Elsevier

Genomics

Volume 74, Issue 2, 1 June 2001, Pages 211-218
Genomics

Regular Article
Central Nervous System, Uterus, Heart, and Leukocyte Expression of the LOXL3 Gene, Encoding a Novel Lysyl Oxidase-Like Protein

https://doi.org/10.1006/geno.2001.6545Get rights and content

Abstract

A BLASTN search using the mouse lor-2 cDNA identified three overlapping ESTs (AI752772, AA852888, and R55706) in the GenBank database. These expressed sequence tags were assembled into a contig of 3121 nucleotides with an open reading frame of 2262 bp. The encoded putative polypeptide of 754 amino acids presented all structural characteristics of the lysyl oxidase (LOX) enzyme family, a copper-binding site with four histidyl residues, the lysyl and tyrosyl residues known to be involved in LOX enzyme in the formation of the quinone cofactor and surrounding sequences, and the cytokine receptor-like domain. In addition, four scavenger receptor cysteine-rich (SRCR) domains were found in the N-terminal region of the protein. The gene encoding this new cDNA, which we have referred to as human lysyl oxidase-like 3 (humanLOXL3), has been mapped to chromosome 2p13.3, overlapping at its 3′ end the HtrA2 serine protease gene. The structure of the humanLOXL3 gene was deduced from the BAC clone bac91a19 sequence and contained 14 exons. The expression pattern of this new member of the LOX gene family appears to be different from that of the LOX and LOX-like genes, as the central nervous system, neurons, and also leukocytes expressed humanLOXL3. A BLASTN search of the human EST database indicated the presence of ESTs, corresponding to alternative splice variants of LOXL3, that lacked exon 5 and exon 8. The putative resulting protein retained the region encoding the structural and functional elements of the amine oxidase but the second and fourth SRCR domains were truncated and the potential BMP-1 cleavage site was not present. The presence of domains unrelated to the traditional amine oxidase activity is a strong indication that humanLOXL3 might fulfill other functions in addition to intrinsic enzyme activity.

References (25)

Cited by (64)

  • Lysyl oxidases: Emerging biomarkers and therapeutic targets for various diseases

    2020, Biomedicine and Pharmacotherapy
    Citation Excerpt :

    Therapeutic targeting of extracellular proteins has attracted considerable attention in curing human diseases. The Lysyl oxidase (LOX) family, a type of secreted copper-containing amine oxidases, is comprised of five paralogues in mammals, LOX and four LOX-like proteins (LOXL1-4) [1–4]. They have been traditionally defined as key enzymes that catalyze covalent cross-linkage of collagen and elastin in the extracellular matrix (ECM), thereby maintaining the tensile strength and structural integrity of many tissues [5,6], although the contribution of each isoenzyme to covalent cross-linkages and their substrate specificity are mysterious.

  • Lysyl oxidase like-2 in fibrosis and cardiovascular disease

    2023, American Journal of Physiology - Cell Physiology
View all citing articles on Scopus

Sequence data from this article have been deposited with the EMBL/GenBank Data Libraries under Accession No. AF311313.

1

To whom correspondence should be addressed. Telephone: (808) 956-9575. Fax: (808) 956-9481. E-mail: [email protected].

View full text