Evidence map›Paper›PMID 19940141›Full record

ArticleThe Journal of biological chemistry2010

ADAMTSL-6 is a novel extracellular matrix protein that binds to fibrillin-1 and promotes fibrillin-1 fibril formation.

Ko Tsutsui, Ri-ichiroh Manabe, Tomiko Yamada, Itsuko Nakano, Yasuko Oguri, Douglas R Keene, Gerhard Sengle, Lynn Y Sakai, Kiyotoshi Sekiguchi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 12% 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

76 citing papers in PubMed, 1 synthesis or guideline pooled it, 113 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Physiology (Bethesda, Md.) · 2026
    Review
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  5. Article
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  7. Article
  8. A triterpene-enriched natural extract fromPharmaceutical biology · 2025
    Article
  9. Article
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  11. Article
  12. Article
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  14. Article
  15. Pathogens (Basel, Switzerland) · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

16 more citing papers are in PubMed but not listed here.

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

9 authors at 3 institutions in 2 countries.

Ko TsutsuiSekiguchi Biomatrix Signaling Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, Aichi Medical University, Nagakute, Aichi 480-1195, Japan.
Ri-ichiroh Manabe
Tomiko Yamada
Itsuko Nakano
Yasuko Oguri
Douglas R Keene
Gerhard Sengle
Lynn Y Sakai
Kiyotoshi Sekiguchi
Aichi Medical University · JPShriners Hospitals for Children - Erie · USOregon Health & Science University · US

Funding

PROJECT 4: Exploration of Therapeutic Strategies in MarP01AR049698 · NIAMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI RAMIREZ, FRANCESCO B · 2004 to 2014
$13.9M
NIAMS NIH HHS P01 AR049698NIAMS NIH HHS P01AR049698
6 · The paper itself

Abstract

ADAMTS (A disintegrin and metalloproteinase with thrombospondin motifs)-like (ADAMTSL) proteins, a subgroup of the ADAMTS superfamily, share several domains with ADAMTS proteinases, including thrombospondin type I repeats, a cysteine-rich domain, and an ADAMTS spacer, but lack a catalytic domain. We identified two new members of ADAMTSL proteins, ADAMTSL-6alpha and -6beta, that differ in their N-terminal amino acid sequences but have common C-terminal regions. When transfected into MG63 osteosarcoma cells, both isoforms were secreted and deposited into pericellular matrices, although ADAMTSL-6alpha, in contrast to -6beta, was barely detectable in the conditioned medium. Immunolabeling at the light and electron microscopic levels showed their close association with fibrillin-1-rich microfibrils in elastic connective tissues. Surface plasmon resonance analyses demonstrated that ADAMTSL-6beta binds to the N-terminal half of fibrillin-1 with a dissociation constant of approximately 80 nm. When MG63 cells were transfected or exogenously supplemented with ADAMTSL-6, fibrillin-1 matrix assembly was promoted in the early but not the late stage of the assembly process. Furthermore, ADAMTSL-6 transgenic mice exhibited excessive fibrillin-1 fibril formation in tissues where ADAMTSL-6 was overexpressed. All together, these results indicated that ADAMTSL-6 is a novel microfibril-associated protein that binds directly to fibrillin-1 and promotes fibrillin-1 matrix assembly.

Indexed as

AdipokinesAmino Acid SequenceAnimalsAnimals, NewbornBlotting, SouthernCartilageCell LineEmbryo, MammalianExtracellular Matrix ProteinsFibrillin-1FibrillinsGlycoproteinsImmunoblottingImmunohistochemistryMiceMice, Inbred C57BLAdipokinesExtracellular Matrix ProteinsFbn1 protein, mouseFibrillin-1FibrillinsGlycoproteinsMicrofilament Proteins

Identifiers

PMID19940141
PMCPMC2836092
OpenAlexW2066748421

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.