Biomaterial Database

Synergism of phosphorylation of 46K protein(s) and arachidonate release in the induction of superoxide anion production in guinea pig polymorphonuclear leukocytes. 1988

T Ohtsuka, and M Ozawa, and T Katayama, and S Ishibashi

Department of Physiological Chemistry, Hiroshima University School of Medicine, Japan.

The phosphorylation of 46K protein(s), which was generally observed in parallel with an activation of NADPH oxidase of guinea pig polymorphonuclear leukocytes (PMNL) in our previous studies (N. Okamura et al. (1984) Arch. Biochem. Biophys. 228, 270-277; T. Ohtsuka et al. (1987) J. Biochem. 101, 897-903), was increased by treatment with 1-oleoyl-2-acetylglycerol (OAG), even at low concentrations at which both superoxide anion (O2-) production and arachidonate release were little induced. On the other hand, exposure of PMNL to low concentrations of a calcium ionophore, A23187, stimulated arachidonate release without causing substantial O2- production and increase in phosphorylation of 46K protein(s). Simultaneous addition of the above-mentioned suboptimal concentrations of both OAG and A23187 markedly enhanced O2- production in PMNL. This enhancing effect may be ascribable to the increase in the phosphorylation of 46K protein(s) and arachidonate release, which are induced by the addition of OAG and A23187, respectively. Another arachidonate-releasing agent, N-formyl-methionylleucyl-phenylalanine (FMLP), also stimulated O2- production in accordance with an increase in the arachidonate release and protein phosphorylation. Simultaneous addition of OAG significantly enhanced the FMLP-induced O2- production, presumably by maintaining the 46K protein phosphorylation which would facilitate the effect of arachidonate released by FMLP. Thus, the present results suggest that phosphorylation of 46K protein(s) and arachidonate release synergistically induce O2- production in PMNL, although either of them alone hardly induces the production.

UI	MeSH Term	Description	Entries
D009240	N-Formylmethionine Leucyl-Phenylalanine	A formylated tripeptide originally isolated from bacterial filtrates that is positively chemotactic to polymorphonuclear leucocytes, and causes them to release lysosomal enzymes and become metabolically activated.	F-Met-Leu-Phe,N-Formyl-Methionyl-Leucyl-Phenylalanine,Formylmet-Leu-Phe,Formylmethionyl Peptide,Formylmethionyl-Leucyl-Phenylalanine,Formylmethionylleucylphenylalanine,N-Formylated Peptide,N-formylmethionyl-leucyl-phenylalanine,fMet-Leu-Phe,F Met Leu Phe,Formylmet Leu Phe,Formylmethionyl Leucyl Phenylalanine,Leucyl-Phenylalanine, N-Formylmethionine,N Formyl Methionyl Leucyl Phenylalanine,N Formylated Peptide,N Formylmethionine Leucyl Phenylalanine,N formylmethionyl leucyl phenylalanine,Peptide, Formylmethionyl,Peptide, N-Formylated,fMet Leu Phe
D009247	NADH, NADPH Oxidoreductases	A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.	Oxidoreductases, NADH, NADPH,NADPH Oxidoreductases NADH,Oxidoreductases NADH, NADPH
D009504	Neutrophils	Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.	LE Cells,Leukocytes, Polymorphonuclear,Polymorphonuclear Leukocytes,Polymorphonuclear Neutrophils,Neutrophil Band Cells,Band Cell, Neutrophil,Cell, LE,LE Cell,Leukocyte, Polymorphonuclear,Neutrophil,Neutrophil Band Cell,Neutrophil, Polymorphonuclear,Polymorphonuclear Leukocyte,Polymorphonuclear Neutrophil
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D011506	Proteins	Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.	Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D004075	Diglycerides	Glycerides composed of two fatty acids esterified to the trihydric alcohol GLYCEROL. There are two possible forms that exist: 1,2-diacylglycerols and 1,3-diacylglycerols.	Diacylglycerol,Diacylglycerols
D005260	Female		Females
D006168	Guinea Pigs	A common name used for the genus Cavia. The most common species is Cavia porcellus which is the domesticated guinea pig used for pets and biomedical research.	Cavia,Cavia porcellus,Guinea Pig,Pig, Guinea,Pigs, Guinea
D000001	Calcimycin	An ionophorous, polyether antibiotic from Streptomyces chartreusensis. It binds and transports CALCIUM and other divalent cations across membranes and uncouples oxidative phosphorylation while inhibiting ATPase of rat liver mitochondria. The substance is used mostly as a biochemical tool to study the role of divalent cations in various biological systems.	4-Benzoxazolecarboxylic acid, 5-(methylamino)-2-((3,9,11-trimethyl-8-(1-methyl-2-oxo-2-(1H-pyrrol-2-yl)ethyl)-1,7-dioxaspiro(5.5)undec-2-yl)methyl)-, (6S-(6alpha(2S,3S),8beta(R*),9beta,11alpha))-,A-23187,A23187,Antibiotic A23187,A 23187,A23187, Antibiotic
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