Biomaterial Database

Specific induction of pulmonary indoleamine 2,3-dioxygenase by bacterial lipopolysaccharide. 1978

O Hayaishi, and R Yoshida

Indoleamine 2,3-dioxygenase (molecular weight about 42,000) has been purified from rabbit intestines and contains one mole of protohaem IX as the sole prosthetic group. It catalyses the oxidative cleavage of the pyrrole ring of various indoleamines with a much broader specificity of substrate than tryptophan 2,3-dioxygenase. The enzyme has an absolute requirement for superoxide anion for catalytic activity. The enzyme was induced specifically in the lungs of mice for 24 h after administration of the lipopolysaccharide fraction of E. coli. This increase is due to synthesis of enzyme protein and is specific for the lipopolysaccharide fraction. These results are interpreted to mean that indoleamine dioxygenase is induced in pulmonary inflammatory processes in response to an increase in production of superoxide anion, 5-hydroxytryptamine or other indoleamines in the lung as a consequence of inflammation. The dioxygenase reaction is a more innocuous way of disposing of superoxide than dismutation.

UI	MeSH Term	Description	Entries
D007211	Indoles	Benzopyrroles with the nitrogen at the number one carbon adjacent to the benzyl portion, in contrast to ISOINDOLES which have the nitrogen away from the six-membered ring.
D007249	Inflammation	A pathological process characterized by injury or destruction of tissues caused by a variety of cytologic and chemical reactions. It is usually manifested by typical signs of pain, heat, redness, swelling, and loss of function.	Innate Inflammatory Response,Inflammations,Inflammatory Response, Innate,Innate Inflammatory Responses
D008070	Lipopolysaccharides	Lipid-containing polysaccharides which are endotoxins and important group-specific antigens. They are often derived from the cell wall of gram-negative bacteria and induce immunoglobulin secretion. The lipopolysaccharide molecule consists of three parts: LIPID A, core polysaccharide, and O-specific chains (O ANTIGENS). When derived from Escherichia coli, lipopolysaccharides serve as polyclonal B-cell mitogens commonly used in laboratory immunology. (From Dorland, 28th ed)	Lipopolysaccharide,Lipoglycans
D008168	Lung	Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood.	Lungs
D008247	Lysosomes	A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured or undergoes MEMBRANE FUSION. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed).	Autolysosome,Autolysosomes,Lysosome
D010105	Oxygenases	Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules.	Oxygenase
D004790	Enzyme Induction	An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.	Induction, Enzyme
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001427	Bacterial Toxins	Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases.	Bacterial Toxin,Toxins, Bacterial,Toxin, Bacterial
D014366	Tryptophan Oxygenase	A dioxygenase with specificity for the oxidation of the indoleamine ring of TRYPTOPHAN. It is a LIVER-specific enzyme that is the first and rate limiting enzyme in the kynurenine pathway of TRYPTOPHAN catabolism.	Tryptophan Pyrrolase,TDO Dioxygenase,Tryptophan 2,3-Dioxygenase,2,3-Dioxygenase, Tryptophan,Dioxygenase, TDO,Oxygenase, Tryptophan,Pyrrolase, Tryptophan,Tryptophan 2,3 Dioxygenase