Dentin matrix acidic phosphoprotein is an extracellular matrix protein and a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family (other members being DSPP, IBSP, MEPE, and SPP1). This protein, which is critical for proper mineralization of bone and dentin, is present in diverse cells of bone and tooth tissues. The protein contains a large number of acidic domains, multiple phosphorylation sites, a functional Arg-Gly-Asp cell attachment sequence, and a DNA binding domain. In undifferentiated osteoblasts it is primarily a nuclear protein that regulates the expression of osteoblast-specific genes. During osteoblast maturation the protein becomes phosphorylated and is exported to the extracellular matrix, where it orchestrates mineralized matrix formation. Mutations in the gene are known to cause autosomal recessivehypophosphatemia, a disease that manifests as rickets and osteomalacia. The gene structure is conserved in mammals. Two transcript variants encoding different isoforms have been described for this gene.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Aplin HM, Hirst KL, Crosby AH, Dixon MJ (Mar 1996). "Mapping of the human dentin matrix acidic phosphoprotein gene (DMP1) to the dentinogenesis imperfecta type II critical region at chromosome 4q21". Genomics. 30 (2): 347–9. doi:10.1006/geno.1995.9867. PMID8586437.
^Hirst KL, Simmons D, Feng J, Aplin H, Dixon MJ, MacDougall M (Jul 1997). "Elucidation of the sequence and the genomic organization of the human dentin matrix acidic phosphoprotein 1 (DMP1) gene: exclusion of the locus from a causative role in the pathogenesis of dentinogenesis imperfecta type II". Genomics. 42 (1): 38–45. doi:10.1006/geno.1997.4700. PMID9177774.
J.O. MANCERA1, T. JHALA2, S. WANG2, C. QIN2, R. D'SOUZA2, and Y. LU2, 1School of Dentistry, Meharry Medical College, Nashville, TN, 2Department of Biomedical Sciences, Texas A&M Health Science Center, Baylor College of Dentistry, Dallas, TX
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Chen S, Inozentseva-Clayton N, Dong J, et al. (2005). "Binding of two nuclear factors to a novel silencer element in human dentin matrix protein 1 (DMP1) promoter regulates the cell type-specific DMP1 gene expression". J. Cell. Biochem. 92 (2): 332–49. doi:10.1002/jcb.20051. PMID15108359. S2CID31421133.