Degradation of MEPE, DMP1, and release of SIBLING ASARM-Peptides (Minhibins): ASARM-Peptide(s) are directly responsible for defective mineralization in HYP
Open accessAbstract
Mutations in PHEX (phosphate-regulating gene with homologies to endopeptidases on the X chromosome) and DMP1 (dentin matrix protein 1) result in X-linked hypophosphatemic rickets (HYP) and autosomal-recessive hypophosphatemic-rickets (ARHR), respectively. Specific binding of PHEX to matrix extracellular phosphoglycoprotein (MEPE) regulates the release of small protease-resistant MEPE peptides [acidic serine- and aspartate-rich MEPE-associated motif (ASARM) peptides]. ASARM peptides are potent inhibitors of mineralization (minhibins) that also occur in DMP1 [MEPE-related small integrin-binding ligand, N-linked glycoprotein (SIBLING) protein]. It is not known whether these peptides are directly responsible for the mineralization defect. We therefore used a bone marrow stromal cell (BMSC) coculture model, ASARM peptides, anti-ASARM antibodies, and a small synthetic PHEX peptide (SPR4; 4.2 kDa) to examine this. Surface plasmon resonance (SPR) and two-dimensional 1H/15N nuclear magnetic resonance demonstrated specific binding of SPR4 peptide to ASARM peptide. When cultured individually for 21 d, HYP BMSCs displayed reduced mineralization compared with wild type (WT) (−87%, P < 0.05). When cocultured, both HYP and WT cells failed to mineralize. However, cocultures (HYP and WT) or monocultures of HYP BMSCs treated with SPR4 peptide or anti-ASARM neutralizing antibodies mineralized normally. WT BMSCs treated with ASARM peptide also failed to mineralize properly without SPR4 peptide or anti-ASARM neutralizing antibodies. ASARM peptide treatment decreased PHEX mRNA and protein (−80%, P < 0.05) and SPR4 peptide cotreatment reversed this by binding ASARM peptide. SPR4 peptide also reversed ASARM peptide-mediated changes in expression of key osteoclast and osteoblast differentiation genes. Western blots of HYP calvariae and BMSCs revealed massive degradation of both MEPE and DMP1 protein compared with the WT. We conclude that degradation of MEPE and DMP-1 and release of ASARM peptides are chiefly responsible for the HYP mineralization defect and changes in osteoblast-osteoclast differentiation.
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MEPE exerts an inhibitory effect on mineralization through direct interaction with hydroxyapatite crystal surfaces.
“MEPE exerts an inhibitory effect on mineralization through direct interaction with hydroxyapatite crystal surfaces 44,45 .”
From Sex-specific gene expression signatures of calcific aortic valve stenosis in a large collection of human tissues (2026) · cites this paper as [44]
The Discussion (page unavailable) says ASARM peptides released from MEPE inhibit mineralization and likely do so partly by binding directly to hydroxyapatite crystals. It does not establish that intact MEPE itself binds those surfaces, and it presents crystal binding as a likely mechanism rather than a demonstrated one. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe PHEX protein binds to MEPE and DMP1, preventing the release of the ASARM peptide that inhibits mineralization.
“The encoded protein binds to MEPE and DMP1, preventing the release of the ASARM peptide that inhibits mineralization 44,45,58,59 .”
From Sex-specific gene expression signatures of calcific aortic valve stenosis in a large collection of human tissues (2026) · cites this paper as [44]
The Abstract (page not provided) says PHEX binds MEPE and that this interaction prevents cathepsin B-mediated release of ASARM peptide. The Discussion says ASARM peptides inhibit mineralization, but treats PHEX–DMP1 binding as a question for future experiments rather than an established interaction. Thus the claim is supported for MEPE, not DMP1. (LLM, conf=0.90)
Experimental — accuracy not yet measuredDMP1 and MEPE belong to the SIBLING protein family, which plays a central role in the mineralization of bone and dentin, possibly through a shared acidic serine aspartate-rich MEPE-associated motif.
“DMP1 (Dentin Matrix Protein 1) and MEPE (Matrix Extracellular Phosphoglycoprotein) belong to the SIBLING (Small Integrin-Binding LIgand, N-linked Glycoprotein) protein family, which plays a central role in the mineralization of bone and dentin, possibly through a shared acidic serine aspartate-rich MEPE-associated motif (ASARM) 36,37 .”
From Sex-specific gene expression signatures of calcific aortic valve stenosis in a large collection of human tissues (2026) · cites this paper as [37]
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Research works printed but not linked: 2
- Addison WN, Nakano Y, Crine P, Rowe PS, McKee MD 2007 Regulation of mineralization by phosphorylated MEPE-ASARM peptide in MC3T3-E1 os- teoblast cultures. Bone 40:S222-S222
- Rowe PS, Hedge A, Schwarz P, Addison WN, McKee MD 2006 MEPE ASARM peptide(s) bind to PHEX protein, PHEX Zn-motif peptide(s) and hydroxyapatite, and inhibit mineralization of MC3T3-E1 osteoblast cultures. J Bone Miner Res 21:S11-S11
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- Authors
- Martin, A., David, V., Laurence, J. S., Schwarz, P. M., Lafer, E. M., Hedge, A.-M., & Rowe, P. S. N.
- Affiliations
- University of Kansas Medical Center (US)
- University of Kansas (US)
- The University of Texas at San Antonio Health Science Center (US)
- Corresponding author
- Rowe, Peter S. N.
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2007-12-27
- Volume
- 149
- Issue
- 4
- Pages
- 1757-1772
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- PMC
- PMC2276704
- OpenAlex
- W2143120521
- Cited by
- 173
- References
- 61
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 1 · 2023: 7 · 2022: 5 · 2021: 10 · 2020: 11 · 2019: 4 · 2018: 9 · 2017: 8 · 2016: 6 · 2015: 12 · 2014: 10 · 2013: 11 · 2012: 18
- FWCI
- 9.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Endocrinology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- KU ScholarWorks (University of Kansas) (submittedVersion, other-oa)
- Funders
- National Institutes of Health (5r01ar051598-09, CA54174)
- University of Texas Health Science Center at San Antonio (CA54174)
- National Cancer Institute (P30CA054174, CA-54174)
- National Institute of Neurological Disorders and Stroke (R01NS029051)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R0-1-AR51598-01, R01-AR051598)
- Topics
- Health Sciences › Medicine › Nephrology › Parathyroid Disorders and Treatments
- Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Alkaline Phosphatase Research Studies
- Keywords
- X-linked hypophosphatemic rickets, MEPE, DMP1, PHEX, bone mineralization defect, mesenchymal stem cells, peptide-peptide binding, osteogenic differentiation, osteoclastogenesis, phosphate regulation
- MeSH terms
- Fibroblast Growth Factor-23, Amino Acid Sequence, Animals, Calcification, Physiologic, Fibroblast Growth Factors, Glycoproteins, Male, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Osteoclasts, Phosphoproteins, Extracellular Matrix Proteins, Surface Plasmon Resonance, Amino Acid Motifs, Genetic Diseases, X-Linked, Mice, Familial Hypophosphatemic Rickets, PHEX Phosphate Regulating Neutral Endopeptidase
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