Abstract
Biomineralization is a widespread process in living organisms to form minerals to harden tissues via hierarchically structured organic−inorganic composites. These processes are very diverse and complex. However, the site-specific location, size, and morphology of the crystals formed are specifically controlled by various cellular activities that vary between organisms. In vertebrates, bone, cartilage, and teeth are calcified tissues that are essential for the functional and structural integrity of the organism. The composition, crystal morphology, and materials properties of these structural elements are intriguing to multidisciplinary scientists. Further, the simplicity of biomineralization process with low energy costs, high quality, and formation under ambient conditions are impossible to reproduce in a bio-free system. Studies have implicated that the organic component of the mineralized tissues which include collagen and non-collagenous proteins (NCPs) play a critical role in mineral nucleation and growth. In this review, we highlight recent developments in dentin biomineralization process with respect to matrix proteins and growth factors.
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Allam L, Ghrifi F, Mohammed H, El Hafidi N, El Jaoudi R, El Harti J, Lmimouni B, Belyamani L, Ibrahimi A (2020) Targeting the GRP78-Dependant SARS-CoV-2 cell entry by peptides and small molecules. Bioinformatics and Biology Insights 14:117793222096550. https://doi.org/10.1177/1177932220965505
Alvares K, Veis A (2012) Commentary on “biomineralization--an active or passive process?”. Connect Tissue Res 53:437
Angker L, Nockolds C, Swain MV, Kilpatrick N (2004) Correlating the mechanical properties to the mineral content of carious dentine--a comparative study using an ultra-micro indentation system (UMIS) and SEM-BSE signals. Arch Oral Biol 49(5):369–378. https://doi.org/10.1016/j.archoralbio.2003.12.005
Aono A, Hazama M, Notoya K, Taketomi S, Yamasaki H, Tsukuda R, Sasaki S, Fujisawa Y (1995) Potent ectopic bone-inducing activity of bone morphogenetic protein-4/7 heterodimer. Biochem Biophys Res Commun 210:670–677
Asano K, Kinzy TG, Merrick WC, Hershey JW (1997) Conservation and diversity of eukaryotic translation initiation factor eIF3. J Biol Chem 272:1101–1109
Bahar E, Kim H, Yoon H (2016) ER stress-mediated signaling: action potential and Ca2+ as key players. Int J Mol Sci 17(9):1558. MDPI AG. https://doi.org/10.3390/ijms17091558
Balemans W, Van Hul W (2002) Extracellular regulation of BMP signaling in vertebrates: a cocktail of modulators. Dev Biol 250:231–250
Behlke J, Bommer UA, Lutsch G, Henske A, Bielka H (1986) Structure of initiation factor eIF-3 from rat liver. Hydrodynamic and electron microscopic investigations. Eur J Biochem 157:523–530
Beniash E, Deshpande AS, Fang PA, Lieb NS, Zhang X, Sfeir CS (2011) Possible role of DMP1 in dentin mineralization. J Struct Biol 174:100–106
Boskey AL (1989) Noncollagenous matrix proteins and their role in mineralization. Bone Miner 6:111–123
Boskey AL (1990) Bone mineral and matrix. Are they altered in osteoporosis? Orthop Clin North Am 21:19–29
Boskey AL (1992) Mineral-matrix interactions in bone and cartilage. Clin Orthop Relat Res 281:244–274
Boskey AL (1998) Biomineralization: conflicts, challenges, and opportunities. J Cell Biochem Suppl 30–31:83–91
Boskey AL (2003a) Biomineralization: an overview. Connect Tissue Res 44(Suppl 1):5–9
Boskey AL (2003b) Mineral analysis provides insights into the mechanism of biomineralization. Calcif Tissue Int 72:533–536
Boskey AL (2013) Bone composition: relationship to bone fragility and antiosteoporotic drug effects. Bonekey Rep 2:447
Boskey AL, Villarreal-Ramirez E (2016) Intrinsically disordered proteins and biomineralization. Matrix Biol 52–54:43–59
Calvo MB, Fernández VB, Villaamil VM, Gallego GA, Prado SD, Pulido EG (2009) Biology of BMP signalling and cancer. Clin Transl Oncol 11:126–137
Chen Y, George A (2018) TRIP-1 promotes the assembly of an ECM that contains extracellular vesicles and factors that modulate angiogenesis. Front Physiol 9:1092
Chen J, Shapiro HS, Sodek J (1992) Developmental expression of bone sialoprotein mRNA in rat mineralized connective tissues. J Bone Miner Res 7(8):987–997. https://doi.org/10.1002/jbmr.5650070816
Chen RH, Miettinen PJ, Maruoka EM, Choy L, Derynck R (1995) A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor. Nature 377:548–552
Conner C, Lager TW, Guldner IH, Wu MZ, Hishida Y, Hishida T, Ruiz S, Yamasaki AE, Gilson RC, Belmonte JCI, Gray PC, Kelber JA, Zhang S, Panopoulos AD (2020) Cell surface GRP78 promotes stemness in normal and neoplastic cells. Sci Rep 10(1):3474. https://doi.org/10.1038/s41598-020-60269-y
Constam DB, Robertson EJ (1999) Regulation of bone morphogenetic protein activity by pro domains and proprotein convertases. J Cell Biol 144:139–149
D’souza RN, Cavender A, Sunavala G, Alvarez J, Ohshima T, Kulkarni AB, MacDougall M (1997) Gene expression patterns of murine dentin matrix protein 1 (Dmp1) and dentin Sialophosphoprotein (DSPP) suggest distinct developmental functions in vivo. J Bone Miner Res 12(12):2040–2049. https://doi.org/10.1359/jbmr.1997.12.12.2040
Daluiski A, Engstrand T, Bahamonde ME, Gamer LW, Agius E, Stevenson SL, Cox K, Rosen V, Lyons KM (2001) Bone morphogenetic protein-3 is a negative regulator of bone density. Nat Genet 27:84–88
Danesh SM, Villasenor A, Chong D, Soukup C, Cleaver O (2009) BMP and BMP receptor expression during murine organogenesis. Gene Expr Patterns 9:255–265
David V, Quarles LD (2010) ASARM mineralization hypothesis: a bridge too far? J Bone Miner Res 25(4):692–694. https://doi.org/10.1002/jbmr.69
De Caestecker M (2004) The transforming growth factor-β superfamily of receptors. Cytokine Growth Factor Rev 15:1–11
de Larco JE, Todaro GJ (1978) Growth factors from murine sarcoma virus-transformed cells. Proc Natl Acad Sci 75(8):4001–4005
Derynck R, Zhang YE (2003) Smad-dependent and Smad-independent pathways in TGF-β family signalling. Nature 425:577–584
Derynck R, Jarrett JA, Chen EY, Eaton DH, Bell JR, Assoian RK, Roberts AB, Sporn MB, Goeddel DV (1985) Human transforming growth factor-β complementary DNA sequence and expression in normal and transformed cells. Nature 316:701–705
Di Guglielmo GM, Le Roy C, Goodfellow AF, Wrana JL (2003) Distinct endocytic pathways regulate TGF-β receptor signalling and turnover. Nat Cell Biol 5:410–421
Dickinson ME, Kobrin MS, Silan CM, Kingsley DM, Justice MJ, Miller DA, Ceci JD, Lock LF, Lee A, Buchberg AM (1990) Chromosomal localization of seven members of the murine TGF-β superfamily suggests close linkage to several morphogenetic mutant loci. Genomics 6:505–520
Dorvee JR, Veis A (2013) Water in the formation of biogenic minerals: peeling away the hydration layers. J Struct Biol 183:278–303
Duer M, Veis A (2013) Bone mineralization: water brings order. Nat Mater 12:1081–1082
Dutta D, Williamson CD, Cole NB, Donaldson JG (2012) Pitstop 2 is a potent inhibitor of Clathrin-independent endocytosis. PLoS One 7(9):e45799. https://doi.org/10.1371/journal.pone.0045799
Ebendal T, Bengtsson H, Söderström S (1998) Bone morphogenetic proteins and their receptors: potential functions in the brain. J Neurosci Res 51:139–146
Estroff LA, Cohen I (2011) Biomineralization: micelles in a crystal. Nat Mater 10:810–811
Feng Q (2011) Principles of calcium-based biomineralization. Prog Mol Subcell Biol 52:141–197
Fetting JL, Guay JA, Karolak MJ, Iozzo RV, Adams DC, Maridas DE, Brown AC, Oxburgh L (2014) FOXD1 promotes nephron progenitor differentiation by repressing decorin in the embryonic kidney. Development 141:17–27
Fisher LW, Fedarko NS (2003) Six genes expressed in bones and teeth encode the current members of the SIBLING family of proteins. Connect Tissue Res 44:33–40. https://doi.org/10.1080/03008200390152061
Fisher LW, Whitson SW, Avioli LV, Termine JD (1983) Matrix sialoprotein of developing bone. J Biol Chem 258(20):12723–12727
Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS (2001) Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. Biochem Biophys Res Commun 280(2):460–465. https://doi.org/10.1006/bbrc.2000.4146
Flanders KC, Ludecke G, Engels S, Cissel DS, Roberts AB, Kondaiah P, Lafyatis R, Sporn MB, Unsicker K (1991) Localization and actions of transforming growth factor-beta s in the embryonic nervous system. Development 113:183–191
Foster BL, Nagatomo KJ, Tso HW, Tran AB, Nociti FH Jr, Narisawa S, Yadav MC, Mckee MD, Millan JI, Somerman MJ (2013) Tooth root dentin mineralization defects in a mouse model of hypophosphatasia. J Bone Miner Res 28:271–282
Foster BL, Ao M, Salmon CR, Chavez MB, Kolli TN, Tran AB, Chu EY, Kantovitz KR, Yadav M, Narisawa S, Millán JL, Nociti FH, Somerman MJ (2018) Osteopontin regulates dentin and alveolar bone development and mineralization. Bone 107:196–207. https://doi.org/10.1016/j.bone.2017.12.004
Franzén A, Heinegård D (1985) Isolation and characterization of two sialoproteins present only in bone calcified matrix. Biochem J 232(3):715–724
Gandhi NS, Mancera RL (2012) Prediction of heparin binding sites in bone morphogenetic proteins (BMPs). Biochim Biophys Acta Proteins Proteom 1824:1374–1381
Ganss B, Kim RH, Sodek J (1999) Bone Sialoprotein. Crit Rev Oral Biol Med 10(1):79–98. https://doi.org/10.1177/10454411990100010401
George A, Veis A (1991) FTIRS in H2O demonstrates that collagen monomers undergo a conformational transition prior to thermal self-assembly in vitro. Biochemistry 30:2372–2377
George A, Veis A (2008) Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition. Chem Rev 108:4670–4693
George A, Sabsay B, Simonian PA, Veis A (1993) Characterization of a novel dentin matrix acidic phosphoprotein. Implications for induction of biomineralization. J Biol Chem 268(17):12624–12630
George A, Gui J, Jenkins NA, Gilbert DJ, Copeland NG, Veis A (1994) In situ localization and chromosomal mapping of the AG1 (Dmp1) gene. J Histochem Cytochem 42(12):1527–1531. https://doi.org/10.1177/42.12.7983353
George A, Silberstein R, Veis A (1995) In situ hybridization shows Dmp1 (AG1) to be a developmentally regulated dentin-specific protein produced by mature odontoblasts. Connect Tissue Res 33(1–3):67–72
George A, Srinivasan R, Thotakura SR, Liu K, Veis A (1999) Rat dentin matrix protein 3 is a compound protein of rat dentin Sialoprotein and Phosphophoryn. Connect Tissue Res 40(1):49–57. https://doi.org/10.3109/03008209909005277
George A, Guirado E, Chen Y (2018) DMP1 binds specifically to type I collagen and regulates mineral nucleation and growth. In: Endo K, Kogure T, Nagasawa H (eds) Biomineralization. Springer, Singapore. https://doi.org/10.1007/978-981-13-1002-7_15
Gericke A, Qin C, Spevak L, Fujimoto Y, Butler WT, Sørensen ES, Boskey AL (2005) Importance of phosphorylation for Osteopontin regulation of biomineralization. Calcif Tissue Int 77(1):45–54. https://doi.org/10.1007/s00223-004-1288-1
Giachelli CM (2005) Inducers and inhibitors of biomineralization: lessons from pathological calcification. Orthod Craniofac Res 8:229–231
Goldberg M, Lacerda-Pinheiro S, Priam F, Jegat N, Six N, Bonnefoix M, Septier D, Chaussain-Miller C, Veis A, Denbesten P, Poliard A (2008) Matricellular molecules and odontoblast progenitors as tools for dentin repair and regeneration. Clin Oral Investig 12:109–112
Goldberg M, Kulkarni AB, Young M, Boskey A (2011) Dentin: structure, composition and mineralization. Front Biosci (Elite Ed) 3:711–735
Gorski JP (2011) Biomineralization of bone: a fresh view of the roles of non-collagenous proteins. Front Biosci (Landmark Ed) 16:2598–2621
Graff JM (1997) Embryonic patterning: to BMP or not to BMP, that is the question. Cell 89:171–174
Gullard A, Gluhak-Heinrich J, Papagerakis S, Sohn P, Unterbrink A, Chen S, MacDougall M (2016) MEPE localization in the craniofacial complex and function in tooth dentin formation. J Histochem Cytochem 64(4):224–236. https://doi.org/10.1369/0022155416635569
Hagiwara M, Shirai Y, Nomura R, Sasaki M, Kobayashi K-I, Tadokoro T, Yamamoto Y (2009) Caveolin-1 activates Rab5 and enhances endocytosis through direct interaction. Biochem Biophys Res Commun 378(1):73–78. https://doi.org/10.1016/j.bbrc.2008.10.172
Halvorsen YD, Franklin D, Bond AL, Hitt DC, Auchter C, Boskey AL, Paschalis EP, Wilkison WO, Gimble JM (2001) Extracellular matrix mineralization and osteoblast gene expression by human adipose tissue-derived stromal cells. Tissue Eng 7:729–741
Hao J, Ramachandran A, George A (2009) Temporal and spatial localization of the dentin matrix proteins during dentin biomineralization. J Histochem Cytochem 57(3):227–237. https://doi.org/10.1369/jhc.2008.952119
He G, Dahl T, Veis A, George A (2003) Dentin matrix protein 1 initiates hydroxyapatite formation in vitro. Connect Tissue Res 44(Suppl 1):240–245
Helseth DL Jr, Veis A (1981) Collagen self-assembly in vitro. Differentiating specific telopeptide-dependent interactions using selective enzyme modification and the addition of free amino telopeptide. J Biol Chem 256:7118–7128
Hershey JW, Asano K, Naranda T, Vornlocher HP, Hanachi P, Merrick WC (1996) Conservation and diversity in the structure of translation initiation factor EIF3 from humans and yeast. Biochimie 78:903–907
Hetz C (2012) The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 13(2):89–102. https://doi.org/10.1038/nrm3270
Hirst KL, Simmons D, Feng J, Aplin H, Dixon MJ, Macdougall M (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. https://doi.org/10.1006/geno.1997.4700
Hu H, Tian M, Ding C, Yu S (2019) The C/EBP homologous protein (CHOP) transcription factor functions in endoplasmic reticulum stress-induced apoptosis and microbial infection. Front Immunol 10(JAN):3083). Frontiers Media S.A. https://doi.org/10.3389/fimmu.2018.03083
Jacob A, Zhang Y, George A (2014) Transcriptional regulation of dentin matrix protein 1 (DMP1) in odontoblasts and osteoblasts. Connect tissue Res 55(Supp 1):107–112. https://doi.org/10.3109/03008207.2014.923850
Kaito T, Morimoto T, Mori Y, Kanayama S, Makino T, Takenaka S, Sakai Y, Otsuru S, Yoshioka Y, Yoshikawa H (2018) BMP-2/7 heterodimer strongly induces bone regeneration in the absence of increased soft tissue inflammation. Spine J 18:139–146
Kalmar L, Homola D, Varga G, Tompa P (2012) Structural disorder in proteins brings order to crystal growth in biomineralization. Bone 51:528–534
Kaartinen V, Voncken JW, Shuler C, Warburton D, Bu D, Heisterkamp N, Groffen J (1995) Abnormal lung development and cleft palate in mice lacking TGF–β3 indicates defects of epithelial–mesenchymal interaction. Nat Genet 11:415–421
Kawashima N, Okiji T (2016) Odontoblasts: specialized hard-tissue-forming cells in the dentin-pulp complex. Congenit Anom 56(4):144–153. https://doi.org/10.1111/cga.12169
Kessler E, Takahara K, Biniaminov L, Brusel M, Greenspan DS (1996) Bone morphogenetic protein-1: the type I procollagen C-proteinase. Science 271:360–362
Kihara T, Ito J, Miyake J (2013) Measurement of biomolecular diffusion in extracellular matrix condensed by fibroblasts using fluorescence correlation spectroscopy. PLoS One 8:e82382
Kim HM, Himeno T, Kawashita M, Kokubo T, Nakamura T (2004) The mechanism of biomineralization of bone-like apatite on synthetic hydroxyapatite: an in vitro assessment. J R Soc Interface 1:17–22
Kirkpatrick CA, Knox SM, Staatz WD, Fox B, Lercher DM, Selleck SB (2006) The function of a Drosophila glypican does not depend entirely on heparan sulfate modification. Dev Biol 300:570–582
Koehne T, Marshall RP, Jeschke A, Kahl-Nieke B, Schinke T, Amling M (2013) Osteopetrosis, osteopetrorickets and hypophosphatemic rickets differentially affect dentin and enamel mineralization. Bone 53:25–33
Liao WX, Moore RK, Otsuka F, Shimasaki S (2003) Effect of intracellular interactions on the processing and secretion of bone morphogenetic protein-15 (BMP-15) and growth and differentiation factor-9 implication of the aberrant ovarian phenotype of BMP-15 mutant sheep. J Biol Chem 278:3713–3719
Linde A, Goldberg M (1993) Dentinogenesis. Crit Rev Oral Biol Med 4(5):679–728
Lorenz-Depiereux B, Bastepe M, Benet-Pagès A, Amyere M, Wagenstaller J, Müller-Barth U, Badenhoop K, Kaiser SM, Rittmaster RS, Shlossberg AH, Olivares JL, Loris C, Ramos FJ, Glorieux F, Vikkula M, Jüppner H, Strom TM (2006) DMP1 mutations in autosomal recessive hypophosphatemia implicate a bone matrix protein in the regulation of phosphate homeostasis. Nat Genet 38(11):1248–1250. https://doi.org/10.1038/ng1868
Ma L, Pang AP, Luo Y, Lu X, Lin F (2020) Beneficial factors for biomineralization by ureolytic bacterium Sporosarcina pasteurii. Microb Cell Factories 19:12
MacDougall M, Simmons D, Luan X, Nydegger J, Feng J, Gu TT (1997) Dentin Phosphoprotein and dentin Sialoprotein are cleavage products expressed from a single transcript coded by a gene on human chromosome 4 dentin phosphoprotein dna sequence determination. J Biol Chem 272(2):835–842. https://doi.org/10.1074/jbc.272.2.835
MacDougall M, Gu TT, Luan X, Simmons D, Chen J (1998) Identification of a novel isoform of mouse dentin matrix protein 1: spatial expression in mineralized tissues. J Bone Miner Res Off J Am Soc Bone Miner Res 13(3):422–431. https://doi.org/10.1359/jbmr.1998.13.3.422
Mark MP, Butler WT, Prince CW, Finkelman RD, Ruch J-V (1988) Developmental expression of 44-kDa bone phosphoprotein (osteopontin) and bone γ-carboxyglutamic acid (Gla)-containing protein (osteocalcin) in calcifying tissues of rat. Differentiation 37(2):123–136. https://doi.org/10.1111/j.1432-0436.1988.tb00804.x
Martin A, David V, Laurence JS, Schwarz PM, Lafer EM, Hedge A-M, Rowe PSN (2008) Degradation of MEPE, DMP1, and release of SIBLING ASARM-peptides (Minhibins): ASARM-peptide(s) are directly responsible for defective mineralization in HYP. Endocrinology 149(4):1757–1772. https://doi.org/10.1210/en.2007-1205
Mckee MD, Hoac B, Addison WN, Barros NM, Millán JL, Chaussain C (2013) Extracellular matrix mineralization in periodontal tissues: noncollagenous matrix proteins, enzymes, and relationship to hypophosphatasia and X-linked hypophosphatemia. Periodontol 2000(63):102–122
Melvyn W, Leblond CP (1973) Radioautographic visualization of the deposition of a phosphoprotein at the mineralization front in the dentin of the rat incisor. J Cell Biol 56(3):838–845
Merkel A, Chen Y, George A (2019) Endocytic trafficking of DMP1 and GRP78 complex facilitates Osteogenic differentiation of human periodontal ligament stem cells. Front Physiol 10:1175. https://doi.org/10.3389/fphys.2019.01175
Miyazono K, Hellman U, Wernstedt C, Heldin C (1988) Latent high molecular weight complex of transforming growth factor beta 1. Purification from human platelets and structural characterization. J Biol Chem 263:6407–6415
Mulloy B, Rider CC (2015) The bone morphogenetic proteins and their antagonists. Vitamins & Hormones. Elsevier
Nabi IR, Le PU (2003) Caveolae/raft-dependent endocytosis. J Cell Biol 161(4):673–677. https://doi.org/10.1083/jcb.200302028
Narayanan K, Ramachandran A, Hao J, He G, Park KW, Cho M, George A (2003) Dual functional roles of dentin matrix protein 1. Implications in biomineralization and gene transcription by activation of intracellular Ca2+ store. J Biol Chem 278(19):17500–17508. https://doi.org/10.1074/jbc.M212700200
Neer EJ, Smith TF (1996) G protein heterodimers: new structures propel new questions. Cell 84:175–178
Neer EJ, Schmidt CJ, Nambudripad R, Smith TF (1994) The ancient regulatory-protein family of WD-repeat proteins. Nature 371:297–300
Neugebauer JM, Kwon S, Kim H-S, Donley N, Tilak A, Sopory S, Christian JL (2015) The prodomain of BMP4 is necessary and sufficient to generate stable BMP4/7 heterodimers with enhanced bioactivity in vivo. Proc Nat Acad Sci 112:E2307–E2316
Ni M, Zhang Y, Lee AS (2011) Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting. Biochem J 434(2):181–188. https://doi.org/10.1042/BJ20101569
Nishimatsu S-I, Thomsen GH (1998) Ventral mesoderm induction and patterning by bone morphogenetic protein heterodimers in Xenopus embryos. Mech Dev 74:75–88
Nogami H, Urist MR (1970) A morphogenetic matrix for differentiation of cartilage in tissue culture. Proc Soc Exp Biol Med 134:530–535
Nohe A, Hassel S, Ehrlich M, Neubauer F, Sebald W, Henis YI, Knaus P (2002) The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways. J Biol Chem 277:5330–5338
Nudelman F, Pieterse K, George A, Bomans PH, Friedrich H, Brylka LJ, Hilbers PA, De With G, Sommerdijk NA (2010) The role of collagen in bone apatite formation in the presence of hydroxyapatite nucleation inhibitors. Nat Mater 9:1004–1009
Ohkawara B, Iemura S-I, Ten Dijke P, Ueno N (2002) Action range of BMP is defined by its N-terminal basic amino acid core. Curr Biol 12:205–209
Opsahl Vital S, Gaucher C, Bardet C, Rowe PS, George A, Linglart A, Chaussain C (2012) Tooth dentin defects reflect genetic disorders affecting bone mineralization. Bone 50:989–997
Paine ML, Snead ML (2005) Tooth developmental biology: disruptions to enamel-matrix assembly and its impact on biomineralization. Orthod Craniofac Res 8:239–251
Pećina M, Vukičević S (2007) Biological aspects of bone, cartilage and tendon regeneration. Int Orthop 31:719–720
Pfaffenbach KT, Lee AS (2011) The critical role of GRP78 in physiologic and pathologic stress. Curr Opin Cell Biol 23(2):150–156. https://doi.org/10.1016/j.ceb.2010.09.007
Pohjolainen V, Taskinen P, Soini Y, Rysa J, Ilves M, Juvonen T, Ruskoaho H, Leskinen H, Satta J (2008) Noncollagenous bone matrix proteins as a part of calcific aortic valve disease regulation. Hum Pathol 39:1695–1701
Pragnère S, Auregan JC, Bosser C, Linglart A, Bensidhoum M, Hoc T, Nouguier-Lehon C, Chaussain C (2021) Human dentin characteristics of patients with osteogenesis imperfecta: insights into collagen-based biomaterials. Acta Biomater 119:259–267. https://doi.org/10.1016/j.actbio.2020.10.033. Epub 2020 Oct 26
Proetzel G, Pawlowski SA, Wiles MV, Yin M, Boivin GP, Howles PN, Ding J, Ferguson MW, Doetschman T (1995) Transforming growth factor–β3 is required for secondary palate fusion. Nat Genet 11:409–414
Qin C, Brunn JC, Jones J, George A, Ramachandran A, Gorski JP, Butler WT (2001) A comparative study of sialic acid-rich proteins in rat bone and dentin. Eur J Oral Sci 109(2):133–141. https://doi.org/10.1034/j.1600-0722.2001.00001.x
Qin C, Baba O, Butler WT (2004) Post-translational modifications of sibling proteins and their roles in osteogenesis and dentinogenesis. Crit Rev Oral Biol Med Off Publ Am Assoc Oral Biol 15(3):126–136
Ramachandran A, Ravindran S, George A (2012) Localization of transforming growth factor beta receptor II interacting protein-1 in bone and teeth: implications in matrix mineralization. J Histochem Cytochem 60:323–337
Ramachandran A, Ravindran S, Huang CC, George A (2016) TGF beta receptor II interacting protein-1, an intracellular protein has an extracellular role as a modulator of matrix mineralization. Sci Rep 6:37885
Ramachandran A, He K, Huang CC, Shahbazian-Yassar R, Shokuhfar T, George A (2018) TRIP-1 in the extracellular matrix promotes nucleation of calcium phosphate polymorphs. Connect Tissue Res 59:13–19
Ramirez F, Sakai L, Rifkin D, Dietz HC (2007) Extracellular microfibrils in development and disease. Cell Mol Life Sci 64:2437–2446
Ravindran S, Narayanan K, Eapen AS, Hao J, Ramachandran A, Blond S, George A (2008) Endoplasmic reticulum chaperone protein GRP-78 mediates endocytosis of dentin matrix protein 1. J Biol Chem 283(44):29658–29670. https://doi.org/10.1074/jbc.M800786200
Ravindran S, Gao Q, Ramachandran A, Sundivakkam P, Tiruppathi C, George A (2012) Expression and distribution of grp-78/bip in mineralizing tissues and mesenchymal cells. Histochem Cell Biol 138(1):113–125. https://doi.org/10.1007/s00418-012-0952-1
Roberts AB, Anzano MA, Lamb LC, Smith JM, Sporn MB (1981) New class of transforming growth factors potentiated by epidermal growth factor: isolation from non-neoplastic tissues. Proc Natl Acad Sci 78(9):5339–5343
Roberts AB, Anzano MA, Wakefield LM, Roche NS, Stern DF, Sporn MB (1985) Type beta transforming growth factor: a bifunctional regulator of cellular growth. Proc Natl Acad Sci 82(1):119–123
Rowe PS, de Zoysa PA, Dong R, Wang HR, White KE, Econs MJ, Oudet CL (2000) MEPE, a new gene expressed in bone marrow and tumors causing osteomalacia. Genomics 67(1):54–68. https://doi.org/10.1006/geno.2000.6235
Ruppert R, Hoffmann E, Sebald W (1996) Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity. Eur J Biochem 237:295–302
Salmon B, Bardet C, Khaddam M, Naji J, Coyac BR, Baroukh B, Letourneur F, Lesieur J, Decup F, Denmat DL, Nicoletti A, Poliard A, Rowe PS, Huet E, Vital SO, Linglart A, McKee MD, Chaussain C (2013) MEPE-derived ASARM peptide inhibits Odontogenic differentiation of dental pulp stem cells and impairs mineralization in tooth models of X-linked hypophosphatemia. PLoS One 8(2):e56749. https://doi.org/10.1371/journal.pone.0056749
Salmon B, Bardet C, Coyac BR, Baroukh B, Naji J, Rowe PS, Vital SO, Linglart A, Mckee MD, Chaussain C (2014) Abnormal osteopontin and matrix extracellular phosphoglycoprotein localization, and odontoblast differentiation, in X-linked hypophosphatemic teeth. Connect Tissue Res 55(Sup 1):79–82. https://doi.org/10.3109/03008207.2014.923864
Saunders M, Kong C, Shaw JA, Clode PL (2011) Matrix-mediated biomineralization in marine mollusks: a combined transmission electron microscopy and focused ion beam approach. Microsc Microanal 17:220–225
Schmid B, Furthauer M, Connors SA, Trout J, Thisse B, Thisse C, Mullins MC (2000) Equivalent genetic roles for bmp7/snailhouse and bmp2b/swirl in dorsoventral pattern formation. Development 127:957–967
Schultz GS, Wysocki A (2009) Interactions between extracellular matrix and growth factors in wound healing. Wound Repair Regen 17(2):153–162
Shi Y, Massagué J (2003) Mechanisms of TGF-β signaling from cell membrane to the nucleus. Cell 113:685–700
Sipe JB, Zhang J, Waits C, Skikne B, Garimella R, Anderson HC (2004) Localization of bone morphogenetic proteins (BMPs)-2, −4, and-6 within megakaryocytes and platelets. Bone 35:1316–1322
Stenmark H (2009) Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 10(8):513–525. https://doi.org/10.1038/nrm2728
Sun Y, Lu Y, Chen L, Gao T, D’Souza R, Feng JQ, Qin C (2011) DMP1 processing is essential to dentin and jaw formation. J Dent Res 90(5):619–624. https://doi.org/10.1177/0022034510397839
Surdilovic D, Natarajan PM, Ille T, Shetty SR, Adtani P (2018) Non-collagen protein in the dentin tissue – the role in the process of Dentinogenesis. Biomed Pharmacol J 11(2):843–849
Takagi Y, Veis A, Sauk JJ (1983) Relation of mineralization defects in collagen matrices to noncollagenous protein components. Identification of a molecular defect in dentinogenesis imperfecta. Clin Orthop 176:282–290
Tavafoghi M, Cerruti M (2016) The role of amino acids in hydroxyapatite mineralization. J R Soc Interface 13:20160462
Ten Dijke P, Hill CS (2004) New insights into TGF-β–Smad signalling. Trends Biochem Sci 29:265–273
Ten Dijke P, Hansen P, Iwata KK, Pieler C, Foulkes JG (1988) Identification of another member of the transforming growth factor type beta gene family. Proc Natl Acad Sci 85:4715–4719
Tian E, Watanabe F, Martin B, Zangari M (2020) Innate Biomineralization. Int J Mol Sci 21:4820
Todaro GJ, Fryling C, De Larco JE (1980) Transforming growth factors produced by certain human tumor cells: polypeptides that interact with epidermal growth factor receptors. Proc Natl Acad Sci 77(9):5258–5262
Tsai Y-L, Lee AS (2018) Cell surface GRP78. In cell surface GRP78, a new paradigm in signal transduction biology. Elsevier, Amsterdam, pp 41–62. https://doi.org/10.1016/B978-0-12-812351-5.00003-9
Umulis D, O'connor MB, Blair SS (2009) The extracellular regulation of bone morphogenetic protein signaling. Development 136:3715–3728
Urist MR, Peltier LF (2002) Bone: formation by autoinduction. Clin Orthop Relat Res 395:4–10
Urist MR, Strates BS (1971) Bone morphogenetic protein. J Dent Res 50:1392–1406
Veis A, Dorvee JR (2013) Biomineralization mechanisms: a new paradigm for crystal nucleation in organic matrices. Calcif Tissue Int 93:307–315
Veis A, Spector AR, Zamoscianyk H (1972) The isolation of an Edta-soluble phosphoprotein from mineralizing bovine dentin. Biochim Biophys Acta BBA - Protein Struct 257(2):404–413. https://doi.org/10.1016/0005-2795(72)90293-0
Wald T, Spoutil F, Osickova A, Prochazkova M, Benada O, Kasparek P, Bumba L, Klein OD, Sedlacek R, Sebo P, Prochazka J, Osicka R (2017) Intrinsically disordered proteins drive enamel formation via an evolutionarily conserved self-assembly motif. Proc Natl Acad Sci U S A 114:E1641–e1650
Walter P, Ron D (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science 334(6059):1081–1086). American Association for the Advancement of Science. https://doi.org/10.1126/science.1209038
Wang N, Butler JP, Ingber DE (1993) Mechanotransduction across the cell surface and through the cytoskeleton. Science 260:1124–1127
Whyte MP, McAlister WH, Fallon MD, Pierpont ME, Bijanki VN, Duan S, Otaify GA, Sly WS, Mumm S (2017) Raine syndrome (OMIM #259775), caused by FAM20C mutation, is congenital Sclerosing Osteomalacia With cerebral calcification (OMIM 259660). J Bone Miner Res Off J Am Soc Bone Miner Res 32(4):757–769. https://doi.org/10.1002/jbmr.3034
Wolfman NM, Hattersley G, Cox K, Celeste AJ, Nelson R, Yamaji N, Dube JL, Diblasio-Smith E, Nove J, Song JJ (1997) Ectopic induction of tendon and ligament in rats by growth and differentiation factors 5, 6, and 7, members of the TGF-beta gene family. J Clin Invest 100:321–330
Wozney JM (1998) The bone morphogenetic protein family: multifunctional cellular regulators in the embryo and adult. Eur J Oral Sci 106:160–166
Wrana JL, Attisano L, Cárcamo J, Zentella A, Doody J, Laiho M, Wang XF, Massagué J (1992) TGF beta signals through a heteromeric protein kinase receptor complex. Cell 71(6):1003–1014
Xu L, Chen Y-G, Massagué J (2000) The nuclear import function of Smad2 is masked by SARA and unmasked by TGFb-dependent phosphorylation. Nat Cell Biol 2:559–562
Xu L, Kang Y, Çöl S, Massagué J (2002) Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFβ signaling complexes in the cytoplasm and nucleus. Mol Cell 10:271–282
Yao S, Xu Y, Shao C, Nudelman F, Sommerdijk N, Tang R (2019) A biomimetic model for mineralization of type-I collagen fibrils. Methods Mol Biol 1944:39–54
Young MF, Kerr JM, Ibaraki K, Heegaard AM, Robey PG (1992) Structure, expression, and regulation of the major noncollagenous matrix proteins of bone. Clin Orthop Relat Res 281:275–294
Zhang Y-R, Du W, Zhou X-D, Yu H-Y (2014) Review of research on the mechanical properties of the human tooth. Int J Oral Sci 6(2):61–69. https://doi.org/10.1038/ijos.2014.21
Zurick KM, Qin C, Bernards MT (2013) Mineralization induction effects of osteopontin, bone sialoprotein, and dentin phosphoprotein on a biomimetic collagen substrate. J Biomed Mater Res A 101:1571–1581
Acknowledgements
We are pleased to acknowledge the support from the National Institutes of Health. A.G has been supported by Grants DE011657, DE 028531and the Brodie Endowment Fund; A.M has been supported by NIDCR F30 DE027601: E.G by NIDCR F30 DE028193.
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Merkel, A., Guirado, E., Narayanan, K., Ganapathy, A., George, A. (2021). Non-collagenous ECM Matrix Components Growth Factors and Cytokines Involved in Matrix Mineralization. In: Goldberg, M., Den Besten, P. (eds) Extracellular Matrix Biomineralization of Dental Tissue Structures. Biology of Extracellular Matrix, vol 10. Springer, Cham. https://doi.org/10.1007/978-3-030-76283-4_4
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