ArticleCells, tissues, organs2009
Studies of the DMP1 57-kDa functional domain both in vivo and in vitro.
Article in Cells, tissues, organs, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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.
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Who cites it
34 citing papers in PubMed, 55 citations in OpenAlex.
- Article
- Article
- Glycosylation of dentin matrix protein 1 is critical for fracture healing via promoting chondrogenesis.Frontiers of medicine · 2019Article
- DMP1 prevents osteocyte alterations, FGF23 elevation and left ventricular hypertrophy in mice with chronic kidney disease.Bone research · 2019Article
- Probing the influence of SIBLING proteins on collagen-I fibrillogenesis and denaturation.Connective tissue research · 2018Article
- A novel auditory ossicles membrane and the development of conductive hearing loss in Dmp1-null mice.Bone · 2017Article
- Efficacy and safety of osteoporosis medications in a rat model of late-stage chronic kidney disease accompanied by secondary hyperparathyroidism and hyperphosphatemia.Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA · 2017Article
- The LPV Motif Is Essential for the Efficient Export of Secretory DMP1 From the Endoplasmic Reticulum.Journal of cellular physiology · 2016Article
- Transgenic expression of dentin phosphoprotein inhibits skeletal development.European journal of histochemistry : EJH · 2016Article
- Constitutive nuclear expression of dentin matrix protein 1 fails to rescue the Dmp1-null phenotype.The Journal of biological chemistry · 2014Article
- The rescue of dentin matrix protein 1 (DMP1)-deficient tooth defects by the transgenic expression of dentin sialophosphoprotein (DSPP) indicates that DSPP is a downstream effector molecule of DMP1 in dentinogenesis.The Journal of biological chemistry · 2013Article
- Insights from genetic disorders of phosphate homeostasis.Seminars in nephrology · 2013Review
- Hexa-D-arginine treatment increases 7B2•PC2 activity in hyp-mouse osteoblasts and rescues the HYP phenotype.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2013Article
- Overexpression of the DMP1 C-terminal fragment stimulates FGF23 and exacerbates the hypophosphatemic rickets phenotype in Hyp mice.Molecular endocrinology (Baltimore, Md.) · 2012Article
- Dentin sialophosphoprotein and dentin matrix protein-1: Two highly phosphorylated proteins in mineralized tissues.Archives of oral biology · 2012Review
- Nuclear localization of DMP1 proteins suggests a role in intracellular signaling.Biochemical and biophysical research communications · 2012Article
- Regulation and function of the FGF23/klotho endocrine pathways.Physiological reviews · 2012Review
- Evidence for FGF23 involvement in a bone-kidney axis regulating bone mineralization and systemic phosphate and vitamin D homeostasis.Advances in experimental medicine and biology · 2012Review
- FGF23 and syndromes of abnormal renal phosphate handling.Advances in experimental medicine and biology · 2012Review
- Bone proteins PHEX and DMP1 regulate fibroblastic growth factor Fgf23 expression in osteocytes through a common pathway involving FGF receptor (FGFR) signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Dmp1-null mice and patients with mutations in dentin matrix protein 1 (DMP1) resulting in autosomal recessive hypophosphatemic rickets display similar skeletal defects. As mutations were observed in the last 18 amino acids of DMP1 in 1 subset of patients and as fragments of intact DMP1, a 37-kDa N-terminal and a 57-kDa C-terminal fragment, have been purified from bone and dentin, we hypothesized that the cleaved 57-kDa C-terminal fragment is the essential functional domain of DMP1. To test this hypothesis, different forms of recombinant DMP1 were expressed in 293EBNA, CHO and 2T3 cells. The results showed that DMP1 was processed into a 37-kDa N-terminal and a 57-kDa C-terminal fragment in vitro in all cell lines examined. DMP1 processing in CHO cells was blocked by a furin protease inhibitor, decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone, in a dose-dependent manner. Coexpression of PHEX, a potential upstream protease, had no apparent effect on DMP1 cleavage in 293EBNA cells, suggesting that PHEX may not be required for DMP1 processing. To test the in vivo role of the C-terminal fragment, transgenic mice overexpressing full-length DMP1 or the 57-kDa fragment controlled by the 3.6-kb Col1 promoter were generated. Overexpression of these transgenes had no effect on the wild-type skeleton, but on the Dmp1-null background showed expression in the osteoblast layer and throughout the bone matrix leading to the rescue of the null bone phenotype. This suggests that the 57-kDa C-terminal fragment may be able to recapitulate the function of intact DMP1 in vivo.
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