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Dmloxl-1 and Dmloxl-2 are differentially expressed; active DmLOXL-1 influences gene expression and development
The expression levels of lysyl oxidase-like 2 (LOXL2) mRNA and protein were markedly suppressed in transfected prostate cancer cells with microRNAs miR (show MLXIP Proteins)-26a, miR (show MLXIP Proteins)-26b, miR (show MLXIP Proteins)-29a, miR (show MLXIP Proteins)-29b, miR (show MLXIP Proteins)-29c and miR (show MLXIP Proteins)-218.
Overexpression of LOXL2 and SERPINH1 (show SERPINH1 Proteins) was observed in clinical specimens of lung cancer and fibrotic lesions. Downregulation of miR (show MLXIP Proteins)-29a caused overexpression of LOXL2 and SERPINH1 (show SERPINH1 Proteins) in lung cancer and IPF, suggesting that these genes are involved in the pathogenesis of these two diseases.
LOXL2 expression is significantly upregulated in human masticatory mucosa during wound healing
BMP2 (show BMP2 Proteins) and RUNX2 (show RUNX2 Proteins) are expressed exclusively by osteoblasts whereas DSPP (show DSPP Proteins) and LOXL2 are expressed exclusively by odontoblasts. (Review)
Results showed that LOXL2 was overexpressed in head and neck squamous cell carcinoma clinical specimens and that silencing of the LOXL2 gene significantly inhibited the migration and invasion of cancer cells.
ECM (show MMRN1 Proteins) crosslinking by EC-derived exosomes is mediated by LOXL2.
Results show that miR (show MLXIP Proteins)-26a and miR (show MLXIP Proteins)-26b were significantly downregulated in renal cell carcinoma (show MOK Proteins) clinical specimens and appeared to function as tumor suppressors through regulation of collagen cross-linking enzymes, LOXL2 and PLOD2 (show PLOD2 Proteins), both of which function as oncogenes in this disease.
Loss of tumor-suppressive miR29s enhanced cancer cell invasion in lung SCC (show CYP11A1 Proteins) through direct regulation of oncogenic LOXL2.
LOXL2 promotes tumor progression.
We identified LOXL2 to be associated with the outcome of colon cancer patients. Furthermore, it can be used to stratify patients at stages II and III for further therapeutic decisions.
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
The efficacy and safety of LOXL2 (show LOXL3 Proteins)-specific monoclonal antibody represents a new therapeutic approach with broad applicability in oncologic and fibrotic diseases.
LoxL2 (show LOXL3 Proteins) is not expressed in MC3T3-E1 cells.
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