lysyl oxidase

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ly·syl ox·i·dase

an enzyme, which requires Cu2+ and O2, that oxidizes certain lysyl residues in collagen to allysyl residues and hydroxylysyl residues to hydroxyallysyl residues; this is a required step for the cross-linking (via aldol condensations and through Amadori rearrangements) of collagen strands; a lower activity of this enzyme is associated with occipital horn syndrome.
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Lysyl oxidase

An enzyme required for the crosslinking of elastin and collagen molecules to form properly functioning connective tissue; present in relatively low levels in at least some forms of cutis laxa.
Mentioned in: Cutis Laxa
Gale Encyclopedia of Medicine. Copyright 2008 The Gale Group, Inc. All rights reserved.
References in periodicals archive ?
Lysyl oxidase enhances the deposition of tropoelastin through the catalysis of tropoelastin molecules on the cell surface.
This can be reduced by the inhibition of lysyl oxidase, a key enzyme involved in collagen crosslinking (29).
Martinez-Gonzalez, "Lysyl oxidase as a potential therapeutic target," Drug News & Perspectives, vol.
Kagan, "Lysyl oxidase: an oxidative enzyme and effector of cell function," Cellular and Molecular Life Sciences, vol.
(2) in ER [right arrow] preprocollagen, (3) ER Lumen [right arrow] signal peptides cleaved; proline and lysine hydroxylation, 2 pro-alpha1 and 1 pro-alpha2 chains [right arrow] Type I procollagen, triple helix formed [right arrow] (4) in Golgi packaged and secreted [right arrow] (5) outside cell propeptides cleaved [right arrow] tropocollagen fibrils formed, (6) lysyl oxidase creates intramolecular and intermolecular cross-links.
BAPN leads to lathyrism by inhibiting lysyl oxidase, which is an important enzyme in the synthesis of collagen and elastin.
Congenital cutis laxa and lysyl oxidase deficiency.
Hypoxia-induced lysyl oxidase is a critical mediator of bone marrow cell recruitment to form the premetastatic niche.
Copper is a cofactor for lysyl oxidase, an enzyme involved in the maturation or cross-linking of collagen to form stable fibrils upon which calcium is deposited to form bone.
Through a molecular approach called differential display analysis, Hendrix's team identified the gene lysyl oxidase and a zinc finger transcription factor in highly aggressive breast cancer cells that spread.
A collagen-specific enzyme, lysyl oxidase, crosslinks these trimers into fibrils or meshworks.