Evidence map›Paper›PMID 30002123›Full record

ArticleThe Journal of biological chemistry2018

The endoplasmic reticulum-resident collagen chaperone Hsp47 interacts with and promotes the secretion of decorin, fibromodulin, and lumican.

Yoshihiro Ishikawa, Kristofer Rubin, Hans Peter Bächinger, Sebastian Kalamajski

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
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  5. Mechanisms of assembly and remodelling of the extracellular matrix.Nature reviews. Molecular cell biology · 2024
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  16. The role of collagen in cancer: from bench to bedside.Journal of translational medicine · 2019
    Review
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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

4 authors at 2 institutions in 2 countries.

Yoshihiro IshikawaFrom the Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97239.
Kristofer Rubinthe Department for Medical Biochemistry and Microbiology, Uppsala University, Uppsala 75237, Sweden.
Hans Peter BächingerFrom the Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97239.
Sebastian Kalamajskithe Department for Medical Biochemistry and Microbiology, Uppsala University, Uppsala 75237, Sweden sebastian.kalamajski@imbim.uu.se.
Oregon Health & Science University · USUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The build-up of diversified and tissue-specific assemblies of extracellular matrix (ECM) proteins depends on secreted and cell surface-located molecular arrays that coordinate ECM proteins into discrete designs. The family of small leucine-rich proteins (SLRPs) associates with and dictates the structure of fibrillar collagens, which form the backbone of most ECM types. However, whether SLRPs form complexes with proteins other than collagens is unclear. Here, we demonstrate that heat shock protein 47 (Hsp47), a well-established endoplasmic reticulum-resident collagen chaperone, also binds the SLRPs decorin, lumican, and fibromodulin with affinities comparable with that in the Hsp47-type I collagen interaction. Furthermore, we show that a lack of Hsp47 inhibits the cellular secretion of decorin and lumican. Our results expand the understanding of the concerted molecular interactions that control the secretion and organization of a functional collagenous ECM.

Indexed as

Protein Interaction MapsAnimalsCell LineCollagen Type IDecorinEndoplasmic ReticulumFibromodulinHSP47 Heat-Shock ProteinsHumansLumicanMiceNIH 3T3 CellsCollagen Type IDecorinFibromodulinHSP47 Heat-Shock ProteinsLumicanchaperonecollagendecorinendoplasmic reticulum (ER)extracellular matrixfibromodulinheat shock protein (HSP)Hsp47lumicanprotein-protein interactionprotein secretionsmall leucine-rich proteinsmall leucine-rich proteoglycan (SLRP)

Identifiers

PMID30002123
PMCPMC6120207
OpenAlexW2838287174

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.