作者: H. A. Lucero , H. M. Kagan
DOI: 10.1007/S00018-006-6149-9
关键词: Proteolysis 、 Lysyl oxidase 、 Elastin 、 LOXL2 、 Lysine 、 Extracellular matrix 、 Protein oxidation 、 Biology 、 Effector 、 Biochemistry
摘要: Lysyl oxidase (LOX) oxidizes the side chain of peptidyl lysine converting specific residues to α-aminoadipic-δ-semialdehyde. This posttranslational chemical change permits covalent crosslinking component chains collagen and those elastin, thus stabilizing fibrous deposits these proteins in extracellular matrix. Four LOX-like (LOXL) with varying degrees similarity LOX have been described, constituting a family related proteins. is synthesized as preproprotein which emerges from cell proLOX then processed active enzyme by proteolysis. In addition elastin collagen, can oxidize within variety cationic proteins, suggesting that its functions extend beyond role stabilization Indeed, recent findings reveal LOXL markedly influence behavior including chemotactic responses, proliferation, shifts between normal malignant phenotypes.