxygen-binding site (His

Indexed as

AnemiaGlobinsAdenosine TriphosphatasesAnimalsBrainHypoxiaNerve Tissue ProteinsNeuroglobinNeuronsOxygenRatsAdenosine TriphosphatasesGlobinsNerve Tissue ProteinsNeuroglobinOxygenAnemiaAstrocyteHypoxiaIschemiaNeuroglobinNeuron

Identifiers

PMID36884214
PMCPMC10533768
OpenAlexW4323531385

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.