Evidence map›Paper›PMID 25398881›Full record

ArticleThe Journal of biological chemistry2015

Heat shock 70-kDa protein 5 (Hspa5) is essential for pronephros formation by mediating retinoic acid signaling.

Weili Shi, Gang Xu, Chengdong Wang, Steven M Sperber, Yonglong Chen, Qin Zhou, Yi Deng, Hui Zhao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Identification of HSPA8 as an interacting partner of MAB21L2 and an important factor in eye development.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Article
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  9. Nuclear receptor binding factor 2 (NRBF2) is required for learning and memory.Laboratory investigation; a journal of technical methods and pathology · 2020
    Article
  10. A novel c.2326G>A KIT pathogenic variant in piebaldism.American journal of translational research · 2020
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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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 7 institutions in 3 countries.

Weili ShiFrom the Key Laboratory for Regenerative Medicine, Ministry of Education, School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Hong Kong Special Administrative Region (SAR), China.
Gang XuSchool of Chinese Medicine, Hong Kong Baptist University, 7 Baptist University Road, Kowloon Tong, Hong Kong SAR, China.
Chengdong WangFrom the Key Laboratory for Regenerative Medicine, Ministry of Education, School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Hong Kong Special Administrative Region (SAR), China, Shenzhen Research Institute, The Chinese University of Hong Kong, Shenzhen 518057, China.
Steven M SperberDepartment of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, New York 10029-6574.
Yonglong ChenKey Laboratory of Regenerative Biology, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China, and.
Qin ZhouDivision of Molecular Nephrology and Creative Training Center for Undergraduates, Ministry of Education Key Laboratory of Laboratory Medicine Diagnostics, College of Laboratory Medicine, Chongqing Medical University, Chongqing 400016, China.
Yi DengDepartment of Biology, South University of Science and Technology of China, Shenzhen 518055, China, deng.y@sustc.edu.cn.
Hui ZhaoFrom the Key Laboratory for Regenerative Medicine, Ministry of Education, School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Hong Kong Special Administrative Region (SAR), China, Shenzhen Research Institute, The Chinese University of Hong Kong, Shenzhen 518057, China, zhaohui@cuhk.edu.hk.
Chinese University of Hong Kong · CNChinese Academy of Sciences · CNChinese University of Hong Kong, Shenzhen · CNChongqing Medical University · CNHong Kong Baptist University · HKIcahn School of Medicine at Mount Sinai · USSouthern University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock 70-kDa protein 5 (Hspa5), also known as binding immunoglobulin protein (Bip) or glucose-regulated protein 78 (Grp78), belongs to the heat shock protein 70 kDa family. As a multifunctional protein, it participates in protein folding and calcium homeostasis and serves as an essential regulator of the endoplasmic reticulum (ER) stress response. It has also been implicated in signal transduction by acting as a receptor or co-receptor residing at the plasma membrane. Its function during embryonic development, however, remains largely elusive. In this study, we used morpholino antisense oligonucleotides (MOs) to knock down Hspa5 activity in Xenopus embryos. In Hspa5 morphants, pronephros formation was strongly inhibited with the reduction of pronephric marker genes Lim homeobox protein 1 (lhx1), pax2, and β1 subunit of Na/K-ATPase (atp1b1). Pronephros tissue was induced in vitro by treating animal caps with all-trans-retinoic acid and activin. Depletion of Hspa5 in animal caps, however, blocked the induction of pronephros as well as reduced the expression of retinoic acid (RA)-responsive genes, suggesting that knockdown of Hspa5 attenuated RA signaling. Knockdown of Hspa5 in animal caps resulted in decreased expression of lhx1, a transcription factor directly regulated by RA signaling and essential for pronephros specification. Co-injection of Hspa5MO with lhx1 mRNA partially rescued the phenotype induced by Hspa5MO. These results suggest that the RA-Lhx1 signaling cascade is involved in Hspa5MO-induced pronephros malformation. This study shows that Hspa5, a key regulator of the unfolded protein response, plays an essential role in pronephros formation, which is mediated in part through RA signaling during early embryonic development.

Indexed as

Gene Expression Regulation, DevelopmentalAnimalsEmbryo, NonmammalianEndoplasmic Reticulum Chaperone BiPFemaleHeat-Shock ProteinsOrganogenesisPronephrosSignal TransductionTretinoinXenopus laevisXenopus ProteinsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsTretinoinXenopus ProteinsDevelopmentEmbryoEndoplasmic Reticulum Stress (ER Stress)KidneyRetinoic AcidXenopus

Identifiers

PMID25398881
PMCPMC4281759
OpenAlexW2061633348

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.