Evidence map›Paper›PMID 16007483›Full record

ArticleCalcified tissue international2005

Importance of phosphorylation for osteopontin regulation of biomineralization.

A Gericke, C Qin, L Spevak, Y Fujimoto, W T Butler, E S Sørensen, A L Boskey

Abstract read
In one paragraph

Article in Calcified tissue international, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
–field-weighted citation impact
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

122 citing papers in PubMed.

  1. Trial
  2. Bone matrix proteins: regulators of skeletal remodeling and repair.Journal of bone and mineral metabolism · 2026
    Review
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  16. Article
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62 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

7 authors.

A GerickeDepartment of Chemistry, Kent State University, Kent, OH, USA.
C Qin
L Spevak
Y Fujimoto
W T Butler
E S Sørensen
A L Boskey

Funding

MECHANISM OF HARD TISSUE MINERALIZATIONR01DE004141 · NIDCR · HOSPITAL FOR SPECIAL SURGERY · PI BOSKEY, ADELE L · 1985 to 2010
$4.9M
Studies of the Roles of DMP1 and DSPP in Osteogenesis and DentinogenesisR01DE005092 · NIDCR · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI QIN, CHUNLIN · 1985 to 2012
$4.4M
MECHANISM OF HARD TISSUE MINERALIZATIONR37DE004141 · NIDCR · HOSPITAL FOR SPECIAL SURGERY · PI BOSKEY, ADELE L · 1987 to 1996
–
STUDIES OF PROTEINS INVOLVED IN DENTINOGENESISR37DE005092 · NIDCR · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI BUTLER, WILLIAM T · 1987 to 1996
–
NIDCR NIH HHS DE04141NIDCR NIH HHS DE05092NIDCR NIH HHS R01 DE004141NIDCR NIH HHS R01 DE005092NIDCR NIH HHS R37 DE004141
6 · The paper itself

Abstract

Previous in vitro and in vivo studies demonstrated that osteopontin (OPN) is an inhibitor of the formation and growth of hydroxyapatite (HA) and other biominerals. The present study tests the hypotheses that the interaction of OPN with HA is determined by the extent of protein phosphorylation and that this interaction regulates the mineralization process. Bone OPN as previously reported inhibited HA formation and HA-seeded growth in a gelatin-gel system. A transglutaminase-linked OPN polymer had similar effects. Recombinant, nonphosphorylated OPN and chemically dephosphorylated OPN, had no effect on HA formation or growth in this system. In contrast, highly phosphorylated milk OPN (mOPN) promoted HA formation. The mOPN stabilized the conversion of amorphous calcium phosphate (a non-crystalline constituent of milk) to HA, whereas bone OPN had a lesser effect on this conversion. Mixtures of OPN and osteocalcin known to form a complex in vitro, unexpectedly promoted HA formation. To test the hypothesis that small alterations in protein conformation caused by phosphorylation account for the differences in the observed ability of OPN to interact with HA, the conformation of bone OPN and mOPN in the presence and absence of crystalline HA was determined by attenuated total reflection (ATR) infrared (IR) spectroscopy. Both proteins exhibited a predominantly random coil structure, which was unaffected by the addition of Ca(2+). Binding to HA did not alter the secondary structure of bone OPN, but induced a small increase of beta-sheet (few percent) in mOPN. These data taken together suggest that the phosphorylation of OPN is an important factor in regulating the OPN-mediated mineralization process.

Indexed as

AnimalsCalcification, PhysiologicCalcium PhosphatesDurapatiteFourier AnalysisOsteopontinPhosphorylationProtein Structure, SecondaryRatsRecombinant ProteinsSialoglycoproteinsamorphous calcium phosphateCalcium PhosphatesDurapatiteOsteopontinRecombinant ProteinsSialoglycoproteinsSpp1 protein, rat

Identifiers

PMID16007483
PMCPMC1451414

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.