Disease relevance of LEUCINOSTATIN

• Glucosylation of the peptide leucinostatin A, produced by an endophytic fungus of European yew, may protect the host from leucinostatin toxicity [1].
• This glucoside, also made by the fungus, has a lower bioactivity against plants, fungi and a breast cancer cell line, BT-20, than leucinostatin A [1].

High impact information on LEUCINOSTATIN

• Cross-resistance to ossamycin, peliomycin, chloramphenicol, antimycin, venturicidin, leucinostatin, and efrapeptin was also expressed codominantly in hybrids [2].
• Inhibition of spinach chloroplasts photophosphorylation by the antibiotics leucinostatin and efrapeptin [3].
• The membrane-bound, but not the soluble (F1) ATPase was inhibited by oligomycin and leucinostatin [4].
• The crystal and molecular structure of the nonapeptide antibiotic leucinostatin A, containing some uncommon amino acids and three Aib residues, has been determined by x-ray diffraction analysis [5].
• Structure of leucinostatin B, an uncoupler on mitochondria [6].

Biological context of LEUCINOSTATIN

• The crystal and molecular structure of the alpha-helical nonapeptide antibiotic leucinostatin A [5].
• This was further confirmed from the evidence that methylation with methyl iodide led each antibiotic to the identical compound which was named leucinostatin A-M (III) [7].

Anatomical context of LEUCINOSTATIN

• The nonapeptide leucinostatin A acts as a weak ionophore and as an immunosuppressant on T lymphocytes [8].
• In plating-efficiency experiments, Chinese hamster lung V79 and bone marrow M3-1 cells were approximately 10,000-fold more resistant to oligomycin, 100-fold more resistant to efrapeptin, and 10-fold more resistant to ossamycin and leucinostatin than were ovary CHO or peritoneal B14 cells [9].
• The most specific inhibitors proved to be vanadate and diethylstilbestrol for the plasma membrane ATPase and azide, oligomycin, venturicidin, and leucinostatin for mitochondrial ATPase [10].

Associations of LEUCINOSTATIN with other chemical compounds

• 3. The solubilized enzyme was insensitive to oligomycin and leucinostatin, which inhibited the membrane-bound ATPase, though inhibited by efrapeptin and quercetin [11].

Analytical, diagnostic and therapeutic context of LEUCINOSTATIN

• In the present paper, the use of microbiological and densitometric methods for quantitative analysis of Leucinostatin A (Leu-A) are described and the results compared with those from HPLC analyses [12].
• High-performance liquid chromatography analysis was carried out to compare the chromatograms of P. lilacinus strain 251 with the chromatogram of known paecilotoxin [13].

References