Autor: |
Trackman PC; The Forsyth Institute, 245 First Street, Cambridge, MA 02142, USA.; Department of Translational Dental Medicine, Boston University Henry M Goldman School of Dental Medicine, 700 Albany Street, Boston, MA 02118, USA., Peymanfar Y; The Forsyth Institute, 245 First Street, Cambridge, MA 02142, USA., Roy S; Department of Medicine, Boston University School of Medicine, 650 Albany Street, Boston, MA 02118, USA. |
Jazyk: |
angličtina |
Zdroj: |
International journal of molecular sciences [Int J Mol Sci] 2022 May 03; Vol. 23 (9). Date of Electronic Publication: 2022 May 03. |
DOI: |
10.3390/ijms23095088 |
Abstrakt: |
Lysyl oxidases are multifunctional proteins derived from five lysyl oxidase paralogues (LOX) and lysyl oxidase-like 1 through lysyl oxidase-like 4 ( LOXL1-LOXL4 ). All participate in the biosynthesis of and maturation of connective tissues by catalyzing the oxidative deamination of lysine residues in collagens and elastin, which ultimately results in the development of cross-links required to function. In addition, the five LOX genes have been linked to fibrosis and cancer when overexpressed, while tumor suppression by the propeptide derived from pro-LOX has been documented. Similarly, in diabetic retinopathy, LOX overexpression, activity, and elevated LOX propeptide have been documented. The proteolytic processing of pro-forms of the respective proteins is beginning to draw attention as the resultant peptides appear to exhibit their own biological activities. In this review we focus on the LOX paralogue, and what is known regarding its extracellular biosynthetic processing and the still incomplete knowledge regarding the activities and mechanisms of the released lysyl oxidase propeptide (LOX-PP). In addition, a summary of the roles of both LOX and LOX-PP in diabetic retinopathy, and brief mentions of the roles for LOX and closely related LOXL1 in glaucoma, and keratoconus, respectively, are included. |
Databáze: |
MEDLINE |
Externí odkaz: |
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