학술논문
Influence of leptin and compression in GAS‐6 mediated homeostasis of periodontal ligament cell.
Document Type
Article
Source
Subject
*PROTEIN metabolism
*HOMEOSTASIS
*ADIPOKINES
*REVERSE transcriptase polymerase chain reaction
*OBESITY
*CELL migration
*STAINS & staining (Microscopy)
*LEPTIN
*ANIMAL experimentation
*WESTERN immunoblotting
*MICROBIOLOGICAL assay
*PERIODONTAL disease
*CELL survival
*CELL proliferation
*FLUORESCENT antibody technique
*GENE expression profiling
*MESSENGER RNA
*ENZYME-linked immunosorbent assay
*DESCRIPTIVE statistics
*MICE
*CASPASES
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Language
ISSN
1354-523X
Abstract
Growth arrest‐specific protein 6 (GAS‐6) regulates immunomodulatory and inflammatory mechanisms in periodontium and may participate in obesity predisposition. This study aimed to determine whether GAS‐6 is associated with the homeostasis of periodontal ligament (SV‐PDL) cells in the presence of adipokines or compressive forces. The SV‐PDL cell line was used. Western blots were employed for TAM receptors detection. Cells were stimulated using different concentrations of GAS‐6. The migration, viability, and proliferation were measured by a standard scratch test, MTS assay, and immunofluorescent staining. The mRNA expression was analyzed by RT‐PCR. Release of TGF‐β1, GAS‐6, and Axl were verified by ELISA. Western blot shows that TAM receptors are expressed in SV‐PDL cells. GAS‐6 has a promoting effect on cell migration and proliferation. RT‐PCR analysis showed that GAS‐6 induces Collagen‐1, Collagen‐3, Periostin, and TGF‐β1 mRNA expression whereas it reduces Caspase‐3, Caspase‐8, Caspase‐9, and IL‐6 mRNA expression. Further, secreted GAS‐6 in SV‐PDL is reduced in response to both compressive forces and leptin and upregulated by IL‐6. Additionally, ADAM‐10 inhibition reduces GAS‐6 and Axl release on SV‐PDL cells. TAM receptors especially Axl are identified as the receptors of GAS‐6. GAS‐6/TAM interactions contribute to periodontal ligament cells homeostasis. Leptin inhibits the GAS‐6 release independently of ADAM‐10 metalloprotease. [ABSTRACT FROM AUTHOR]