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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Lysyl oxidase-like 4

LOXL4, lysyl oxidase-like 4
This gene encodes a member of the lysyl oxidase gene family. The prototypic member of the family is essential to the biogenesis of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. A highly conserved amino acid sequence at the C-terminus end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The N-terminus is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: lysyl oxidase, LOXL2, Lol, elastin, CAN
Papers on LOXL4
Lysyl oxidase like-4 monoclonal antibody demonstrates therapeutic effect against head and neck squamous cell carcinoma cells and xenografts.
Hoffmann et al., Kiel, Germany. In Int J Cancer, Feb 2016
UNASSIGNED: A new member of the lysyl oxidase (LOX) family, lysyl oxidase-like 4 (LOXL4), is overexpressed in head and neck squamous cell carcinoma (HNSCC) compared to normal squamous epithelium.
The presence of lysyl oxidase-like enzymes in human control and keratoconic corneas.
Jirsova et al., Praha, Czech Republic. In Histol Histopathol, Jan 2016
No prominent differences were detected using IHC for LOXL4, but a slight decrease was observed in KC corneas using Western blot analysis.
Accumulation and Changes in Composition of Collagens in Subcutaneous Adipose Tissue After Bariatric Surgery.
Clément et al., Paris, France. In J Clin Endocrinol Metab, Jan 2016
Expression levels of genes encoding ECM components (eg, COL3A1, COL6A1, COL6A2, ELN), cross-linking enzymes (eg, lysyl oxidase [LOX], LOXL4, transglutaminase), metalloproteinases, and their inhibitors were modified 1 year after BS.
Differential Expression of LOXL4 in Normal and Tumor Tissue Samples of Laryngeal Squamous Cell Carcinoma.
Ozen et al., İstanbul, Turkey. In Clin Otolaryngol, Aug 2015
LOXL4 is expressed in several tissues and its expression has been shown to display a significant correlation with local lymph node metastasis.
A new role for LOX and LOXL2 proteins in transcription regulation.
Peiró et al., Barcelona, Spain. In Febs J, May 2015
The lysyl oxidase (LOX) family of proteins (LOX and LOXL1-LOXL4) oxidize amino groups located in the ε-position in lysines to generate an aldehyde group.
Characterisation of seven newly established head and neck squamous cell carcinoma cell lines.
Hoffmann et al., Kiel, Germany. In Eur Arch Otorhinolaryngol, May 2015
Overexpression of LOXL4 and Pim-1 proteins as distinctive features of head and neck carcinomas were shown in all seven cell lines.
Lysyl oxidase-like 4 (LOXL4) promotes proliferation and metastasis of gastric cancer via FAK/Src pathway.
Zhang et al., Shanghai, China. In J Cancer Res Clin Oncol, Feb 2015
BACKGROUND: Lysyl oxidase-like 4 (LOXL4) has been found up-regulated in a variety of human malignancies, but its clinical significance and functional roles in gastric cancer (GC) remain unknown.
Targeting lysyl oxidase for molecular imaging in breast cancer.
Löser et al., Edmonton, Canada. In Breast Cancer Res, 2014
INTRODUCTION: Lysyl oxidase (LOX; ExPASy ENZYME entry: EC and members of the LOX-like family, LOXL1-LOXL4, are copper-dependent enzymes that can modify proteins of the extracellular matrix.
LOXL4 is downregulated in hepatocellular carcinoma with a favorable prognosis.
Shi et al., Shanghai, China. In Int J Clin Exp Pathol, 2014
Lysyl oxidase like 4 (LOXL4), a member of the secreted copper-dependent amine oxidases that contribute to the assemble and maintenance of the extracellular matrix (ECM), was found to be up-regulated or down-regulated in different cancer types, suggesting its paradoxical roles in cancer.
Identification of the involvement of LOXL4 in generation of keratocystic odontogenic tumors by RNA-Seq analysis.
Li et al., Beijing, China. In Int J Oral Sci, 2014
Expression of lysyl oxidase-like 4 (LOXL4), the only candidate gene that encodes a secreted protein, was enhanced at both the mRNA and protein levels in KCOT stromal tissues and primary KCOT stromal fibroblasts compared to control tissues and primary fibroblasts (P<0.05).
Prospective isolation of human bone marrow stromal cell subsets: A comparative study between Stro-1-, CD146- and CD105-enriched populations.
Oreffo et al., Southampton, United Kingdom. In J Tissue Eng, 2013
Molecular analysis of a number of select osteogenic and potential osteo-predictive genes including ALP, CADM1, CLEC3B, DCN, LOXL4, OPN, POSTN and SATB2 showed Stro-1+ and CD146+ populations possessed similar expression profiles.
miR-193a-3p regulates the multi-drug resistance of bladder cancer by targeting the LOXL4 gene and the oxidative stress pathway.
Zhu et al., Hefei, China. In Mol Cancer, 2013
We further demonstrated that lysyl oxidase-like 4 (LOXL4) gene [GenBank: NM_032211.6] is a direct target of miR-193a-3p and executes the former's impact on bladder cancer chemoresistance.
Genes responsible for vaginal extracellular matrix metabolism are modulated by women's reproductive cycle and menopause.
Alarab et al., Toronto, Canada. In Int Braz J Urol, 2013
RESULTS: According to the phase of menstrual cycle, MMP1 was significantly reduced (p = 0.003), whereas the expression of TIMP1 and LOXL4 was significantly up-regulated during proliferative phase (both p < 0.01) when compared to the secretory phase in premenopausal control women.
Molecular mechanisms mediating metastasis of hypoxic breast cancer cells.
Semenza, Baltimore, United States. In Trends Mol Med, 2012
Recently, HIFs have been shown to play critical roles in the metastasis of breast cancer to the lungs through the transcriptional activation of genes encoding angiopoietin-like 4 and L1 cell adhesion molecule, which promote the extravasation of circulating cancer cells from the lung vasculature, and the lysyl oxidase family members LOX, LOXL2, and LOXL4, which promote invasion and metastatic niche formation.
Single-nucleotide polymorphisms in the lysyl oxidase-like protein 4 and complement component 3 genes are associated with increased risk for endometriosis and endometriosis-associated infertility.
Flores et al., Ponce, Puerto Rico. In Fertil Steril, 2011
SNPs in the lysyl oxidase-like protein 4 and complement component 3 genes are associated with increased risk for endometriosis and endometriosis-associated infertility in a Puerto Rican population.
Common polymorphisms in human lysyl oxidase genes are not associated with the adolescent idiopathic scoliosis phenotype.
Muglia et al., Nashville, United States. In Bmc Med Genet, 2010
The human lysyl oxidase-like 4 gene does not confer increased genotypic risk for adolescent idiopathic scoliosis.
LOXL4 as a selective molecular marker in primary and metastatic head/neck carcinoma.
Görögh et al., Bochum, Germany. In Anticancer Res, 2010
Overexpression of the lysyl oxidase-like 4 gene is associated with metastatic head/neck carcinoma.
Lysyl oxidase-like 4 is alternatively spliced in an anatomic site-specific manner in tumors involving the serosal cavities.
Reich et al., Jerusalem, Israel. In Virchows Arch, 2009
In breast carcinoma, LOXL4 was expressed only in the effusion samples. In malignant mesothelioma, LOXL4 and its splice variants were expressed at all sites.
Functional analysis of the 5' flanking domain of the LOXL4 gene in head and neck squamous cell carcinoma cells.
Csiszar et al., Kiel, Germany. In Int J Oncol, 2008
Functional analysis of the 5' flanking domain of the LOXL4 gene in head and neck squamous cell carcinoma cells.
Structural and functional diversity of lysyl oxidase and the LOX-like proteins.
Csiszar et al., Honolulu, United States. In Biochim Biophys Acta, 2003
Lysyl oxidase (LOX) and four lysyl oxidase-like proteins, LOXL, LOXL2, LOXL3 and LOXL4, each contain a copper binding site, conserved lysyl and tyrosyl residues that may contribute to quinone co-factor formation, and a cytokine receptor-like domain.
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