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Protein-lysine 6-oxidase

GeneName

LOX

Summary

LOX, also known as lysyl oxidase, LAAO, or Lao, is a 47 kDa secreted enzyme that plays a crucial role in the cross-linking of collagen and elastin in the extracellular matrix. It is predominantly found in the extracellular space and is involved in various biological processes, including collagen fibril organisation, blood vessel morphogenesis, and connective tissue development. LOX exhibits molecular functions such as collagen binding, copper ion binding, and protein-lysine 6-oxidase activity, contributing to its role in tissue integrity and repair. Additionally, it is implicated in the regulation of cellular responses to chemokines and various signalling pathways, including those associated with muscle and bone development.

Importance

LOX is relevant to: - Tissue remodelling and repair, particularly in the context of fibrosis and wound healing - Vascular biology, as it influences blood vessel formation and integrity - Cancer progression, where altered LOX activity can affect tumour microenvironment and metastasis - Bone health, due to its role in osteoblast differentiation and bone mineralisation - Cardiovascular diseases, given its involvement in heart and aorta development and function

Top Products

For researchers investigating LOX, we recommend two excellent primary antibodies. The first is the well-cited polyclonal antibody, Anti-LOX antibody (ab31238), which has garnered 84 citations and is particularly effective for Western blotting (WB). This product is trusted by many in the field for its reliable performance. Additionally, we offer the recombinant antibody, Anti-LOX antibody [EPR4025] (ab174316), which has been validated in knockout models and is suitable for a broader range of applications, including WB, immunohistochemistry (IHC), immunocytochemistry (ICC), flow cytometry (FC), and immunoprecipitation (IP). With 68 citations, this recombinant antibody is a versatile choice, providing the consistency and reliability that researchers often seek.

Abcam Product Citation Summary

The data indicates that LOX antibodies are frequently used in studies related to tissue composition and disease contexts, particularly in mouse models and human tissues. The studies focus on conditions such as altered extracellular matrix composition, liver fibrosis, and idiopathic pulmonary fibrosis, highlighting the relevance of LOX in these pathological processes.

Abcam Product Citation Table

Product Code
Species
Application
Study Context
PMID
ab174316
Mouse
WB, IHC-IF
Altered peritoneal ECM composition due to ApoE loss
29458390
ab174316
Human
IHC
Cancer
32286443
ab174316
Mouse
WB
Liver fibrosis
32296422
ab31238
Human
WB, IHC
Idiopathic pulmonary fibrosis (IPF)
29125826

Function

Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:26838787). Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity).

Involvement in disease

Aortic aneurysm, familial thoracic 10

AAT10

A form of thoracic aortic aneurysm, a disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.

Proteolytically cleaved by BMP1 which removes the propeptide (PubMed:31152061). Also proteolytically cleaved by ADAMTS2 and ADAMTS14, but not by ADAMTS3, at an additional cleavage site downstream of the BMP1 cleavage site (PubMed:31152061). The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin (By similarity). Cleavage by BMP1 to remove the propeptide does not increase enzymatic activity but increases binding to collagen (PubMed:31152061). Cleavage by ADAMTS2 produces a form with reduced collagen-binding activity (PubMed:31152061).

Sulfated at Tyr-187 and also at either Tyr-183 or Tyr-184 which enhances binding to collagen.

Sequence Similarities

Belongs to the lysyl oxidase family.

Tissue Specificity

Heart, placenta, skeletal muscle, kidney, lung and pancreas.

Cellular localization

Alternative names

Protein-lysine 6-oxidase, Lysyl oxidase, LOX

swissprot:P28300 entrezGene:4015 omim:153455