Amelogenin Enhances the Proliferation of Cementoblast Lineage Cells

Kunimatsu, Ryo; Tanimoto, Kotaro; Tanne, Yuki; Kamiya, Takashi; Ohkuma, Satoru; Huang, Yu‐Ching; Yoshimi, Yuki; Miyauchi, Mutsumi; Takata, Takashi; Tanne, Kazuo

doi:10.1902/jop.2011.110031

Cited by 18 publications

(22 citation statements)

References 36 publications

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“…Haze, 2009 [8]; Tamburstuen, 2011 [10], 2. Zeichner-David, 2006 [57]; Fukae, 2006 [58]; Matsuzawa, 2009 [59]; Tambursten, 2010 [42]; Kakegawa, 2010 [60]; Zhang, 2011 [54]; Kitagawa, 2011 [53]; Kunimatsu, 2011 [61]; Izumikawa, 2012 [62]; Amin, 2013 [63], 3. Spahr, 2006 [36]; Haze, 2009 [8]; Iizuka, 2011 [18]; Tamburstuen, 2011 [10]; Atsawasuwan, 2013 [40], 4.…”

Section: Discussionmentioning

confidence: 99%

Tracking Endogenous Amelogenin and Ameloblastin In Vivo

et al. 2014

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Research on enamel matrix proteins (EMPs) is centered on understanding their role in enamel biomineralization and their bioactivity for tissue engineering. While therapeutic application of EMPs has been widely documented, their expression and biological function in non-enamel tissues is unclear. Our first aim was to screen for amelogenin (AMELX) and ameloblastin (AMBN) gene expression in mandibular bones and soft tissues isolated from adult mice (15 weeks old). Using RT-PCR, we showed mRNA expression of AMELX and AMBN in mandibular alveolar and basal bones and, at low levels, in several soft tissues; eyes and ovaries were RNA-positive for AMELX and eyes, tongues and testicles for AMBN. Moreover, in mandibular tissues AMELX and AMBN mRNA levels varied according to two parameters: 1) ontogenic stage (decreasing with age), and 2) tissue-type (e.g. higher level in dental epithelial cells and alveolar bone when compared to basal bone and dental mesenchymal cells in 1 week old mice). In situ hybridization and immunohistodetection were performed in mandibular tissues using AMELX KO mice as controls. We identified AMELX-producing (RNA-positive) cells lining the adjacent alveolar bone and AMBN and AMELX proteins in the microenvironment surrounding EMPs-producing cells. Western blotting of proteins extracted by non-dissociative means revealed that AMELX and AMBN are not exclusive to mineralized matrix; they are present to some degree in a solubilized state in mandibular bone and presumably have some capacity to diffuse. Our data support the notion that AMELX and AMBN may function as growth factor-like molecules solubilized in the aqueous microenvironment. In jaws, they might play some role in bone physiology through autocrine/paracrine pathways, particularly during development and stress-induced remodeling.

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Section: Discussionmentioning

confidence: 99%

Tracking Endogenous Amelogenin and Ameloblastin In Vivo

et al. 2014

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“…Amelogenin protein, such as rp(H)M180, has recently been shown to enhance the growth rate for human PDL cells and BMSCs [23, 44, 45]. Samples containing more CD146 marked cells respond by proliferation not only to rp(H)M180, but to all mitogens tested [13, 14].…”

Section: Discussionmentioning

confidence: 99%

The role of cell surface markers and enamel matrix derivatives on human periodontal ligament mesenchymal progenitor responses in vitro

et al. 2011

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“…Previous studies have reported that recombinant full-length amelogenin (rh174 or rm180) binds to LAMP-1 or LAMP-3 expressed on the cell membrane of cementoblasts 21,25) , and that the presence of LAMP-3 antibody in the culture medium inhibited the cementoblast proliferation promoted by rh174 25) . Furthermore in cementoblast, LRAP showed no effect on cell proliferation 36) .…”

Section: Discussionmentioning

confidence: 99%

“…ATDC5 and MC3T3-E1 cells were seeded at 1 × 10 3 cells per well on a 96-well plate, and after 3 hours for initial cell attachment, the serumfree growth medium was changed to media with or without 10 g/ml of LRAP. For the inhibition experiment, the medium was changed to contain both LRAP and rat monoclonal antibody to mouse LAMP-1 (Santa Cruz Biotech, Tokyo, Japan) diluted to 2 g/ml according to a previous report 25) . After 48 hours of culture, the cells were incubated with the counting reagent for one hour as per the manufacturer's instructions.…”

Section: Cell Proliferationmentioning

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 Enhances the Proliferation of Cementoblast Lineage Cells

Abstract: The results show that rh174 interacts with CD63, and rh174/CD63 interaction activates the ERK1/2 signaling pathway, enhancing the proliferation activities of HCEM and HPDL cells.

Cited by 18 publications

References 36 publications

Tracking Endogenous Amelogenin and Ameloblastin In Vivo

Tracking Endogenous Amelogenin and Ameloblastin In Vivo

The role of cell surface markers and enamel matrix derivatives on human periodontal ligament mesenchymal progenitor responses in vitro

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

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