Evidence map›Paper›PMID 26634432›Full record

ArticleScientific reports2015

Glycosylation of Dentin Matrix Protein 1 is critical for osteogenesis.

Yao Sun, Yuteng Weng, Chenyang Zhang, Yi Liu, Chen Kang, Zhongshuang Liu, Bo Jing, Qi Zhang, Zuolin Wang

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Regulation of Glycosylation in Bone Metabolism.International journal of molecular sciences · 2024
    Review
  2. Article
  3. Article
  4. Article
  5. The role of proteoglycan form of DMP1 in cranial repair.BMC molecular and cell biology · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. The Role of DMP1 in CKD-MBD.Current osteoporosis reports · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Bone and heart health in chronic kidney disease: role of dentin matrix protein 1.Current opinion in nephrology and hypertension · 2019
    Review
  16. 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

9 authors.

Yao SunTongji University, School of Stomatology, Laboratory of oral biomedical science and translational medicine, Shanghai, China, 200072.
Yuteng WengTongji University, School of Stomatology, Laboratory of oral biomedical science and translational medicine, Shanghai, China, 200072.
Chenyang ZhangTongji University, School of Stomatology, Laboratory of oral biomedical science and translational medicine, Shanghai, China, 200072.
Yi LiuTongji University, School of Stomatology, Laboratory of oral biomedical science and translational medicine, Shanghai, China, 200072.
Chen KangHarbin Medical University, Institute of Hard Tissue Development and Regeneration, Harbin, China, 150086.
Zhongshuang LiuTongji University, School of Stomatology, Laboratory of oral biomedical science and translational medicine, Shanghai, China, 200072.
Bo JingTongji University, School of medicine, stem cell center, Shanghai, China, 200072.
Qi ZhangTongji University, School of Stomatology, Laboratory of oral biomedical science and translational medicine, Shanghai, China, 200072.
Zuolin WangTongji University, School of Stomatology, Laboratory of oral biomedical science and translational medicine, Shanghai, China, 200072.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteoglycans play important roles in regulating osteogenesis. Dentin matrix protein 1 (DMP1) is a highly expressed bone extracellular matrix protein that regulates both bone development and phosphate metabolism. After glycosylation, an N-terminal fragment of DMP1 protein was identified as a new proteoglycan (DMP1-PG) in bone matrix. In vitro investigations showed that Ser(89) is the key glycosylation site in mouse DMP1. However, the specific role of DMP1 glycosylation is still not understood. In this study, a mutant DMP1 mouse model was developed in which the glycosylation site S(89) was substituted with G(89) (S89G-DMP1). The glycosylation level of DMP1 was down-regulated in the bone matrix of S89G-DMP1 mice. Compared with wild type mice, the long bones of S89G-DMP1 mice showed developmental changes, including the speed of bone remodeling and mineralization, the morphology and activities of osteocytes, and activities of both osteoblasts and osteoclasts. These findings indicate that glycosylation of DMP1 is a key posttranslational modification process during development and that DMP1-PG functions as an indispensable proteoglycan in osteogenesis.

Indexed as

GlycosylationAnimalsBone MatrixExtracellular Matrix ProteinsGene Expression Regulation, DevelopmentalMiceOsteoblastsOsteogenesisDmp1 protein, mouseExtracellular Matrix Proteins

Identifiers

PMID26634432
PMCPMC4669440

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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.