スギモト マサズミ   Sugimoto Masazumi
  杉本 雅純
   所属   東邦大学  理学部 生物分子科学科
   職種   教授
論文種別 原著
言語種別 英語
査読の有無 査読あり
表題 Myosin II activity is required for functional leading-edge cells and closure of epidermal sheets in fish skin ex vivo.
掲載誌名 正式名:Cell and Tissue Research
略  称:Cell Tissue Res
ISSNコード:0302766X/14320878
巻・号・頁 345(3),379-90頁
著者・共著者 Morita T, Tsuchiya A, Sugimoto M.
発行年月 2011/08
概要 Re-epithelialization in skin wound healing is a process in which epidermal sheets grow and close the wound. Although the actin-myosin system is thought to have a pivotal role in re-epithelialization, its role is not clear. In fish skin, re-epithelialization occurs around 500 mum/h and is 50 times faster than in mammalian skin. We had previously reported that leading-edge cells of the epidermal outgrowth have both polarized large lamellipodia and "purse string"-like actin filament cables in the scale-skin culture system of medaka fish, Oryzias latipes (Cell Tissue Res, 2007). The actin purse-string (APS) is a supracellular contractile machinery in which adherens junctions (AJs) link intracellular myosin II-including actin cables between neighboring cells. In this study, we developed a modified "face-to-face" scale-skin culture system as an ex vivo model to study epidermal wound healing, and examined the role of the actin-myosin system in the rapid re-epithelialization using a myosin II ATPase inhibitor, blebbistatin. A low level of blebbistatin suppressed the formation of APS and induced the dissociation of keratocytes from the leading edge without attenuating the growth of the epidermal sheet or the migration rate of solitary keratocytes. AJs in the superficial layer showed no obvious changes elicited by blebbistatin. However, two epidermal sheets without APSs did not make a closure with each other, which was confirmed by inhibiting the connecting AJs between the superficial layers. These results suggest that myosin II activity is required for functional leading-edge cells and for epidermal closure.
DOI 10.1007/s00441-011-1219-1
文献番号 21847608/PubMedID