Disease relevance of Lao1

• L-amino acid oxidase (LOX) modulation of melphalan activity against intracranial glioma [1].

High impact information on Lao1

• IL-4-induced gene-1 is a leukocyte L-amino acid oxidase with an unusual acidic pH preference and lysosomal localization [2].
• LAO mRNA increased 1 day before parturition, peaked during early to mid-lactation, and decreased at the end of lactation [3].
• As mouse milk produced H(2)O(2) using endogenous free amino acids, we suggest that LAO, together with free amino acids, is responsible for killing bacteria in the mammary gland [3].
• LAO reacted with l-amino acids in an apparent order of Phe > Met, Tyr > Cys, Leu > His other 11 amino acids tested and produced H(2)O(2) in a dose- and time-dependent manner [3].
• LAO mRNA spanned about 2.0 kb, and its expression was found only in the mammary epithelial cells [3].

Biological context of Lao1

• Glucocorticoid was essential for LAO gene expression [3].
• Amino acid sequence analysis of the apoxin I showed close similarity to L-amino acid oxidase from the Malayan pit viper (Calloselasma rhodostoma) [4].
• After 18 h treatment with 25-100 microg/ml of LAO, the typical DNA fragmentation pattern of apoptotic cells was observed by means of fluorescent microscopy and agarose gel electrophoresis [5].
• We have identified that a cytotoxic substance of Korean snake venom which is responsible for the apoptosis is L-amino acid oxidase (LAO) [6].
• Platelet aggregation and antibacterial effects of an l-amino acid oxidase purified from Bothrops alternatus snake venom [7].

Anatomical context of Lao1

• Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein [8].

Associations of Lao1 with chemical compounds

• Treating the transfected cells with tunicamycin inhibited the secretion and LAO activity of the recombinant apoxin I [9].
• In addition, deleting the amino-terminal region flanking the signal sequence, the FAD-binding domain and the carboxy-terminal region abolished the secretion and LAO activity of the recombinant proteins [9].
• The effect of L-amino acid oxidase on activity of melphalan against an intracranial xenograft [10].
• The purified LNV-LAO not only retained its specific enzymatic activity (73.46 U/mg), determined against L-leucine as a substrate, but also exhibited potent haemolytic (1-10 microg/ml), edema- (MED 4.8 microg/ml) and human platelet aggregation-inducing (ED50 33 microg/ml) properties [5].
• Treatment with L-amino acid oxidase (LOX) significantly depleted murine plasma LNAAs: phenylalanine, leucine, and tyrosine (> 95%); methionine (83%); isoleucine (70%); and valine (46%) [10].

Other interactions of Lao1

• Bungarus candidus venom exhibited high hyaluronidase, acetylcholinesterase and phospholipase A activities; low proteinase, 5'-nucleotidase, alkaline phosphomonoesterase and phosphodiesterase activities and moderately high L-amino acid oxidase activity [11].

Analytical, diagnostic and therapeutic context of Lao1

• LAO in milk had a molecular mass of about 113 kDa and was converted to a 60-kDa protein by SDS-PAGE [3].
• The secondary structural contents analysis of LAO, established by means of circular dichroism, revealed ca. 49% alpha-helix, 19% beta-sheet, 10% beta-turn, and 22% random coil structure [5].
• In addition to these local effects, the purified LNV-LAO showed apoptosis-inducing activity in the MM6 cell culture assay [5].
• The enzyme L-amino acid oxidase (LAO) from the leaf-nosed viper (Eristocophis macmahoni) snake venom was purified to homogeneity in a single step using high performance liquid chromatography on a Nucleosil 7C18 reverse phase column [5].
• Molecular sieve chromatography of P. p. persicus venom shows a typical elution profile of a viperid snake, with hemorrhagic activity and L-amino acid oxidase activity confined to the high molecular weight peak of proteins [12].

References