Evidence map›Paper›PMID 33742129›Full record

ArticleCommunications biology2021

A Vaspin-HSPA1L complex protects proximal tubular cells from organelle stress in diabetic kidney disease.

Atsuko Nakatsuka, Satoshi Yamaguchi, Jun Eguchi, Shigeru Kakuta, Yoichiro Iwakura, Hitoshi Sugiyama, Jun Wada

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. 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
1.1field-weighted citation impact, top 27% 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, 17 citations in OpenAlex.

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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

7 authors at 3 institutions in 1 country.

Atsuko NakatsukaDepartment of Nephrology, Rheumatology, Endocrinology and Metabolism, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Kita-ku, Okayama, 700-8558, Japan. atsuko-n@md.okayama-u.ac.jp.ORCID 0000-0002-3154-4073
Satoshi YamaguchiDepartment of Nephrology, Rheumatology, Endocrinology and Metabolism, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Kita-ku, Okayama, 700-8558, Japan.
Jun EguchiDepartment of Nephrology, Rheumatology, Endocrinology and Metabolism, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Kita-ku, Okayama, 700-8558, Japan.
Shigeru KakutaDepartment of Biomedical Science, Graduate School of Agricultural and Life Sciences, the University of Tokyo, Tokyo, 113-8657, Japan.
Yoichiro IwakuraResearch Institute for Biomedical Sciences, Tokyo University of Science, Chiba, 278-0022, Japan.ORCID 0000-0002-9934-5775
Hitoshi SugiyamaDepartment of Human Resource Development of Dialysis Therapy for Kidney Disease, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Kita-ku, Okayama, 700-8558, Japan.
Jun WadaDepartment of Nephrology, Rheumatology, Endocrinology and Metabolism, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Kita-ku, Okayama, 700-8558, Japan. junwada@okayama-u.ac.jp.ORCID 0000-0003-1468-5170
Okayama University · JPThe University of Tokyo · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proximal tubular cells (PTCs) are crucial for maintaining renal homeostasis, and tubular injuries contribute to progression of diabetic kidney disease (DKD). However, the roles of visceral adipose tissue-derived serine protease inhibitor (vaspin) in the development of DKD is not known. We found vaspin maintains PTCs through ameliorating ER stress, autophagy impairment, and lysosome dysfunction in DKD. Vaspin-/- obese mice showed enlarged and leaky lysosomes in PTCs associated with increased apoptosis, and these abnormalities were also observed in the patients with DKD. During internalization into PTCs, vaspin formed a complex with heat shock protein family A (Hsp70) member 1 like (HSPA1L) as well as 78 kDa glucose-regulated protein (GRP78). Both vaspin-partners bind to clathrin heavy chain and involve in the endocytosis. Notably, albumin-overload enhanced extracellular release of HSPA1L and overexpression of HSPA1L dissolved organelle stresses, especially autophagy impairment. Thus, vapsin/HSPA1L-mediated pathways play critical roles in maintaining organellar function of PTCs in DKD.

Indexed as

Endoplasmic Reticulum StressAdipokinesAnimalsApoptosisAutophagyCell LineClathrinDiabetic NephropathiesDiet, High-FatDisease Models, AnimalEndocytosisEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansInflammasomesAdipokinesClathrinEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHSPA1L protein, humanHspa1l protein, mouseHSPA5 protein, humanHspa5 protein, mouseInflammasomesSERPINA12 protein, humanSerpinsvaspin protein, mouse

Identifiers

PMID33742129
PMCPMC7979793
OpenAlexW3137343878

What OpenQuestion holds

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LicenceCC BY
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.