LOXL3-sv2, a novel variant of human lysyl oxidase-like 3 (LOXL3), functions as an amine oxidase

Jeong,Chankyu; Kim,Youngho

doi:10.3892/ijmm.2017.2862

LOXL3-sv2, a novel variant of human lysyl oxidase-like 3 (LOXL3), functions as an amine oxidase

Authors:
- Chankyu Jeong
- Youngho Kim
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Affiliations: Department of Biochemistry, Wonkwang University School of Medicine, Institute of Wonkwang Medical Science, Iksan, Jeonbuk 570-749, Republic of Korea
Published online on: January 19, 2017 https://doi.org/10.3892/ijmm.2017.2862
Pages: 719-724

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Abstract

Human lysyl oxidase-like 3 (LOXL3) functions as a copper-dependent amine oxidase toward collagen and elastin. The LOXL3 protein contains four scavenger receptor cysteine-rich (SRCR) domains in the N-terminus in addition to the C-terminal characteristic domains of the lysyl oxidase (LOX) family, such as a copper-binding domain, a cytokine receptor‑like domain and residues for the lysyl-tyrosyl quinone cofactor. Using BLASTN searches, we identified a novel variant of LOXL3 (termed LOXL3-sv2), which lacked the sequences corresponding to exons 4 and 5 of LOXL3. The LOXL3-sv2 mRNA is at least 2,398 bp in length, encoding a 608 amino acid-long polypeptide with a calculated molecular mass of 67.4 kDa. The deletion of exons 4 and 5 do not change the open-reading frame of LOXL3 but results in deletion of the SRCR domain 2. The recombinant LOXL3-sv2 protein showed a β-aminopropionitrile-inhibitable amine oxidase activity toward collagen type I. In RT-PCR analysis, LOXL3-sv2 was detected in all human tissues tested, along with LOXL3 and LOXL3-sv1, a previously identified variant of LOXL3. These findings indicate that the human LOXL3 gene encodes at least three variants, LOXL3, LOXL3-sv1 and LOXL3-sv2, all of which function as amine oxidases.

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