2009•PubMedOpen access

Lysyl oxidases in mammalian development and certain pathological conditions.

Joni M. Mäki

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Abstract

Lysyl oxidase (LOX) catalyzes the oxidation of the side chain of a peptidyl lysine converting specific lysine and hydroxylysine residues of alpha-aminoadipic-delta-semialdehydes, which form covalent crosslinks in collagens and elastin. Five different but closely related lysyl oxidase isoenzymes have been identified to date, and they seem to have overlapping functions in many tissues. Modification of the extracellular matrix by lysyl oxidases has been shown to be a critical contributor to the development of various organs and certain pathological conditions.

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Lysyl oxidase (LOX) catalyzes the oxidation of the side chain of a peptidyl lysine converting specific lysine and hydroxylysine residues of alpha-aminoadipic-delta-semialdehydes, which form covalent crosslinks in collagens and elastin. Five different but closely related lysyl oxidase isoenzymes have been identified to date, and they seem to have overlapping functions in many tissues. Modification of the extracellular matrix by lysyl oxidases has been shown to be a critical contributor to the development of various organs and certain pathological conditions.

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Available abstract

Lysyl oxidase (LOX) catalyzes the oxidation of the side chain of a peptidyl lysine converting specific lysine and hydroxylysine residues of alpha-aminoadipic-delta-semialdehydes, which form covalent crosslinks in collagens and elastin. Five different but closely related lysyl oxidase isoenzymes have been identified to date, and they seem to have overlapping functions in many tissues. Modification of the extracellular matrix by lysyl oxidases has been shown to be a critical contributor to the development of various organs and certain pathological conditions.

Key concepts: Lysyl oxidase, Hydroxylysine, Elastin, Lysine, Extracellular matrix, Biochemistry, Chemistry, Isozyme

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