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Microarray of lysyl oxidase-like 2 (LOXL2)-overexpressing human buccal SCC TW2.6 and hypopharyngeal SCC FaDu cells against respective vector controls

ABSTRACT: To investigated the effects of LOXL2 overexpression in HNSCC TW2.6/FaDu cells. 8 samples

ORGANISM(S): Homo sapiens

PROVIDER: GSE201040 | GEO | 2022/04/22

REPOSITORIES: GEO

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Microarray of lysyl oxidase-like 2 (LOXL2)-overexpressing human buccal SCC TW2.6 and hypopharyngeal SCC FaDu cells against respective vector controls

Project description:Microarray of lysyl oxidase-like 2 (LOXL2)-overexpressing human buccal SCC TW2.6 and hypopharyngeal SCC FaDu cells against respective vector controls

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A novel Lysyl oxidase like 2 alternative splicing LOXL2 â³e13 in esophageal squamous carcinoma cells

Project description:A novel alternative splicing isoform of LOXL2 â³e13 was expressed ubiquitously in all cell lines and ESCC tissues. In contrast to the impaired deamination enzymatic activity compared with full length LOXL2, LOXL2 â³e13 showed an enhanced ability to promote cell mobility and invasiveness in ESCC cells than full length LOXL2 through a different mechanism. We used cDNA microarrays to identify genes that were differentially expressed upon LOXL2 â³ e13 overexpressed. For this purpose, we selected LOXL2 â³ e13, WT and empty vector control transfeced ESCC KYSE150 cell lines. Total RNA was extracted,compare the gene expression patterns between LOXL2 â³e13, LOXL2 WT and empty vector control transfected cells through the Genechip Primeview Human Gene Expression Array.

2016-07-03 | E-GEOD-53676 | biostudies-arrayexpress

A novel Lysyl oxidase like 2 alternative splicing LOXL2 △e13 in esophageal squamous carcinoma cells

Project description:A novel alternative splicing isoform of LOXL2 △e13 was expressed ubiquitously in all cell lines and ESCC tissues. In contrast to the impaired deamination enzymatic activity compared with full length LOXL2, LOXL2 △e13 showed an enhanced ability to promote cell mobility and invasiveness in ESCC cells than full length LOXL2 through a different mechanism.

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Lysyl oxidase-like 2 (LOXL2) a new regulator of cell polarity required for metastatic dissemination of basal-like breast carcinomas

Project description:Basal-like breast carcinoma is characterized by the expression of basal/myoepithelial markers, undifferentiated phenotype, highly aggressive behaviour and a frequent triple negative status (ESR-, PR-, Her2neu-). We have previously shown that epithelial-mesenchymal transition (EMT) occurs in basal-like breast tumours and identified Lysyl- Oxidase-Like 2 (LOXL2) as an EMT player and a poor prognosis marker in squamous cell carcinomas. We now show that LOXL2 mRNA is overexpressed in basal-like human breast carcinomas. Identification of new molecular markers in basal breast carcinomas 58 (IDC) infiltrative breast ductal carcinoma samples (Grade 3)

2011-10-20 | E-GEOD-29581 | biostudies-arrayexpress

Expression data of human hypopharyngeal tumor cells (FaDu)

Project description:FaDu cells were infected with lentivirus containing sh-luciferase plasmid to compared with cells infected with sh-G9a containing lentivirus. We performed microarray analysis to identify the genes possibly regulated by G9a in FaDu cells

2017-02-13 | GSE56330 | GEO

Lysyl oxidase-like 2 (LOXL2) a new regulator of cell polarity required for metastatic dissemination of basal-like breast carcinomas

2011-10-21 | GSE29581 | GEO

Regulation of downstream pathway of NSUN2 knockdown in hypopharyngeal carcinoma FaDu cell line

Project description:It has been confirmed that nsun2 promotes cell proliferation and migration in hypopharyngeal cancer cell lines, but the pathway of nsun2 in hypopharyngeal cancer cell lines is poorly understood. We constructed stable cell lines by knocking down nsun2 to find the key genes of downstream pathway, and compared them with normal FaDu cell lines.It has been confirmed that nsun2 promotes cell proliferation and migration in FaDu cell line, but the pathway of nsun2 in FaDu cell line is poorly understood. We constructed stable cell lines by knocking down nsun2 to find the key genes of downstream pathway, compared them with normal FaDu cell lines.

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Genome-wide analysis of histone modification in UPCI-SCC-090, UM-SCC-104, FaDu and NP69SV40T.

Project description:We analysed active enhancers in UPCI-SCC-090, UM-SCC-104, FaDu and NP69SV40T by performing ChIP-seq on H3K4me3, H3K4me1 and H3K27ac.

2023-01-06 | GSE211473 | GEO

Lysyl oxidase-like 2 (LOXL2)-mediated cross-linking of tropoelastin.

Project description:Lysyl oxidases (LOXs) play a central role in extracellular matrix remodeling during development and tumor growth and fibrosis through cross-linking of collagens and elastin. We have limited knowledge of the structure and substrate specificity of these secreted enzymes. LOXs share a conserved C-terminal catalytic domain but differ in their N-terminal region, which is composed of 4 repeats of scavenger receptor cysteine-rich (SRCR) domains in LOX-like (LOXL) 2. We investigated by X-ray scattering and electron microscopy the low-resolution structure of the full-length enzyme and the structure of a shorter form lacking the catalytic domain. Our data demonstrate that LOXL2 has a rod-like structure with a stalk composed of the SRCR domains and the catalytic domain at its tip. We detected direct interaction between LOXL2 and tropoelastin (TE) and also LOXL2-mediated deamination of TE. Using proteomics, we identified several allysines together with cross-linked TE peptides. The elastin-like material generated was resistant to trypsin proteolysis and displayed mechanical properties similar to mature elastin. Finally, we detected the codistribution of LOXL2 and elastin in the vascular wall. Altogether, these data suggest that LOXL2 could participate in elastogenesis in vivo and could be used as a means of cross-linking TE in vitro for biomimetic and cell-compatible tissue engineering purposes.-Schmelzer, C. E. H., Heinz, A., Troilo, H., Lockhart-Cairns, M.-P., Jowitt, T. A., Marchand, M. F., Bidault, L., Bignon, M., Hedtke, T., Barret, A., McConnell, J. C., Sherratt, M. J., Germain, S., Hulmes, D. J. S., Baldock, C., Muller, L. Lysyl oxidase-like 2 (LOXL2)-mediated cross-linking of tropoelastin.

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Lysyl Oxidase-like Protein LOXL2 Promotes Lung Metastasis of Breast Cancer.

Project description:The lysyl oxidase-like protein LOXL2 has been suggested to contribute to tumor progression and metastasis, but in vivo evidence has been lacking. Here we provide functional evidence that LOXL2 is a key driver of breast cancer metastasis in two conditional transgenic mouse models of PyMT-induced breast cancer. LOXL2 ablation in mammary tumor cells dramatically decreased lung metastasis, whereas LOXL2 overexpression promoted metastatic tumor growth. LOXL2 depletion or overexpression in tumor cells does not affect extracellular matrix stiffness or organization in primary and metastatic tumors, implying a function for LOXL2 independent of its conventional role in extracellular matrix remodeling. In support of this likelihood, cellular and molecular analyses revealed an association of LOXL2 action with elevated levels of the EMT regulatory transcription factor Snail1 and expression of several cytokines that promote premetastatic niche formation. Taken together, our findings established a pathophysiologic role and new function for LOXL2 in breast cancer metastasis. Cancer Res; 77(21); 5846-59. ©2017 AACR.

| S-EPMC5656180 | biostudies-literature

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