REGENERASI SEL LIGAMEN PERIODONTAL DENGAN KOLAGEN SISIK IKAN NILA (Oreochromis niloticus)

Background : Regeneration of periodontal ligament cells with tilapia scales collagen (Oreochromis niloticus) is one of the therapies that can be used in the field of periodontics. This review aims to explain the mechanism of periodontal ligament cell regeneration using tilapia scales (Oreochromis niloticus) collagen.Methods : Literature collection is done by selecting journals or articles through PubMed, NCBI, and Google Scholar based on keywords that match the author's criteria.Results : Regeneration of cells using collagen from tilapia scales can be used by using a bone graft technique because fish collagen contains calcium and phosphate that resembles human, namely hydroxyapatite (HAP). Fish scales are an alternative source of type I collagen and have the potential to be an alternative material for bone graft.Conclusions : Regeneration of periodontal ligament cells using tilapia scale collagen can be done using bone graft techniques. Fish scales have many benefits apart from having almost the same content as humans as well as materials that are still easy to obtain and a more economical price to use. The authors suggest that the researchers further conduct further research on the preparation of tilapia scales so that they can be applied in tissue engineering actions in the field of periodonsia.

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Hypoxia-inducible factor-1α is required for transforming growth factor-β1-induced type I collagen, periostin and α-smooth muscle actin expression in human periodontal ligament cells

Archives of Oral Biology ◽

10.1016/j.archoralbio.2014.03.003 ◽

2014 ◽

Vol 59 (6) ◽

pp. 595-600 ◽

Cited By ~ 11

Author(s):

Teppei Watanabe ◽

Akihiro Yasue ◽

Eiji Tanaka

Keyword(s):

Periodontal Ligament ◽

Type I Collagen ◽

Transforming Growth Factor ◽

Smooth Muscle Actin ◽

Hypoxia Inducible Factor ◽

Transforming Growth Factor Β1 ◽

Periodontal Ligament Cells ◽

Type I ◽

Muscle Actin ◽

Actin Expression

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Sphingomyelin Phosphodiesterase 3 Enhances Cytodifferentiation of Periodontal Ligament Cells

Journal of Dental Research ◽

10.1177/0022034516677938 ◽

2016 ◽

Vol 96 (3) ◽

pp. 339-346 ◽

Cited By ~ 5

Author(s):

S. Miyauchi ◽

J. Kitagaki ◽

R. Masumoto ◽

A. Imai ◽

K. Kobayashi ◽

...

Keyword(s):

Mrna Expression ◽

Periodontal Ligament ◽

Type I Collagen ◽

Alveolar Bone ◽

Skeletal Development ◽

Aggressive Periodontitis ◽

Periodontal Ligament Cells ◽

Type I ◽

Phosphodiesterase 3 ◽

Pdl Cells

Sphingomyelin phosphodiesterase 3 ( Smpd3), which encodes neutral sphingomyelinase 2 (nSMase2), is a key molecule for skeletal development as well as for the cytodifferentiation of odontoblasts and alveolar bone. However, the effects of nSMase2 on the cytodifferentiation of periodontal ligament (PDL) cells are still unclear. In this study, the authors analyzed the effects of Smpd3 on the cytodifferentiation of human PDL (HPDL) cells. The authors found that Smpd3 increases the mRNA expression of calcification-related genes, such as alkaline phosphatase (ALPase), type I collagen, osteopontin, Osterix (Osx), and runt-related transcription factor (Runx)-2 in HPDL cells. In contrast, GW4869, an inhibitor of nSMase2, clearly decreased the mRNA expression of ALPase, type I collagen, and osteocalcin in HPDL cells, suggesting that Smpd3 enhances HPDL cytodifferentiation. Next, the authors used exome sequencing to evaluate the genetic variants of Smpd3 in a Japanese population with aggressive periodontitis (AgP). Among 44 unrelated subjects, the authors identified a single nucleotide polymorphism (SNP), rs145616324, in Smpd3 as a putative genetic variant for AgP among Japanese people. Moreover, Smpd3 harboring this SNP did not increase the sphingomyelinase activity or mRNA expression of ALPase, type I collagen, osteopontin, Osx, or Runx2, suggesting that this SNP inhibits Smpd3 such that it has no effect on the cytodifferentiation of HPDL cells. These data suggest that Smpd3 plays a crucial role in maintaining the homeostasis of PDL tissue.

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Effects of Daidzein on the Production of Type I Collagen and Matrix Metalloproteinase1 by Stretched Human Periodontal Ligament Cells

International Journal of Oral-Medical Sciences ◽

10.5466/ijoms.17.27 ◽

2018 ◽

Vol 17 (1) ◽

pp. 27-32

Author(s):

Masaru Yamaguchi ◽

Erika Nakayama ◽

Mami Shimizu ◽

Jun Kikuta ◽

Satoshi Horihata ◽

...

Keyword(s):

Periodontal Ligament ◽

Type I Collagen ◽

Periodontal Ligament Cells ◽

Type I ◽

Human Periodontal Ligament Cells

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Asiaticoside Induces Type I Collagen Synthesis and Osteogenic Differentiation in Human Periodontal Ligament Cells

Phytotherapy Research ◽

10.1002/ptr.4742 ◽

2012 ◽

Vol 27 (3) ◽

pp. 457-462 ◽

Cited By ~ 22

Author(s):

Nunthawan Nowwarote ◽

Thanaphum Osathanon ◽

Peachaya Jitjaturunt ◽

Sukuman Manopattanasoontorn ◽

Prasit Pavasant

Keyword(s):

Osteogenic Differentiation ◽

Periodontal Ligament ◽

Collagen Synthesis ◽

Type I Collagen ◽

Periodontal Ligament Cells ◽

Type I ◽

Human Periodontal Ligament Cells

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Morphologic study and syntheses of type I collagen and fibronectin of human periodontal ligament cells cultured on poly(ethylene-co-vinyl alcohol) (EVA) with collagen immobilization

Journal of Biomedical Materials Research ◽

10.1002/1097-4636(200102)54:2<241::aid-jbm11>3.0.co;2-p ◽

2000 ◽

Vol 54 (2) ◽

pp. 241-246 ◽

Cited By ~ 17

Author(s):

Chunyan Peng ◽

Sadami Tsutsumi ◽

Kazuaki Matsumura ◽

Naoki Nakajima ◽

Suong-Hyu Hyon

Keyword(s):

Vinyl Alcohol ◽

Periodontal Ligament ◽

Type I Collagen ◽

Periodontal Ligament Cells ◽

Type I ◽

Morphologic Study ◽

Human Periodontal Ligament Cells ◽

Poly Ethylene ◽

Collagen Immobilization ◽

Cells Cultured

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Autophagy facilitates type I collagen synthesis in periodontal ligament cells

Scientific Reports ◽

10.1038/s41598-020-80275-4 ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Tomomi Nakamura ◽

Motozo Yamashita ◽

Kuniko Ikegami ◽

Mio Suzuki ◽

Manabu Yanagita ◽

...

Keyword(s):

Periodontal Ligament ◽

Collagen Synthesis ◽

Type I Collagen ◽

Periodontal Diseases ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Physiological Role ◽

Type I ◽

Periodontal Tissue ◽

Pdl Cells

AbstractAutophagy is a lysosomal protein degradation system in which the cell self-digests its intracellular protein components and organelles. Defects in autophagy contribute to the pathogenesis of age-related chronic diseases, such as myocardial infarction and rheumatoid arthritis, through defects in the extracellular matrix (ECM). However, little is known about autophagy in periodontal diseases characterised by the breakdown of periodontal tissue. Tooth-supportive periodontal ligament (PDL) tissue contains PDL cells that produce various ECM proteins such as collagen to maintain homeostasis in periodontal tissue. In this study, we aimed to clarify the physiological role of autophagy in periodontal tissue. We found that autophagy regulated type I collagen synthesis by elimination of misfolded proteins in human PDL (HPDL) cells. Inhibition of autophagy by E-64d and pepstatin A (PSA) or siATG5 treatment suppressed collagen production in HPDL cells at mRNA and protein levels. Immunoelectron microscopy revealed collagen fragments in autolysosomes. Accumulation of misfolded collagen in HPDL cells was confirmed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. E-64d and PSA treatment suppressed and rapamycin treatment accelerated the hard tissue-forming ability of HPDL cells. Our findings suggest that autophagy is a crucial regulatory process that facilitates type I collagen synthesis and partly regulates osteoblastic differentiation of PDL cells.

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