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Cell Biology and Functions of the Multifunctional Lysyl Oxidase Family of Proteins 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 20 April 2025 | Viewed by 7019

Special Issue Editor

Prof. Dr. Philip C. Trackman

E-Mail Website
Guest Editor
1. The Forsyth Institute, 245 First Street, Cambridge, MA 02142, USA
2. Department of Translational Dental Medicine, School of Dental Medicine, Boston University, 700 Albany Street, Boston, MA 02138, USA
Interests: diabetic bone disease; oral cancer; gingival overgrowth; lysyl oxidases biosynthesis and functions; extracellular matrix biosynthesis; extracellular matrix pathology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue is a continuation of our previous Special Issue, entitled "Cell Biology and Functions of the Multifunctional Lysyl Oxidase Family of Proteins".

The lysyl oxidase family of genes consists of five related paralogues, each possessing the active lysyl oxidase enzyme activity domain at the C-terminus of the corresponding proteins. All five enzymes participate in extracellular biosynthetic collagen and elastin cross-linking and maturation, critical for normal extracellular structure and function. The N-terminal propeptide regions are more variable between the five paralogues and exhibit their own functions. Some of these assist in coordinating cell signaling, in addition to other extracellular and cellular interactions and functions. Some examples include modulation of growth factor signaling, tumor suppression, basement membrane assembly, differentiation and functions of cells as diverse as endothelial cells, osteoblasts and megakaryocytes, macrophages, functional interactions with matricellular proteins, and coordination of elastin biosynthesis. Abnormal regulation, and lysyl oxidase mutations, can result in pathologies including cancer and vascular abnormalities. This Special Issue will compile new data, ideas and methodologies from active experts, helping to integrate the understanding of the latest findings in this ever-growing field, both in terms of health and disease.

Prof. Dr. Philip C. Trackman
Guest Editor

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Keywords

  • lysyl oxidases
  • cancer
  • tumor suppression
  • bone biology
  • gene polymorphisms and mutations
  • collagen cross-linking
  • elastin cross-linking
  • fibrosis
  • aneurysm

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Published Papers (2 papers)

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26 pages, 3886 KiB  
Review
LOXL2 in Cancer: A Two-Decade Perspective
by Amparo Cano, Pilar Eraso, María J. Mazón and Francisco Portillo
Int. J. Mol. Sci. 2023, 24(18), 14405; https://doi.org/10.3390/ijms241814405 - 21 Sep 2023
Cited by 7 | Viewed by 3466
Abstract
Lysyl Oxidase Like 2 (LOXL2) belongs to the lysyl oxidase (LOX) family, which comprises five lysine tyrosylquinone (LTQ)-dependent copper amine oxidases in humans. In 2003, LOXL2 was first identified as a promoter of tumour progression and, over the course of two decades, numerous [...] Read more.
Lysyl Oxidase Like 2 (LOXL2) belongs to the lysyl oxidase (LOX) family, which comprises five lysine tyrosylquinone (LTQ)-dependent copper amine oxidases in humans. In 2003, LOXL2 was first identified as a promoter of tumour progression and, over the course of two decades, numerous studies have firmly established its involvement in multiple cancers. Extensive research with large cohorts of human tumour samples has demonstrated that dysregulated LOXL2 expression is strongly associated with poor prognosis in patients. Moreover, investigations have revealed the association of LOXL2 with various targets affecting diverse aspects of tumour progression. Additionally, the discovery of a complex network of signalling factors acting at the transcriptional, post-transcriptional, and post-translational levels has provided insights into the mechanisms underlying the aberrant expression of LOXL2 in tumours. Furthermore, the development of genetically modified mouse models with silenced or overexpressed LOXL2 has enabled in-depth exploration of its in vivo role in various cancer models. Given the significant role of LOXL2 in numerous cancers, extensive efforts are underway to identify specific inhibitors that could potentially improve patient prognosis. In this review, we aim to provide a comprehensive overview of two decades of research on the role of LOXL2 in cancer. Full article
(This article belongs to the Special Issue Cell Biology and Functions of the Multifunctional Lysyl Oxidase Family of Proteins 2.0)
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20 pages, 2620 KiB  
Review
Exploring the Interplay between Polyphenols and Lysyl Oxidase Enzymes for Maintaining Extracellular Matrix Homeostasis
by Carolina Añazco, Janin Riedelsberger, Lorenzo Vega-Montoto and Armando Rojas
Int. J. Mol. Sci. 2023, 24(13), 10985; https://doi.org/10.3390/ijms241310985 - 1 Jul 2023
Cited by 11 | Viewed by 3112
Abstract
Collagen, the most abundant structural protein found in mammals, plays a vital role as a constituent of the extracellular matrix (ECM) that surrounds cells. Collagen fibrils are strengthened through the formation of covalent cross-links, which involve complex enzymatic and non-enzymatic reactions. Lysyl oxidase [...] Read more.
Collagen, the most abundant structural protein found in mammals, plays a vital role as a constituent of the extracellular matrix (ECM) that surrounds cells. Collagen fibrils are strengthened through the formation of covalent cross-links, which involve complex enzymatic and non-enzymatic reactions. Lysyl oxidase (LOX) is responsible for catalyzing the oxidative deamination of lysine and hydroxylysine residues, resulting in the production of aldehydes, allysine, and hydroxyallysine. These intermediates undergo spontaneous condensation reactions, leading to the formation of immature cross-links, which are the initial step in the development of mature covalent cross-links. Additionally, non-enzymatic glycation contributes to the formation of abnormal cross-linking in collagen fibrils. During glycation, specific lysine and arginine residues in collagen are modified by reducing sugars, leading to the creation of Advanced Glycation End-products (AGEs). These AGEs have been associated with changes in the mechanical properties of collagen fibers. Interestingly, various studies have reported that plant polyphenols possess amine oxidase-like activity and can act as potent inhibitors of protein glycation. This review article focuses on compiling the literature describing polyphenols with amine oxidase-like activity and antiglycation properties. Specifically, we explore the molecular mechanisms by which specific flavonoids impact or protect the normal collagen cross-linking process. Furthermore, we discuss how these dual activities can be harnessed to generate properly cross-linked collagen molecules, thereby promoting the stabilization of highly organized collagen fibrils. Full article
(This article belongs to the Special Issue Cell Biology and Functions of the Multifunctional Lysyl Oxidase Family of Proteins 2.0)
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