Expression of amelin and amelogenin in epithelial root sheath remnants of fully formed rat molars

Fong, Cheng Dan; Hammarström, Lars

doi:10.1067/moe.2000.107052

Cited by 73 publications

(66 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…These cells include presecretion-and maturation-stage ameloblasts, 39 enamel-free zone ameloblasts 40 and, even more strikingly, the cells of the Hertwig root sheath 41 and ERM. 42 This suggests that MSX2 downregulation is a prerequisite for significant enamel deposition, exclusively realized by secretion-stage ameloblasts. Indeed, the present data establish a link between MSX2-controlled amelogenin levels and enamel morphogenesis (regional enamel thickness and rod/inter-rod proportion).…”

Section: ; This Study and Berdal Et Al 3 ) Amelogenin Mrna Was Incrementioning

confidence: 99%

Enamel Protein Regulation and Dental and Periodontal Physiopathology in Msx2 Mutant Mice

Molla

Descroix

Aïoub

et al. 2010

The American Journal of Pathology

View full text Add to dashboard Cite

Signaling pathways that underlie postnatal dental and periodontal physiopathology are less studied than those of early tooth development. Members of the muscle segment homeobox gene (Msx) family encode homeoproteins that show functional redundancy during development and are known to be involved in epithelial-mesenchymal interactions that lead to crown morphogenesis and ameloblast cell differentiation. This study analyzed the MSX2 protein during mouse postnatal growth as well as in the adult. The analysis focused on enamel and periodontal defects and enamel proteins in Msx2-null mutant mice. In the epithelial lifecycle, the levels of MSX2 expression and enamel protein secretion were inversely related. Msx2؉/؊ mice showed increased amelogenin expression, enamel thickness, and rod size. Msx2 ؊/؊ mice displayed compound phenotypic characteristics of enamel defects, related to both enamel-specific gene mutations (amelogenin and enamelin) in isolated amelogenesis imperfecta, and cell-cell junction elements (laminin 5 and cytokeratin 5) in other syndromes. These effects were also related to ameloblast disappearance, which differed between incisors and molars. In Msx2 ؊/؊ roots, Malassez cells formed giant islands that overexpressed amelogenin and ameloblastin that grew over months. Aberrant expression of enamel proteins is proposed to underlie the regional osteopetrosis and hyperproduction of cellular cementum. These enamel and periodontal phenotypes of Msx2 mutants constitute the first case report of structural and signaling defects associated with enamel protein overexpression in a postnatal context.

show abstract

Section: ; This Study and Berdal Et Al 3 ) Amelogenin Mrna Was Incrementioning

confidence: 99%

Enamel Protein Regulation and Dental and Periodontal Physiopathology in Msx2 Mutant Mice

Molla

Descroix

Aïoub

et al. 2010

The American Journal of Pathology

View full text Add to dashboard Cite

show abstract

“…However, in more recent years different isoforms of amelogenin have also been found in the dentin matrix (Hammarstrom et al, 1997;Nebgen et al, 1999) and the odontoblasts (Oida et al, 2002;Papagerakis et al, 2003), during cementogenesis in remnants of Hertwig's root sheath and in periodontal ligament (PDL) cells (Fong and Hammarstrom, 2000;Janones et al, 2005).Very recently, we have described amelogenin expression in long bone cells; osteocytes, osteoblasts and osteoclasts, and some of the bone marrow cells. Amelogenin is also expressed in chondrocytes of the articular cartilage and differentially in cell layers of the epiphyseal growth plate.…”

Section: Introductionmentioning

confidence: 99%

Amelogenin in cranio‐facial development: the tooth as a model to study the role of amelogenin during embryogenesis

et al. 2008

View full text Add to dashboard Cite

The amelogenins comprise 90% of the developing extracellular enamel matrix proteins and play a major role in the biomineralization and structural organization of enamel. Amelogenins were also detected, in smaller amounts, in postnatal calcifying mesenchymal tissues, and in several nonmineralizing tissues including brain. Low molecular mass amelogenin isoforms were suggested to have signaling activity; to produce ectopically chondrogenic and osteogenic‐like tissue and to affect mouse tooth germ differentiation in vitro. Recently, some amelogenin isoforms were found to bind to the cell surface receptors; LAMP‐1, LAMP‐2 and CD63, and subsequently localize to the perinuclear region of the cell. The recombinant amelogenin protein (rHAM+) alone brought about regeneration of the tooth supporting tissues: cementum, periodontal ligament and alveolar bone, in the dog model, through recruitment of progenitor cells and mesenchymal stem cells.We show that amelogenin is expressed in various tissues of the developing mouse embryonic cranio‐facial complex such as brain, eye, ganglia, peripheral nerve trunks, cartilage and bone, and is already expressed at E10.5 in the brain and eye, long before the initiation of tooth formation. Amelogenin protein expression was detected in the tooth germ (dental lamina) already at E13.5, much earlier than previously reported (E19). Application of amelogenin (rHAM+) beads together with DiI, on E13.5 and E14.5 embryonic mandibular mesenchyme and on embryonic tooth germ, revealed recruitment of mesenchymal cells. The present results indicate that amelogenin has an important role in many tissues of the cranio‐facial complex during mouse embryonic development and differentiation, and might be a multifunctional protein. J. Exp. Zool. (Mol. Dev. Evol.) 312B:445–457, 2009. © 2008 Wiley‐Liss, Inc.

show abstract

“…Although for over 4 decades, the amelogenins were thought to be tissue-specific and exclusively expressed by the ectodermal enamel-producing ameloblast cells, more recently, amelogenin has also been implicated in dentin matrix (Nebgen et al, 1999) and odontoblasts (Papagerakis et al, 2003), during cementogenesis, and in periodontal ligament (PDL) cells (Fong and Hammarstrom, 2000;Janones et al, 2005). Smaller amelogenin gene-spliced products, e.g., leucine-rich-amelogenin peptide (LRAP), have been suggested to be associated with cell signaling and to have chondrogenic and osteogenic potential (Veis et al, 2000;Viswanathan et al, 2003).…”

mentioning

confidence: 99%

Amelogenin expression in long bone and cartilage cells and in bone marrow progenitor cells

Haze

Taylor

Blumenfeld

et al. 2007

The Anatomical Record

View full text Add to dashboard Cite

The amelogenin protein is considered as the major molecular marker of developing ectodermal enamel. Recent data suggest other roles for amelogenin beyond structural regulation of enamel mineral crystal growth. Here we describe our novel discovery of amelogenin expression in long bone cells, in cartilage cells, in cells of the epiphyseal growth plate, and in bone marrow stromal cells. Anat Rec, 290:455-460, 2007. 2007 Wiley-Liss, Inc.

show abstract

Expression of amelin and amelogenin in epithelial root sheath remnants of fully formed rat molars

Cited by 73 publications

References 23 publications

Enamel Protein Regulation and Dental and Periodontal Physiopathology in Msx2 Mutant Mice

Enamel Protein Regulation and Dental and Periodontal Physiopathology in Msx2 Mutant Mice

Amelogenin in cranio‐facial development: the tooth as a model to study the role of amelogenin during embryogenesis

Amelogenin expression in long bone and cartilage cells and in bone marrow progenitor cells

Contact Info

Product

Resources

About