Evidence map›Paper›PMID 24799420›Full record

ArticleJournal of dental research2014

DPP and DSP are Necessary for Maintaining TGF-β1 Activity in Dentin.

Y Yamakoshi, S Kinoshita, L Izuhara, T Karakida, M Fukae, S Oida

Open access · greenAbstract read
In one paragraph

Article in Journal of dental research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-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

14 citing papers in PubMed, 24 citations in OpenAlex.

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  9. Oxidized Low-Density Lipoprotein PromotesMaterials (Basel, Switzerland) · 2020
    Article
  10. Article
  11. Article
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  13. Article
  14. TGF-β and Physiological Root Resorption of Deciduous Teeth.International journal of molecular sciences · 2016
    Article
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

6 authors at 2 institutions in 1 country.

Y YamakoshiDepartment of Biochemistry and Molecular Biology, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230-8501, Japan yamakoshi-y@tsurumi-u.ac.jp.
S KinoshitaDepartment of Pediatric Dentistry, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230-8501, Japan.
L IzuharaDivision of Regenerative Medicine, The Jikei University School of Medicine, 3-25-8 Nishishinbashi, Minato-ku, Tokyo 105-0003, Japan.
T KarakidaDepartment of Biochemistry and Molecular Biology, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230-8501, Japan.
M FukaeDepartment of Biochemistry and Molecular Biology, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230-8501, Japan.
S OidaDepartment of Biochemistry and Molecular Biology, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230-8501, Japan.
Tsurumi University · JPJikei University School of Medicine · JP

Funding

Structural and Functional Analysis of Dentin ProteinsR01DE018020 · NIDCR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SIMMER, JAMES P · 2008 to 2012
$1.7M
NIDCR NIH HHS DE018020NIDCR NIH HHS R01 DE018020
6 · The paper itself

Abstract

Porcine dentin sialophosphoprotein (DSPP) is the most abundant non-collagenous protein in dentin. It is processed by proteases into 3 independent proteins: dentin sialoprotein (DSP), dentin glycoprotein (DGP), and dentin phosphoprotein (DPP). We fractionated DPP and DSP along with TGF-β activity by ion exchange (IE) chromatography from developing pig molars and measured their alkaline phosphatase (ALP)-stimulating activity in human periodontal (HPDL) cells with or without TGF-β receptor inhibitor. We then purified TGF-β-unbound or -bound DPP and DSP by reverse-phase high-performance liquid chromatography (RP-HPLC) using the ALP-HPDL system. The TGF-β isoform bound to DPP and DSP was identified as being TGF-β1 by both ELISA and LC-MS/MS analysis. We incubated carrier-free human recombinant TGF-β1 (CF-hTGF-β1) with TGF-β-unbound DPP or DSP and characterized the binding on IE-HPLC using the ALP-HPDL system. When only CF-hTGF-β1 was incubated, approximately 3.6% of the ALP-stimulating activity remained. DPP and DSP rescued the loss of TGF-β1 activity. Approximately 19% and 10% of the ALP stimulating activities were retained by the binding of TGF-β to DPP and DSP, respectively. The type I collagen infrequently bound to CF-hTGF-β1. We conclude that both DPP and DSP help retain TGF-β1 activity in porcine dentin.

Indexed as

Alkaline PhosphataseAnimalsCells, CulturedChromatography, Ion ExchangeChromatography, LiquidChromatography, Reverse-PhaseDentinDentin SialophosphoproteinExtracellular Matrix ProteinsHumansPeriodontal LigamentPhosphoproteinsProtein BindingProtein IsoformsReceptors, Transforming Growth Factor betaRecombinant ProteinsAlkaline PhosphataseDentin SialophosphoproteinExtracellular Matrix ProteinsPhosphoproteinsProtein IsoformsReceptors, Transforming Growth Factor betaRecombinant ProteinsSialoglycoproteinsTransforming Growth Factor beta1cell cultureextracellular matrix (ECM)HPLCisolation and purificationphosphophoryntooth

Identifiers

PMID24799420
PMCPMC4107551
OpenAlexW2044394933

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.