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LOXL1 encodes a member of the lysyl oxidase gene family. Additionally we are shipping LOXL1 Antibodies (68) and LOXL1 Kits (12) and many more products for this protein.
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To identify additional candidate functional variants, we sequenced the entire LOXL1 genomic locus ( approximately 40 kb) in 50 indigenous, black South African XFS (show FST Proteins) cases and 50 matched controls.
This is the first study associating two SNPs of LOXL1 (rs3825942 and rs2165241) and XFS (show FST Proteins)/XFG in a Spanish population, confirming findings in patients from Europe.
Aortic tissue from Marfan syndrome patients and display enhanced expression of the members of the LOX (show LOX Proteins) family, LOX (show LOX Proteins) and LOX (show LOX Proteins)-like 1.
Our meta-analysis indicates that rs1048661 had weak association with XFG/XFS (show FST Proteins); rs3825942 had strongly association with XFG/XFS (show FST Proteins); and rs2165241 had significant risk with XFG/XFS (show FST Proteins) in some ethnicity.
CTR1 (show SLC31A1 Proteins), ATP7A (show ATP7A Proteins), and lysyl oxidase (show LOX Proteins) were upregulated in the lung tissues and pulmonary arteries of mice with hypoxia-induced pulmonary hypertension and pulmonary arterial smooth muscle cells.
Different SNPs in LOXL1 affect risk of pseudoexfoliative glaucoma in different ethnic groups [meta-analysis]
When the LOXL1 variants were used as disease markers for clinically undetectable exfoliation syndrome (EX), there was no association between central retinal vein occlusion and EX.
results indicate that hypermethylation of CpG islands in the promoter region of the LOXL1 gene leads directly to downregulation of LOXL1 mRNA and protein, which functions as an essential mechanism in the pathogenesis of Pseudoexfoliation Syndrome
Data indicate that single-nucleotide polymorphisms (SNPs) distributing in not only lysyl oxidase-like 1 gene (LOXL1) but also TBC1 domain family member 21 (show TBC1D21 Proteins) protein (TBC1D21 (show TBC1D21 Proteins)) and promyelocytic leukemia protein (PML (show PML Proteins)).
Single nucleotide polymorphisms of the LOXL1 gene are associated with pseudoexfoliation glaucoma in the Spanish population.
LOXL1-/- mutant mice develop appendicular and axial skeletal phenotypes characterized by decreased bone volume fraction and compromised trabecular microstructure, predominantly in females
Elimination of LOXL1 in mice impairs the blood-aqueous humor barrier in the ocular anterior segment and causes lens abnormalities consistent with cataract formation, but does not result in deposition of macromolecular material or glaucoma.
There is a possible fundamental role of LOXL-1 in cardiac hypertrophy.
loxl appears non-allelic to rough coat in mice; heart- and skin-specific downregulation of LOXL in rough coat mice, however, may contribute to the extracellular matrix alterations and the rough coat phenotype
Data report that cells in the hippocampal granule cell layer of LOXL -/- mice have significantly smaller somas and muted (show MUTED Proteins) long-term potentiation compared to LOXL +/+ mice.
pro-regions of lysyl oxidase (show LOX Proteins) and lysyl oxidase-like 1 are required for deposition onto elastic fibers
LOXL1 deficiency caused failure of elastic fiber homeostasis leading to pelvic floor disorders
LOXL1 (lysyl oxidase-like 1) mutation results in a global defect in connective tissues and correlates with altered biomechanical behavior of the vagina and supportive tissues
LOXL1-KO lower urogenital tract anatomical and functional phenotype resembles female pelvic floor dysfunction in humans. Elastin (show ELN Proteins) disorganization may lead to such functional abnormalities.
Loxl1(-/-) males bred with control females demonstrated relative fecundity values intermediate between Loxl1(-/-) pairs (lowest fecundity) and control pairs (highest fecundity), suggesting a component of male-factor infertility.
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 1
, lysyl oxidase homolog 1-like
, lysyl oxidase homolog 1
, lysyl oxidase-like protein 1
, lysyl oxidase 2