Related Experiment Video
Updated: Mar 23, 2026

07:26
Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
Published on: April 1, 2022
2.5K
Role of PHOSPHO1 in Periodontal Development and Function
L E Zweifler1, M Ao2, M Yadav3
1Division of Biosciences, College of Dentistry, Ohio State University, Columbus, OH, USA.
Journal of Dental Research
|March 27, 2016
Summary
Orphan Phosphatase 1 (PHOSPHO1) regulates alveolar bone and cellular cementum mineralization. While acellular cementum is unaffected, PHOSPHO1 deficiency causes bone defects but preserves periodontal function.
Area of Science:
- Biochemistry
- Mineralization Biology
- Periodontal Science
Background:
- Tooth root and periodontal apparatus are vital for tooth function.
- Mineralization of cementum and bone involves enzymes and matrix proteins.
- Orphan Phosphatase 1 (PHOSPHO1) is known to initiate hydroxyapatite deposition in skeletal and dentin mineralization.
Purpose of the Study:
- To investigate the functional importance of PHOSPHO1 in periodontal tissue formation and mineralization.
- To determine if PHOSPHO1 regulates the mineralization of the periodontal apparatus.
Main Methods:
- Spatiotemporal expression mapping of PHOSPHO1 during periodontal development.
- Analysis of Phospho1(-/-) mice using histology, immunohistochemistry, in situ hybridization, radiography, and micro-computed tomography.
Main Results:
- PHOSPHO1 is expressed by osteoblasts and cementoblasts during cellular cementum formation.
- Phospho1(-/-) mice showed increased cellular cementum deposition with delayed mineralization and cementoid.
- Alveolar bone in Phospho1(-/-) mice exhibited mineralization disturbances, including unmineralized osteoid and altered osteopontin deposition.
- Acellular cementum formation and periodontal ligament (PDL) structure were unaffected.
Conclusions:
- PHOSPHO1 plays a role in the mineralization of alveolar bone and cellular cementum.
- Acellular cementum formation does not appear to be substantially regulated by PHOSPHO1.
- Despite bone mineralization defects, periodontal attachment and function remain undisturbed in the absence of PHOSPHO1.
Related Concept Videos
Phosphoinositides and PIPs
10.5K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10.5K
Phosphorylation
55.4K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
55.4K
Phosphorylation
7.9K
7.9K
Protein Kinases and Phosphatases
15.5K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.5K
Protein Kinases and Phosphatases
4.7K
4.7K
IP3/DAG Signaling Pathway
15.8K
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
15.8K

