Functions and Mechanisms of Pro-Lysyl Oxidase Processing in Cancers and Eye Pathologies with a Focus on Diabetic Retinopathy
Lysyl oxidases are multifunctional proteins derived from five lysyl oxidase paralogues <i>(LOX)</i> and lysyl oxidase-like 1 through lysyl oxidase-like 4 (<i>LOXL1–LOXL4</i>). All participate in the biosynthesis of and maturation of connective tissues by catalyzing the oxidat...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-05-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/9/5088 |
| _version_ | 1797504402306629632 |
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| author | Philip C. Trackman Yaser Peymanfar Sayon Roy |
| author_facet | Philip C. Trackman Yaser Peymanfar Sayon Roy |
| author_sort | Philip C. Trackman |
| collection | DOAJ |
| description | Lysyl oxidases are multifunctional proteins derived from five lysyl oxidase paralogues <i>(LOX)</i> and lysyl oxidase-like 1 through lysyl oxidase-like 4 (<i>LOXL1–LOXL4</i>). 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 <i>LOX</i> 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 <i>LOX</i> 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. |
| first_indexed | 2024-03-10T04:04:06Z |
| format | Article |
| id | doaj.art-30de317da6db45219c2ec13d859a96d3 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T04:04:06Z |
| publishDate | 2022-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-30de317da6db45219c2ec13d859a96d32023-11-23T08:26:55ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-05-01239508810.3390/ijms23095088Functions and Mechanisms of Pro-Lysyl Oxidase Processing in Cancers and Eye Pathologies with a Focus on Diabetic RetinopathyPhilip C. Trackman0Yaser Peymanfar1Sayon Roy2The Forsyth Institute, 245 First Street, Cambridge, MA 02142, USAThe Forsyth Institute, 245 First Street, Cambridge, MA 02142, USADepartment of Medicine, Boston University School of Medicine, 650 Albany Street, Boston, MA 02118, USALysyl oxidases are multifunctional proteins derived from five lysyl oxidase paralogues <i>(LOX)</i> and lysyl oxidase-like 1 through lysyl oxidase-like 4 (<i>LOXL1–LOXL4</i>). 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 <i>LOX</i> 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 <i>LOX</i> 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.https://www.mdpi.com/1422-0067/23/9/5088lysyl oxidaselysyl oxidase propeptidestructure–functiondiabeteseye pathologies |
| spellingShingle | Philip C. Trackman Yaser Peymanfar Sayon Roy Functions and Mechanisms of Pro-Lysyl Oxidase Processing in Cancers and Eye Pathologies with a Focus on Diabetic Retinopathy International Journal of Molecular Sciences lysyl oxidase lysyl oxidase propeptide structure–function diabetes eye pathologies |
| title | Functions and Mechanisms of Pro-Lysyl Oxidase Processing in Cancers and Eye Pathologies with a Focus on Diabetic Retinopathy |
| title_full | Functions and Mechanisms of Pro-Lysyl Oxidase Processing in Cancers and Eye Pathologies with a Focus on Diabetic Retinopathy |
| title_fullStr | Functions and Mechanisms of Pro-Lysyl Oxidase Processing in Cancers and Eye Pathologies with a Focus on Diabetic Retinopathy |
| title_full_unstemmed | Functions and Mechanisms of Pro-Lysyl Oxidase Processing in Cancers and Eye Pathologies with a Focus on Diabetic Retinopathy |
| title_short | Functions and Mechanisms of Pro-Lysyl Oxidase Processing in Cancers and Eye Pathologies with a Focus on Diabetic Retinopathy |
| title_sort | functions and mechanisms of pro lysyl oxidase processing in cancers and eye pathologies with a focus on diabetic retinopathy |
| topic | lysyl oxidase lysyl oxidase propeptide structure–function diabetes eye pathologies |
| url | https://www.mdpi.com/1422-0067/23/9/5088 |
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