A matricellular protein fibulin-4 is essential for the activation of lysyl oxidase
Kazuo Noda, Kaori Kitagawa, Takao Miki, Masahito Horiguchi, Tomoya O. Akama, Takako Taniguchi, Hisaaki Taniguchi, Kazuaki W. TAKAHASHI, Yasumitsu Ogra, Robert P. Mecham, Masahiko Terajima, Mitsuo Yamauchi, Tomoyuki Nakamura
Abstract
cells had lower activity than LOX produced by wild-type cells due to the absence of lysine tyrosyl quinone (LTQ), a unique cofactor required for LOX activity. Our studies showed that fibulin-4 is required for copper ion transfer from the copper transporter ATP7A to LOX in the trans-Golgi network (TGN), which is a necessary step for LTQ formation. These results uncover a pivotal role for fibulin-4 in the activation of LOX and, hence, in ECM assembly.
Topics & Concepts
FibulinLysyl oxidaseElastinExtracellular matrixChemistryLysineBiochemistryTropoelastinCell biologyAmino acidBiologyGeneticsMicrobial metabolism and enzyme functionConnective tissue disorders researchAortic aneurysm repair treatments