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

Matsuda, Yuko; Hatakeyama, Yuji; Nakashima, Kazuki; Kamogashira, Naoko; Hatakeyama, Jun; Tamaoki, Sachio; Sawa, Yoshihiko; Ishikawa, Hiroyuki

doi:10.2485/jhtb.26.51

Cited by 3 publications

(7 citation statements)

References 38 publications

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“…Of the latter, 10 [24][25][26][27][28][29][30][31][32][33] were excluded due to the descriptive analysis (Table 1), while 14 studies met the inclusion criteria (Table 2). In the 14 studies selected [8,[34][35][36][37][38][39][40][41][42][43][44][45][46], it was not possible to perform a quantitative analysis due to major differences in terms of the cell model, peptide concentrations, time points, and methodologies employed (Table 2). Among the included papers, there were no clinical trials, 13 were in vitro [8,[34][35][36][37][38][39][41][42][43][44][45][46], and 1 was in vivo [40].…”

Section: Systematic Reviewmentioning

confidence: 99%

“…In the 14 studies selected [8,[34][35][36][37][38][39][40][41][42][43][44][45][46], it was not possible to perform a quantitative analysis due to major differences in terms of the cell model, peptide concentrations, time points, and methodologies employed (Table 2). Among the included papers, there were no clinical trials, 13 were in vitro [8,[34][35][36][37][38][39][41][42][43][44][45][46], and 1 was in vivo [40]. Only one article tested TRAP [38], five LRAP [8,[34][35][36][37], six SP [39][40][41][42][43][44], and two the C11 peptide [45,46].…”

Section: Systematic Reviewmentioning

confidence: 99%

“…Among the included papers, there were no clinical trials, 13 were in vitro [8,[34][35][36][37][38][39][41][42][43][44][45][46], and 1 was in vivo [40]. Only one article tested TRAP [38], five LRAP [8,[34][35][36][37], six SP [39][40][41][42][43][44], and two the C11 peptide [45,46]. Fifty percent of the selected articles evaluated, simultaneously, the effect of the various peptides on osteoblastic differentiation, deposition of mineral crystals, and cell proliferation [35,37,39,[41][42][43]46].…”

Section: Systematic Reviewmentioning

confidence: 99%

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Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review

Fiorino

Marturano

Placella

et al. 2021

IJMS

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Amelogenins are enamel matrix proteins currently used to treat bone defects in periodontal surgery. Recent studies have highlighted the relevance of amelogenin-derived peptides, named LRAP, TRAP, SP, and C11, in bone tissue engineering. Interestingly, these peptides seem to maintain or even improve the biological activity of the full-length protein, which has received attention in the field of bone regeneration. In this article, the authors combined a systematic and a narrative review. The former is focused on the existing scientific evidence on LRAP, TRAP, SP, and C11’s ability to induce the production of mineralized extracellular matrix, while the latter is concentrated on the structure and function of amelogenin and amelogenin-derived peptides. Overall, the collected data suggest that LRAP and SP are able to induce stromal stem cell differentiation towards osteoblastic phenotypes; specifically, SP seems to be more reliable in bone regenerative approaches due to its osteoinduction and the absence of immunogenicity. However, even if some evidence is convincing, the limited number of studies and the scarcity of in vivo studies force us to wait for further investigations before drawing a solid final statement on the real potential of amelogenin-derived peptides in bone tissue engineering.

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Section: Systematic Reviewmentioning

confidence: 99%

Section: Systematic Reviewmentioning

confidence: 99%

Section: Systematic Reviewmentioning

confidence: 99%

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Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review

Fiorino

Marturano

Placella

et al. 2021

IJMS

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“…7). It has been suggested that LAMP-1 and LAMP-3 on the cell membrane bind to amelogenin and could be signaling receptor of amelogenin (Veis et al, 2000;Zou et al), and several studies have shown that LAMP-1 and LAMP-3 may be involved in the biological function of amelogenin as signaling molecules (Xu et al, 2008;Zhang et al, 2010;Kunimatsu et al, 2011;Matsuda et al, 2017). The cytoplasm of the secretory stage Amelx* ameloblasts has been reported to display strong amelogenin immunopositivity (Barron et al).…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse

et al. 2019

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OTAWA-KAMOGASHIRA, N.; MATSUDA, Y.; TAKEZAKI, M.; HATAKEYAMA, Y.; TAMAOKI, S. & ISHIKAWA, H.Immunohistochemical study of amelogenin binding proteins in an amelogenin point mutation mouse. Int. J. Morphol., 37(2):522-532, 2019. SUMMARY:Amelogenin is one of the enamel matrices secreted by ameloblasts. A mutation of the amelogenin gene can cause hereditary dental enamel defects known as amelogenesis imperfecta (AI). Since lysosome-associated membrane protein-1 (LAMP-1), -3 (LAMP-3), and 78kDa glucose-related protein (Grp78) were identified as binding proteins of amelogenin, several studies have suggested the involvement of these binding proteins with the cell kinetics of ameloblasts in normal or abnormal conditions. The purpose of this study is to investigate the distribution of these amelogenin binding proteins in the ameloblast cell differentiation of mice with a point mutation of the amelogenin gene (Amelx*). The incisors of Amelx* mice had a white opaque color and the tooth surface was observed to be rough under a scanning electron microscope. Among the sequential ameloblast cell differentiation in the Amelx* mice, the shape of ameloblasts at the transition stage was irregular in comparison to those in wild-type (WT) mice. Immunostaining of Grp78 revealed that the whole cytoplasm of the transition stage ameloblasts was immunopositive for Grp78 antibody, while only the distal part of cell was positive in the WT mice. Furthermore, in the Amelx* mice, the cytoplasm of the transition stage ameloblasts was immunopositive for LAMP-1 and LAMP-3. These results suggest that Amelx* may cause the abnormal distribution of amelogenin binding proteins in the cytoplasm of ameloblasts. KEY WORDS: Amelogenin; Amelogenesis imperfecta; 78kDa glucose-related protein (Grp78); Lysosome-associated membrane proteins (LAMPs). OTAWA-KAMOGASHIRA, N.; MATSUDA, Y.; TAKEZAKI, M.; HATAKEYAMA, Y.; TAMAOKI, S. & ISHIKAWA, H. Immunohistochemical study of amelogenin binding proteins in an amelogenin point mutation mouse. OTAWA-KAMOGASHIRA, N.; MATSUDA, Y.; TAKEZAKI, M.; HATAKEYAMA, Y.; TAMAOKI, S. & ISHIKAWA, H. Immunohistochemical study of amelogenin binding proteins in an amelogenin point mutation mouse. Int. J. Morphol., 37(2):527-537, 2019.

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“…A proportional number of cells was counted, as described previously [17] with minor modification. Briefly, HAM2 cells were seeded at each cell density, 5.0, 2.5, and 0.6 × 10 3 cells per well on a type I collagen-coated 96-well plate (Corning Life Sciences, NY, USA) depending on each experiment.…”

Section: Cell Proliferationmentioning

confidence: 99%

Distinct Role of Transforming Growth Factor-Beta 1 and Fibroblast Growth Factors in Human Amelobastoma Epithelial Cell Proliferation

Matsuda¹,

Kamogashira²,

Hatakeyama³

et al. 2017

BMB

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Ameloblastoma is a locally invasive benign epithelial odontogenic tumor and its histopathological structures are similar to the enamel organ. Although various studies have investigated cell proliferation in ameloblastoma to elucidate the biological behavior and clinicopathological mechanisms, it remains poorly understood. The studies on the development of the enamel organ reports that FGF-9, -10, and TGF-β1 are strongly involved in dental epithelial cell differentiation and cell proliferation. In this study, we attempt to evaluate the effect of these growth factors on ameloblastoma cells. Both collagen-coated and normal plastic cell culture plate cell growth curves were steeper in the presence of growth supplement than in the absence of growth supplement. The presence of TGF-β1 at each dose (1 to 10 ng/ml), however, suppressed the number of cells cultured on the collagen-coated plate but made no significant difference on the normal plastic plate. The number of cells was increased in the presence of FGF-10 at 100 ng/ml, but not in the presence of FGF-9 after 48 h culture. These results suggest that FGF-10 and TGF-β1 play distinct roles in the cell proliferation of human ameloblastoma cells.

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

Cited by 3 publications

References 38 publications

Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review

Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review

Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse

Distinct Role of Transforming Growth Factor-Beta 1 and Fibroblast Growth Factors in Human Amelobastoma Epithelial Cell Proliferation

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