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Micallef, J., Taccone, M., Mukherjee, J., Croul, S., Busby, J., Moran, M.F. and Guha, A. (2009) Epidermal growth factor receptor variant III-induced glioma invasion is mediated through myristoylated alanine-rich protein kinase C substrate overexpression. Cancer research, 69, 7548-7556. doi:10.1158/0008-5472.CAN-08-4783

has been cited by the following article:

• TITLE: Dephosphorylation of myristoylated alanine-rich C kinase substrate accelerates wound-induced migration of SH-SY5Y cells

  AUTHORS: Atsuhiro Tanabe, Mitsuya Shiraishi, Yasuharu Sasaki

  KEYWORDS: Wound Healing; MARCKS; Phosphorylation/Dephosphorylation; Cell Migration; Inflammation; ROCK

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.8B, August 8, 2013

  ABSTRACT: Inflammation, which is induced after infection of bacteria and tissue injury, is one of the important early stages of wound healing. Bradykinin is increased during acute and chronic inflammation. We previously reported that bradykinin stimulation induces dephosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) after phosphorylation by ROCK leading neurite outgrowth in neuroblastoma SH-SY5Y cells. In this report we showed that knock-down of MARCKS by RNAi reduced cell migration. Wild-type MARCKS-overexpressed SH-SY5Y cells migrated faster than the control cells. Unphosphorylatable MARCKS-overexpressed cells notably migrated fast. Moreover, chronic MARCKS dephosphorylation by a ROCK inhibitor HA-1077 promoted the cell migration, on the other hand a PKC inhibitor Ro-31-8220 did not. After wounding, MARCKS was transiently phosphorylated and dephospho-rylated by 20 min. Immunocytochemistry showed that the dephosphorylated MARCKS was localized at neurite tips. These findings suggest that MARCKS dephosphorylation is important in wound-induced migration of SH-SY5Y cells. It indicates the possibility that MARCKS is associated with wound repair after inflammation.