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J Cell Commun Signal. 2018 Mar;12(1):45-53. doi: 10.1007/s12079-017-0424-4. Epub 2017 Oct 30.

Functional importance of lysyl oxidase family propeptide regions.

Author information

1
Henry M. Goldman School of Dental Medicine, Department of Molecular and Cell Biology, Boston University, 700 Albany Street, W-201, Boston, MA, 02118, USA. trackman@bu.edu.

Abstract

The lysyl oxidase family of proteins is primarily known for its critical role in catalyzing extracellular oxidative deamination of hydroxylysine and lysine residues in collagens, and lysine residues in elastin required for connective tissue structure and function. Lysyl oxidases have additional important biological functions in health and disease. While the enzyme domains are highly conserved, the propeptide regions are less uniform, and have biological activity, some of which are independent of their respective enzymes. This review summarizes what has been published regarding the functions of the propeptide regions of this family of proteins in the context of extracellular matrix biosynthesis, fibrosis and cancer biology. Although much has been learned, there is a need for greater attention to structure/function relationships and mechanisms to more fully understand these multifunctional proteins.

KEYWORDS:

Cancer; Extracellular matrix; Fibrosis; Lysyl oxidases; Propeptides

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