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Dmloxl-1 and Dmloxl-2 are differentially expressed; active DmLOXL-1 influences gene expression and development
expression of LOXL2 endowed dormant tumor cells with cancer stem cell-like phenotype driving their transition to metastatic outgrowth and this stem-like phenotype is dependent on epithelial to mesenchymal transition (EMT (show ITK Proteins)) that can be driven by the tumor microenvironment.
Simtuzumab is a humanized IgG4 monoclonal antibody that inhibits enzymatic activity of LOXL2... inhibition of LOXL2 expression reduced numbers of activated fibroblasts, decreased ECM (show MMRN1 Proteins) deposition, inhibited angiogenesis, and prevented tumor cell invasion and metastases
higher LOXL2 expression is associated with the invasiveness of pancreatic cancer cells and the low survival rate of pancreatic cancer patients
LOXL2 c.C133T is a pathogenic mutation that is responsible for a fraction of familial intracranial aneurysms.
data demonstrate that proteolytic processing is an important event that allows LOXL2-mediated crosslinking of basement membrane collagen IV (show COL4 Proteins).
new LOXL2 splice variant contributes to tumor progression by novel molecular mechanisms different from LOXL2WT
LOXL2 is a potential therapeutic target against tumor progression.
Insulin (show INS Proteins) resistance promotes lysyl oxidase like 2 induction and fibrosis accumulation in non-alcoholic fatty liver disease.
SMYD3 (show SMYD3 Proteins) enhances tumorigenicity in esophageal squamous cell carcinoma by enhancing transcription of ezrin (show EZR Proteins) and LOXL2, which are involved in proliferation, migration, and invasion.
Data show that lysyl oxidase-like 2 (LOXL2) is a histone modifier enzyme that removes trimethylated lysine 4 (K4) in histone H3 (show HIST3H3 Proteins) (H3K4me3) through an amino-oxidase reaction.
Findings indicate a pathophysiologic role and function for lysyl oxidase (show LOX Proteins)-like protein LOXL2 (show LOXL3 Proteins) in breast cancer metastasis.
Insulin (show INS Proteins) resistance promotes lysyl oxidase like 2 (show LOXL3 Proteins) induction and fibrosis accumulation in non-alcoholic fatty liver disease.
glomerular extracellular matrix. Altogether, we demonstrate that LOXL2 (show LOXL3 Proteins) is a novel component of the molecular machinery that forms cross-linked collagen IV (show COL4 Proteins) networks, which are essential for glomerular basement membrane stability and molecular ultrafiltration function.
LOX (show LOX Proteins) and LOXL2 (show LOXL3 Proteins) may play an important role in the pathogenesis of AMD (show AMD1 Proteins). Targeting LOXL2 (show LOXL3 Proteins) could have a broader efficacy than targeting LOX (show LOX Proteins), by reducing angiogenesis and inflammation, as well as fibrosis.
Loss and gain of function analyses combined with in vivo studies in syngeneic breast cancer models demonstrate the participation of LOXL2 (show LOXL3 Proteins) and E47 (show TCF3 Proteins) in tumor growth and their requirement for lung metastasis.
Findings reveal new insight into the mechanisms of fibroblast activation, a novel function of LOXL2 (show LOXL3 Proteins), and further highlight the importance of generating LOXL2 (show LOXL3 Proteins)-targeted therapies for the prevention of tumor progression and metastasis.
The Snail1 (show SNAI1 Proteins) transcription factor represses mouse pericentromeric transcription, acting through the H3K4 deaminase LOXL2 (show LOXL3 Proteins).
The enzymatic activity of lysyl oxidas-like-2 (LOXL2 (show LOXL3 Proteins)) is not required for LOXL2 (show LOXL3 Proteins)-induced inhibition of keratinocyte differentiation.
This study provides the first evidence for the role of LOXL2 (show LOXL3 Proteins) in regulating angiogenesis through collagen IV (show COL4 Proteins) scaffolding.
LOXL2 (show LOXL3 Proteins) promotes chondrocyte differentiation by mechanisms that are likely to include roles as both a regulator and an effector of chondrocyte differentiation
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.
, lysyl oxidase-like 2
, Lysyl oxidase-like protein 2
, lysyl oxidase homolog 2
, lysyl oxidase homolog 2-like
, lysyl oxidase related 2
, lysyl oxidase-like protein 2
, lysyl oxidase-related protein 2
, lysyl oxidase-related protein WS9-14
, Lysyl oxidase homolog 2