What does lysyl oxidase do?
Lysyl oxidase (LO) is a copper-dependent amine oxidase that plays a critical role in the biogenesis of connective tissue matrices by crosslinking the extracellular matrix proteins, collagen and elastin.
What is anti lysyl oxidase?
Abstract. Lysyl oxidase (LOX) is a secreted copper-dependent amine oxidase that cross-links collagens and elastin in the extracellular matrix and is a critical mediator of tumor growth and metastatic spread.
What is the single most important action which lysyl oxidase contributes for collagen maturation?
The lysyl oxidase family of enzymes is classically known as being required for connective tissue maturation by oxidizing lysine residues in elastin and lysine and hydroxylysine residues in collagen precursors.
What is lox cell?
LOX-IMVI cells are genetically characterized by lack of the Y chromosome and trisomy 7 (2), and are heterozygous for the BRAF V600E melanoma driver mutation (4). LOX-IMVI cells are amelanotic and express the human melanoma marker GD3 ganglioside, a factor in metastatic potential of malignant melanoma (5).
Does lysyl hydroxylase need vitamin C?
Vitamin C. Vitamin C, oxygen, ketoglutarate, and iron are essential cofactors for the enzymes prolyl hydroxylase and lysyl hydroxylase, both of which are required for normal collagen metabolism. Vitamin C is important in aerobic metabolism.
Does lysyl oxidase require vitamin C?
Vitamin C. Vitamin C, oxygen, ketoglutarate, and iron are essential cofactors for the enzymes prolyl hydroxylase and lysyl hydroxylase, both of which are required for normal collagen metabolism. Vitamin C is important in aerobic metabolism. Fibroplasia is especially sensitive to vitamin C deficiency.
What are lox sites?
LoxP sites are directional 34 bp sequences made up of two 13 bp recognition sites separated by an 8 bp spacer region. The sequences don’t occur naturally in any known genomes other than the P1 bacteriophage, and are long enough that they are unlikely to occur by chance.
How does a Cre lox system work?
Cre recombinase proteins bind to the first and last 13 bp regions of a lox site forming a dimer. This dimer then binds to a dimer on another lox site to form a tetramer. The double stranded DNA is cut at both loxP sites by the Cre protein. The strands are then rejoined with DNA ligase in a quick and efficient process.
How does vitamin C help collagen synthesis?
Vitamin C (VitC) plays a critical role in the maintenance of a normal mature collagen network in humans (anti-scurvy properties) by preventing the auto-inactivation of lysyl and prolyl hyroxylase, two key enzymes in collagen biosynthesis.
Does vitamin C protect against damage from free radicals?
As a water soluble molecule, vitamin C can work both inside and outside the cells, and can neutralize free radicals and prevent free radical damage. Vitamin C is an excellent source of electrons for free radicals that are seeking out an electron to regain their stability.
How does Cre loxP system work?
How does it work? As alluded to above, the Cre recombinase catalyzes the site specific recombination event between two loxP sites, which can be located either on the same or on separate pieces of DNA. Both 13bp repeat sequences on a single loxP site are recognized and bound by a Cre protein, forming a dimer.
Who invented Cre-lox?
Nat L. Sternberg
The origins of this tool date to more than 30 years ago when Nat L. Sternberg discovered the recombinase, Cre, and its specific locus of crossover, lox, while studying the maintenance of bacteriophage P1 as a stable plasmid.
