Mineral induction by immobilized phosphoproteins

Saito, Takashi; Arsenault, A. Larry; Yamauchi, Mitsuo; Kuboki, Yoshinori; Crenshaw, M.A.

doi:10.1016/s8756-3282(97)00149-x

Cited by 153 publications

(144 citation statements)

References 52 publications

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“…When DMP1-collagen complex was incubated in a pseudo-physiological buffer and tested for its mineralization property in vitro, it was observed that only DMP1-collagen complex initiated biomineral deposition on the collagen surface, whereas there was no calcium phosphate deposition on the control collagen surface. Similar results have been achieved when the collagen surface was immobilized with bone sialoprotein-decorin chimeric protein (51) and phosphophoryn (4). In all of these cases, mineralization was initiated specifically on the collagen surface adsorbed with noncollagenous proteins.…”

Section: Discussionsupporting

confidence: 75%

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Dentin Matrix Protein 1 Immobilized on Type I Collagen Fibrils Facilitates Apatite Deposition in Vitro

George

2004

Journal of Biological Chemistry

205

199

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During bone and dentin mineralization, the crystal nucleation and growth processes are considered to be matrix regulated. Osteoblasts and odontoblasts synthesize a polymeric collagenous matrix, which forms a template for apatite initiation and elongation. Coordinated and controlled reaction between type I collagen and bone/dentin-specific noncollagenous proteins are necessary for well defined biogenic crystal formation. However, the process by which collagen surfaces become mineralized is not understood. Dentin matrix protein 1 (DMP1) is an acidic noncollagenous protein expressed during the initial stages of mineralized matrix formation in bone and dentin. Here we show that DMP1 bound specifically to type I collagen, with the binding region located at the N-telopeptide region of type I collagen. Peptide mapping identified two acidic clusters in DMP1 responsible for interacting with type I collagen. The collagen binding property of these domains was further confirmed by site-directed mutagenesis. Transmission electron microscopy analyses have localized DMP1 in the gap region of the collagen fibrils. Fibrillogenesis assays further demonstrated that DMP1 accelerated the assembly of the collagen fibrils in vitro and also increased the diameter of the reconstituted collagen fibrils. In vitro mineralization studies in the presence of calcium and phosphate ions demonstrated apatite deposition only at the collagenbound DMP1 sites. Thus specific binding of DMP1 and possibly other noncollagenous proteins on the collagen fibril might be a key step in collagen matrix organization and mineralization.Mineralized tissues such as bone and dentin are hierarchically organized biocomposites possessing unique mechanical properties (1). Understanding the biomineralization process is of great value for synthesis of bioengineered bone and dentinlike materials with optimum structural properties. Type I collagen accounts for 90% of the total protein in the organic matrix of bone and dentin (1). It not only provides the structural framework with viscoelastic properties but also defines compartments for ordered mineral deposition. Studies have demonstrated that the apatite crystals are first nucleated in the gap region, and the growing mineral platelets are highly organized in a staggered manner within the collagen fibrils (2, 3).It is well established that type I collagen matrix does not have the capacity to induce matrix-specific mineral formation from metastable calcium phosphate solutions that do not spontaneously precipitate. Several in vitro studies have demonstrated that ordered mineralization of apatite on collagen fibril is impossible without additives (4, 5). As a result, much attention has been drawn to the noncollagenous proteins (NCPs) 1 that are tightly bound to the collagen fibers in mineralized tissues. Bone and/or dentin-specific NCPs are mostly acidic in nature and are rich in glutamic acid, aspartic acid, and phosphoserines (6, 7). They possess high calcium binding capacity and hydroxyapatite affinity (8 -10). In vitro ...

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Section: Discussionsupporting

confidence: 75%

“…Several in vitro studies have demonstrated that ordered mineralization of apatite on collagen fibril is impossible without additives (4,5). As a result, much attention has been drawn to the noncollagenous proteins (NCPs) 1 that are tightly bound to the collagen fibers in mineralized tissues.…”

mentioning

confidence: 99%

Dentin Matrix Protein 1 Immobilized on Type I Collagen Fibrils Facilitates Apatite Deposition in Vitro

George

2004

Journal of Biological Chemistry

205

199

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“…The high phosphoserine content of the 22-kDa fish phosphoprotein is reminiscent of phosphophoryn, a cleavage product of dentin sialophosphoprotein belonging to the same small integrin binding ligand N-linked glycoprotein family of OPN and BSP, in which phosphorylation is important for the deposition of calcium phosphate crystals and that the acidic carboxylate groups alone are not sufficient (46,58). The generation of dentin sialophosphoprotein null mice resulted in tooth defects similar to human dentinogenesis imperfecta III (59).…”

Section: Discussionmentioning

confidence: 99%

The Isolation and Characterization of Glycosylated Phosphoproteins from Herring Fish Bones

Zhou

Salih

Glimcher

2010

Journal of Biological Chemistry

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Past studies of bone extracellular matrix phosphoproteins such as osteopontin and bone sialoprotein have yielded important biological information regarding their role in calcification and the regulation of cellular activity. Most of these studies have been limited to proteins extracted from mammalian and avian vertebrates and nonvertebrates. The present work describes the isolation and purification of two major highly glycosylated and phosphorylated extracellular matrix proteins of 70 and 22 kDa from herring fish bones. The 70-kDa phosphoprotein has some characteristics of osteopontin with respect to amino acid composition and susceptibility to thrombin cleavage. Unlike osteopontin, however, it was found to contain high levels of sialic acid similar to bone sialoprotein. The 22-kDa protein has very different properties such as very high content of phosphoserine (ϳ270 Ser(P) residues/1000 amino acid residues), Ala, and Asx residues. The N-terminal amino acid sequence analysis of both the 70-kDa (NPIMA(M)ETTS(M)DSKVNPLL) and the 22-kDa (NQDMAMEASSDPEAA) fish phosphoproteins indicate that these unique amino acid sequences are unlike any published in protein databases. An enzyme-linked immunosorbent assay revealed that the 70-kDa phosphoprotein was present principally in bone and in calcified scales, whereas the 22-kDa phosphoprotein was detected only in bone. Immunohistological analysis revealed diffusely positive immunostaining for both the 70-and 22-kDa phosphoproteins throughout the matrix of the bone. Overall, this work adds additional support to the concept that the mechanism of biological calcification has common evolutionary and fundamental bases throughout vertebrate species.The noncollagenous phosphoproteins of bone extracellular matrix (ECM) 2 have been of major scientific interest for more than three decades and continue to be the subject of a number of studies. This is due to observations and experimental evidence that they are involved in a number of biological events such as regulation of biomineralization and cellular activity/ behavior in normally mineralizing tissues including bone (1-7), cartilage (8), and dentin (9). ECM phosphoproteins have been also found in the pathologically mineralizing tissues such as atherosclerotic plaque (10), kidney stones (11), dental calculus (12), and breast tumors (13). Two most abundant and well known are bone sialoprotein (BSP) and osteopontin (OPN), which are synthesized by osteoblasts during bone formation (1-7, 14, 15). In addition to their involvement in biomineralization and its regulation (6, 7, 16 -19), bone ECM phosphoproteins are implicated in modulating cellular function and the behavior of bone cells such as osteoblasts (20 -22), osteoclasts (23-27), and other cell types such as tumor and immune (28, 29) where they promote cell adhesion, motility, and transmembrane signaling. The involvement of both BSP and OPN in such biological functions has been predominantly linked to the presence of an integrin receptor-binding tripeptide Arg-Gly-Asp sequence in t...

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“…As pointed out by Hunter et al [6], in vitro effects of a variety of proteins vary between solution studies, gel systems, and especially when proteins are bound to agarose beads or collagen. Although gel precipitation techniques were not used, Crenshaw et al [49][50][51] have shown that a variety of matrix proteins that do not promote mineralization in solution, do induce mineral formation when cross-linked to agarose beads or collagen. These results suggest the need to perform side-by-side studies on individual matrix molecules with systematic variation of components in the gel matrix.…”

Section: Variations Between Study Systemsmentioning

confidence: 99%

Diffusion Systems for Evaluation of Biomineralization

Silverman

Boskey

2004

Calcif Tissue Int

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A variety of in vitro study methods have been used to elucidate the roles of matrix molecules in biomineralization processes. Among these, gel diffusion-precipitation studies have proved to be an effective tool. This methodology is uniquely capable of characterizing the effects of matrix molecules on mineralization while only using very small quantities of material. Furthermore, gel methods have been extended for use as a mineralization assay system to characterize modified matrix molecules and synthetic analogues. Here we discuss the advantages and limitations of gelatin, agar, agarose, and other systems for studying the mechanisms of biomineralization. KeywordsHydroxyapatite; Biomineralization; Gel diffusion; Gelatin; Agarose; Agar In Vitro StudiesThe functions of vertebrate and non-vertebrate mineralized tissue matrix biomolecules, such as osteopontin [1][2][3][4], osteonectin [5,6], amelogenin [7,8], bone sialoprotein [2,3,6,9], and a variety of shell proteins [10,11] generally have been demonstrated in a three-step process. First, molecules that may influence the biomineralization process are either isolated from mineralized tissue, purified, and characterized, or cloned and expressed in recombinant forms. Their spatial and temporal distribution in mineralizing tissue, and their presence or absence from diseased or non-mineralizing tissue, as assessed by immunolocalization or in situ hybridization, suggests their role in mineral formation. Second, the molecule being studied can be associated with the biomineralization process in vivo via tissue studies on genetically modified or diseased organisms where expression of the substance of interest is altered, prevented, or enhanced. Third, in vitro mineralization studies may be used to provide insight into the mechanism of action of matrix proteins and to elucidate a molecule's function in vivo [12]. While many different techniques have been used in the in vitro studies, gel precipitation methods, used for over a century for the growth of large crystals [13], have recently been introduced to help elucidate how non-collagenous proteins and other biomolecules act to control biomineralization processes.The interplay of in vivo and in vitro studies allows characterization of a molecule's role in complex living tissue, where we have limited experimental control, against a backdrop of information from well-controlled, simpler precipitation studies. The cell-free in vitro studies allow characterization of an individual compound or mixture's effects on nucleation, growth kinetics, inhibition, and crystal composition and habit, as well as quantitative comparisons We review here the recent application of crystal formation in gels to probe mineralization mechanisms with emphasis placed on hydroxyapatite formation and growth, although the techniques described are applicable to other types of biomineralization.Most in vitro studies of matrix proteins involved in hydroxyapatite (HA) formation have been done in solution, as opposed to gels. The solution studies charact...

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Mineral induction by immobilized phosphoproteins

Cited by 153 publications

References 52 publications

Dentin Matrix Protein 1 Immobilized on Type I Collagen Fibrils Facilitates Apatite Deposition in Vitro

Dentin Matrix Protein 1 Immobilized on Type I Collagen Fibrils Facilitates Apatite Deposition in Vitro

The Isolation and Characterization of Glycosylated Phosphoproteins from Herring Fish Bones

Diffusion Systems for Evaluation of Biomineralization

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