Regulation of bone-renal mineral and energy metabolism: the PHEX, FGF23, DMP1, MEPE ASARM pathway
Open accessAbstract
More than 300 million years ago, vertebrates emerged from the vast oceans to conquer gravity and the dry land. With this transition, new adaptations occurred that included ingenious changes in reproduction, waste secretion, and bone physiology. One new innovation, the egg shell, contained an ancestral protein (ovocleidin-116) that likely first appeared with the dinosaurs and was preserved through the theropod lineage in modern birds and reptiles. Ovocleidin-116 is an avian homolog of matrix extracellular phosphoglycoprotein (MEPE) and belongs to a group of proteins called short integrin-binding ligand-interacting glycoproteins (SIBLINGs). These proteins are all localized to a defined region on chromosome 5q in mice and chromosome 4q in humans. A unifying feature of SIBLING proteins is an acidic serine aspartate-rich MEPE-associated motif (ASARM). Recent research has shown that the ASARM motif and the released ASARM peptide have regulatory roles in mineralization (bone and teeth), phosphate regulation, vascularization, soft-tissue calcification, osteoclastogenesis, mechanotransduction, and fat energy metabolism. The MEPE ASARM motif and peptide are physiological substrates for PHEX, a zinc metalloendopeptidase. Defects in PHEX are responsible for X-linked hypophosphatemic rickets (HYP). There is evidence that PHEX interacts with another ASARM motif containing SIBLING protein, dentin matrix protein-1 (DMP1). DMP1 mutations cause bone and renal defects that are identical with the defects caused by a loss of PHEX function. This results in autosomal recessive hypophosphatemic rickets (ARHR). In both HYP and ARHR, increased FGF23 expression plays a major role in the disease and in autosomal dominant hypophosphatemic rickets (ADHR), FGF23 half-life is increased by activating mutations. ASARM peptide administration in vitro and in vivo also induces increased FGF23 expression. FGF23 is a member of the fibroblast growth factor (FGF) family of cytokines, which surfaced 500 million years ago with the boney fish (i.e., teleosts) that do not contain SIBLING proteins. In terrestrial vertebrates, FGF23, like SIBLING proteins, is expressed in the osteocyte. The boney fish, however, are an-osteocytic, so a physiological bone-renal link with FGF23 and the SIBLINGs was cemented when life ventured from the oceans to the land during the Triassic period, approximately 300 million years ago. This link has been revealed by recent research that indicates a competitive displacement of a PHEX-DMP1 interaction by an ASARM peptide that leads to increased FGF23 expression. This review discusses the new discoveries that reveal a novel PHEX, DMP1, MEPE, ASARM peptide, and FGF23 bone-renal pathway. This pathway impacts not only bone formation, bone-renal mineralization, and renal phosphate homeostasis but also energy metabolism. The study of this new pathway is relevant for developing therapies for several diseases: bone-teeth mineral loss disorders, renal osteodystrophy, chronic kidney disease and bone mineralization disorders (CKD-MBD), end-stage renal diseases, ectopic arterial-calcification, cardiovascular disease renal calcification, diabetes, and obesity.
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The 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 [58]
Section II says PHEX binds MEPE, and section V.A proposes that it binds DMP1. Sections III and V.A say free ASARM peptides inhibit mineralization and arise from cleavage of MEPE and related proteins. The passages do not establish the claimed mechanism that PHEX binding prevents ASARM peptide release. (LLM, conf=0.84)
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Cellular Contributors to Bone Homeostasis
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Disorders of Mineral Metabolism: Normal Homeostasis
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Mechanical loading modulates phosphate related genes in rat bone
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- Authors
- Rowe, P. S. N.
- Affiliations
- University of Kansas Medical Center (US)
- Corresponding author
- Rowe, Peter S. N.
- ORCID
- Rowe, Peter S. N.
- Venue
- Critical Reviews™ in Eukaryotic Gene Expression
- Publisher
- Begell House
- Published
- 2012
- Volume
- 22
- Issue
- 1
- Pages
- 61-86
- ISSN
- 1045-4403 (ISSN-L)
- PMC
- PMC3362997
- OpenAlex
- W2047998890
- Cited by
- 173
- References
- 196
- Citations by year
- 2026: 11 · 2025: 9 · 2024: 11 · 2023: 10 · 2022: 9 · 2021: 12 · 2020: 11 · 2019: 18 · 2018: 14 · 2017: 7 · 2016: 10 · 2015: 14 · 2014: 20 · 2013: 12 · 2012: 5
- FWCI
- 12.89
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Critical Reviews in Eukaryotic Gene Expression (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5r01ar051598-09)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01-AR051598, 5R01AR051598)
- Topics
- Health Sciences › Medicine › Nephrology › Parathyroid Disorders and Treatments
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Alkaline Phosphatase Research Studies
- Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
- Keywords
- PHEX, fibroblast growth factor 23, DMP1, MEPE, SIBLING proteins, hypophosphatemic rickets, phosphate regulation, bone mineralization, renal phosphate reabsorption, energy metabolism, osteocytes, fibroblast growth factor family, vertebrate evolution, calcinosis, osteoclastogenesis
- MeSH terms
- Fibroblast Growth Factor-23, Animals, Bone and Bones, Bone Diseases, Metabolic, Calcification, Physiologic, Diabetes Mellitus, Egg Proteins, Energy Metabolism, Female, Fibroblast Growth Factors, Glycoproteins, Humans, Kidney, Kidney Failure, Chronic, Male, Mice, Transgenic, Obesity, Osteocytes, Osteomalacia, Phosphoproteins, Chronic Kidney Disease-Mineral and Bone Disorder, Rickets, Extracellular Matrix Proteins, Hypophosphatemia, Bone Demineralization, Pathologic, Mechanotransduction, Cellular, Mice, PHEX Phosphate Regulating Neutral Endopeptidase
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