ArticleHistochemistry and cell biology2017
Immunohistochemical analysis of dentin matrix protein 1 (Dmp1) phosphorylation by Fam20C in bone: implications for the induction of biomineralization.
Article in Histochemistry and cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 44 citations in OpenAlex.
- Fam20C overexpression in odontoblasts regulates dentin formation and odontoblast differentiation.Journal of molecular histology · 2023Article
- Generation of bicistronic Dmp1-Cre knock-in mice using a self-cleaving 2A peptide.Journal of bone and mineral metabolism · 2023Article
- Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis.Journal of translational medicine · 2023Article
- Matrix Vesicle-Mediated Mineralization and Osteocytic Regulation of Bone Mineralization.International journal of molecular sciences · 2022Review
- Final irrigation protocols affect radicular dentin DMP1-CT expression, microhardness, and biochemical composition.Clinical oral investigations · 2022Article
- Self-assembly peptide PJournal of dentistry · 2022Article
- FAM20C Overview: Classic and Novel Targets, Pathogenic Variants and Raine Syndrome Phenotypes.International journal of molecular sciences · 2021Review
- A Rare Cause of Hypophosphatemia: Raine Syndrome Changing Clinical Features with Age.Calcified tissue international · 2020Article
- Two NovelGenes · 2020Article
- Multiple Modes of Vitamin K Actions in Aging-Related Musculoskeletal Disorders.International journal of molecular sciences · 2019Review
- A case of Raine syndrome presenting with facial dysmorphy and review of literature.BMC medical genetics · 2018Review
- Elevated solute transport at sites of diffuse matrix damage in cortical bone: Implications on bone repair.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2018Article
- Role of Fibroblast Growth Factor-23 in Innate Immune Responses.Frontiers in endocrinology · 2018Review
- In focus in HCB.Histochemistry and cell biology · 2017Article
- The ABCs of the atypical Fam20 secretory pathway kinases.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dmp1 is an acidic phosphoprotein that is specifically expressed in osteocytes. During the secretory process, the full-length, precursor Dmp1 is cleaved into N- and C-terminal fragments. C-terminal Dmp1 is phosphorylated, becoming a highly negatively charged domain that may assist in bone mineralization by recruiting calcium ions and influencing subsequent mineral deposition. It has been recently reported that the Golgi-localized protein kinase Fam20C phosphorylates Dmp1 in vitro. To investigate this phosphorylation in situ, we determined the locations of phosphorylated Dmp1 and Fam20C in rat bones using immunohistochemistry. During osteocytogenesis, osteoblastic, osteoid, and young osteocytes (but not old osteocytes) express Dmp1 mRNA and contain Dmp1 protein in the Golgi apparatus. These Dmp1-producing cells were distributed across the surface layer of cortical bone. Using immunofluorescence, we found that N- and C-terminal Dmp1 fragments were predominantly distributed along the lacunar walls and canaliculi of mineralized bone, respectively, but were not present in the osteoid matrix. We also found that Fam20C and its substrate, C-terminal Dmp1, colocalized in the Golgi of osteoblastic, osteoid, and young osteocytes. Furthermore, phosphorylated C-terminal Dmp1 was present in the Golgi of young osteocytes. Double-labeling immunoelectron microscopy revealed that phosphorylated C-terminal Dmp1 localized to the canalicular wall in mineralized bone. These findings suggest that C-terminal Dmp1 is phosphorylated within osteocytes and then secreted into the pericanalicular matrix of mineralized bone. Phosphorylated, negatively charged C-terminal Dmp1 in the pericanalicular matrix may play an important role in bone mineralization by recruiting calcium ions.
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