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

Haze, Amir; Taylor, Angie; Blumenfeld, Anat; Rosenfeld, Eli; Leiser, Yoav; Dafni, Leah; Shay, Boaz; Gruenbaum-Cohen, Yael; Fermon, Eran; Haegewald, Stefan; Bernimoulin, Jean‐Pierre; Deutsch, D.

doi:10.1002/ar.20520

Cited by 49 publications

(57 citation statements)

References 27 publications

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“…Amelogenin message and protein have been detected by various strategies in other tissues, including dental pulp cells [34][35][36][37] , periodontium, bone, brain and other tissues 38,39 . The reader is directed to a recent review for discussion 40 , but major defects have not yet been reported outside of the enamel in either murine models or in humans with AI specific gene mutations.…”

Section: Amelogenin Expression In Other Tissuesmentioning

confidence: 99%

The Amelogenin Proteins and Enamel Development in Humans and Mice

Gibson

2011

Journal of Oral Biosciences

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Before a tooth erupts into the oral cavity, the mineralized enamel and dentin layers begin to develop. During these early stages of enamel formation, an abundant group of proteins known as amelogenins are secreted by ameloblast cells within the developing tooth. These proteins are required for the enamel layer to reach its normal thickness and attain its intricate structure. Human patients with amelogenin gene mutations have a condition referred to as amelogenesis imperfecta, and we have analyzed human gene defects so that we can recreate them in mice. We have generated mice with a null amelogenin mutation where no amelogenin is produced, mice that over-express normal and mutated amelogenins, and over-expressors have been mated to null mice for rescue experiments. Because there are at least 15 messages that are alternatively spliced from a single amelogenin primary RNA transcript, these approaches have begun to reveal the functions of individual amelogenin proteins during enamel development. Finally, amelogenins are processed by carefully regulated proteolytic digestion leading to many additional amelogenin peptides and it is likely that protein function is altered during this developmental process. We have also had some surprises, as one of our mouse models develops odontogenic tumors, and we know now that some of the amelogenins are expressed in other regions of the body outside of the oral cavity, and may have a role in signal transduction.

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Section: Amelogenin Expression In Other Tissuesmentioning

confidence: 99%

The Amelogenin Proteins and Enamel Development in Humans and Mice

Gibson

2011

Journal of Oral Biosciences

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“…Using the same antibody, we additionally revealed that periodontal ligaments in the developing dental root and dental follicle cells were also immunopositive for amelogenin. Amelogenin is reported to be expressed in long bone marrow stromal cells, including mesenchymal stem cells 15) . Dental follicle cells also express mesenchymal precursor cell markers and include multipotential mesenchymal stem cells, which differentiate into mineralized tissues, including alveolar bone and the cementum 16) .…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical Study of Lysosome-Associated Membrane Proteins During Periodontal Ligament Development

Hatakeyama

Oka

et al. 2013

J. Hard Tissue Biology.

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Amelogenin is an enamel matrix protein also expressed in periodontal tissues. Recent studies suggest that lysosome-associated membrane proteins (LAMPs) can bind cell surface amelogenin and act as signaling receptors for amelogenin in periodontal ligament (PDL) cells and cementoblasts in vitro. However, whether amelogenin and LAMPs are involved in the development of periodontal tissues is unclear. To address this issue, we used immunohistochemistry to profile LAMPs and amelogenin expression during periodontal tissue development. Paraffin sections from mice at embryonic day 15 (E15) and 1, 2, and 4 weeks were made, and serial sections at each age were stained with hematoxylin-eosin, followed by immunostaining with antiamelogenin, LAMP-1, and LAMP-3. At E15, dental follicle cells, which are the source of periodontal tissues, were amelogenin-positive and weakly positive for LAMP-1 and LAMP-3. At 1 week, dental follicle cells were immunopositive for amelogenin and LAMP-1 but weakly positive for LAMP-3. At 2 weeks, PDL cells were positive for amelogenin and LAMP-1 but negative for LAMP-3. At 4 weeks, PDL cells were immunopositive for both amelogenin and LAMP-1. These results suggest that LAMP-1 is expressed in both the dental follicle and PDL, and that LAMP-1 and LAMP-3 have temporally distinct roles as signaling receptors for amelogenin.

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“…In this decade, several studies have revealed that amelogenin isoform genes and proteins are expressed not only in enamel formation but also in adult connective tissue forming cells like rat osteoblasts 6) , rat chondrocytes 6) , odontoblasts 7) , cementoblasts 8,9) and periodontal ligament cells 8,10) . In amelogenin null mice, dramatically reduced expression of bone sialoprotein (BSP), a mineralized tissue-specific marker, was observed at both the gene and protein levels 11) .…”

Section: Introductionmentioning

confidence: 99%

Effects of a Chemically Synthesized Leucine-Rich Amelogenin Peptide (csLRAP) on Chondrogenic and Osteogenic Cells

Matsuda

Hatakeyama

Nakashima

et al. 2017

J. Hard Tissue Biology.

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Amelogenin is one of the enamel matrices secreted by ameloblasts and is known to have at least 15 alternative mRNA splicing isoforms. The leucine rich amelogenin peptide (LRAP) is one of most abundant amelogenin isoforms and numerous studies have shown that amelogenin peptides including LRAP, are expressed in cartilage and bone. Lysosome-associated membrane protein-1 (LAMP-1) has been identified as amelogenin binding partner, however, the mechanism of action for LRAP in chondrogenesis or osteogenesis is still unclear. This study aimed to assay the effect of chemically synthesized LRAP (csLRAP) on chondrogenic or osteogenic differentiation with the involvement of LAMP-1. The csLRAP used in this study was generated by F-moc solid phase chemistry based on the mouse LRAP amino acid sequence and was added to the culture medium of the chondrogenic cells, ATDC5 and the osteoblast cells, MC3T3-E1. Both chondrogenic and osteoblast cells, in which an immunopositive reaction to LAMP-1 antibody was observed by immunocytochemistry, showed significant suppression in cell number in the presence of csLRAP at 10 g/ml compared to that in control, but this effect was rescued in the presence of LAMP-1 antibody. On the other hand, the intensity of alcian blue staining in chondrogenic cells and alizarin red staining in osteoblast cells was significantly increased in the presence of csLRAP at a dose of 10 g/ml after 4 weeks culture, and this effect was suppressed in the presence LAMP-1 antibody. Moreover, the chondrogenic or osteogenic differentiation marker genes including Sox9, Type II Collagen, Type X Collagen, Runx2, Alkaline Phosphatase, and Type I Collagen, were upregulated in the presence of csLRAP after one week of culture and were suppressed in the presence of LAMP-1 antibody. These results suggest that csLRAP could promote osteogenic and chondrogenic differentiation in vitro, and that LAMP-1 may be involved in the differentiation and proliferation of these cells.

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

Cited by 49 publications

References 27 publications

The Amelogenin Proteins and Enamel Development in Humans and Mice

The Amelogenin Proteins and Enamel Development in Humans and Mice

Immunohistochemical Study of Lysosome-Associated Membrane Proteins During Periodontal Ligament Development

Effects of a Chemically Synthesized Leucine-Rich Amelogenin Peptide (csLRAP) on Chondrogenic and Osteogenic Cells

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