Intracellular interaction of EMILIN-1 with fibrillin-1 in human periodontal ligament cells

Nakatomi, Yuka; Tsuruga, Eichi; Yamauchi, Yoshinori; Kawagoe, Megumi; Yamanouchi, Kaori; Nakashima, Kazuki; Sawa, Yoshihiko; Ishikawa, Hiroyuki

doi:10.1016/j.odw.2012.01.002

Cited by 1 publication

(1 citation statement)

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“…Our data show that Emilin‐1 is also greatly reduced and disorganized by intrinsic and UV‐induced ageing. Whether a decrease of Emilin‐1 contributes to the breakdown of the fibres network remains to be elucidated but such an assumption seems reasonable since Emilin‐1 contribute to the initial assembly of pericellular Fibrillin‐1 during the process of oxytalan fibre formation and play a major part in the homeostasis of these fibres .…”

Section: Discussionmentioning

confidence: 99%

Localization, fate and interactions of Emilin‐1 in human skin

Fitoussi

Beauchef

Guéré

et al. 2019

Intern J of Cosmetic Sci

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Abstracts Objective Emilin‐1 is a versatile protein abundant in tissues where resilience and elastic recoil are prominent and interacting with components of the extracellular matrix. Still, little is known about Emilin‐1 in the skin. Therefore, we investigated Emilin‐1 in the skin, its localization, its fate upon ageing, its interactions with other proteins and the effect of its knockdown. Methods Skin explants from young or old Caucasian women, immunofluorescently labelled by anti‐Emilin‐1, anti‐Fibrillin‐1 and anti‐Elastin antibodies, were analysed using confocal microscopy. Skin explants subjected to UV‐induced skin ageing were also analysed. Colocalization of Emilin‐1 with Collagen IV, Fibrillin‐1 and Elastin was studied by multiphoton microscopy and co‐immunoprecipitation. Finally, the effect of Emilin‐1 extinction was studied by producing small interfering RNA (siRNA) knockdown fibroblasts and by analysing the outcome on selected genes. Results In skin sections from young donors, Emilin‐1 localizes similarly to Elastin and Fibrillin‐1. In the papillary dermis, it shows clear and ramified structures, perpendicular to the dermo‐epidermal junction that are reminiscent of the oxytalan fibres. In the reticular dermis, Emilin‐1 signal appears identical to that of the elastic fibres network. Upon intrinsic or UV‐induced ageing, the signal associated with Emilin‐1 is drastically reduced and disorganized. Multiphoton microscopy study shows that, as expected, Emilin‐1 colocalizes with Elastin. It also colocalizes with Collagen IV in the basement membrane and within dermal fibroblasts. Interaction of Emilin‐1 with Elastin and Collagen IV was also found by co‐immunoprecipitation. It also reveals interaction with Laminin‐5. Finally, siRNA‐mediated knockdown of EMILIN‐1 show little effect on the expression level of the 61 genes we studied. The most striking change is a downregulation of fibroblast growth factor receptor 2 that show a decrease similar to that of EMILIN‐1 itself and after 8 days a downregulation of COL6A1. Conclusion In skin, Emilin‐1 locates in the dermis, up to the basement membrane, interacting with components of the extracellular matrix but also with the anchoring complex. These interactions are important for cell adhesion, migration, proliferation and would suggest that Emilin‐1 might be important for maintaining the 3D structure of the extracellular matrix.

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Section: Discussionmentioning

confidence: 99%