Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes.

Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes. Abstract Text:

H Tsuda,K Takeshige,Y Shibata,S Minakami,

Human colostral macrophages stimulated by opsonized zymosan or phorbol myristate acetate (PMA) released superoxide anions (O2-) and hydrogen peroxide (H2O2) with activities comparable to those of monocytes and about one-fourth of those of polymorphonuclear leukocytes (PMNL) of blood. The O2- -forming oxidase in the macrophages stimulated by PMA was dependent on NADPH as an electron donor with an apparent Km value for NADPH of 27.6 +/- 4.0 microM, which is comparable to those obtained for the stimulated monocytes and PMNL of blood. The Vmax was 1.86 +/- 0.33 nmol O2/min/10(6) cells, which is essentially the same as that of monocytes and about half of that of PMNL. p-Chloromercuribenzoate or cetyltrimethylammonium bromide completely inhibited oxidases of all three types of phagocytes. A b-type cytochrome was identified in the macrophages but the concentrations in the macrophages and monocytes were less than half of that in PMNL. These results suggest that the differences in the O2- -forming activities of the three types of phagocytes are quantitative rather than qualitative. The macrophages and monocytes showed very low activities of myeloperoxidase [EC 1.11.1.7] in contrast to PMNL. The activity of beta-glucuronidase [EC 3.2.1.31] in the macrophages was much higher than those of the monocytes and PMNL, but little difference was observed in the activities of lysozyme [EC 3.2.1.17], catalase [EC 1.11.1.6] and superoxide dismutase [EC 1.15.1.1] among the three types of phagocytes examined. Electron micrographs of the macrophages showed little increase of vacuoles upon exposure to PMA, in contrast to the cases of monocytes and PMNL.

Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes. Publishing Authors By Initials

H Tsuda,K Takeshige,Y Shibata,S Minakami,

For similar beta-glucans: zymosan research abstracts see: beta-glucans: zymosan research

PUBMED ID PMID:

MEDLINE DATE:

Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 95

Page Numbers: 1237-45

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: May

YEAR: 1984

Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes. Keywords Mesh Terms:

KEYWORDS: Zymosan

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes. Information

Substance Name: Glucuronidase

Registry Number: EC 3.2.1.31

Grant and Affiliation Information for Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes Related Publications

• A polymorphism in the CYP17 gene and intrauterine fetal growth restriction.
• Accumulation of phosphoenolpyruvate in red cells incubated with the phosphate ester in an acidified isotonic sucrose medium.
• Effect of cobalt on heme biosynthesis in rat liver and spleen.
• Effect of cobalt on the synthesis of liver microsomal cytochromes.
• Effect of cyclic nucleotides on the cyanide-insensitive respiration of polymorphonuclear leucocytes.
• Effect of ionic sites of surfactants on leukocyte metabolism.
• Effect of oxygen tension on glycolysis in human erythrocytes.
• Effects of Triton X-100 on drug hydroxylation system of rat liver microsomes induced by phenobarbital or 3-methylcholanthrene.
• Glycolysis of red cells suspended in solutions of impermeable solutes. Intracellular pH and glycolysis.
• Hexose-6-phosphate and 6-phosphogluconate dehydrogenases of rat liver microsomes. Involvement in NADPH and carbon dioxide generation in the luminal space of microsomal vesicles.
• Human NADH-cytochrome b5 reductases: comparison among those of erythrocyte membrane, erythrocyte cytosol, and liver microsomes.
• Incorporation of radioactive iron into cytochrome b5 and cytochrome P-450 of liver microsomes.
• Intracellular distribution of hepatic catalase activity in rats treated with aminotriazole and allylisopropylacetamide.
• Intracellular pH (pHi) of red cells stored in acid citrate dextrose medium. Effects of temperature and citrate anions.
• Metabolic pattern of polymorphonuclear leucocytes induced by trypsin-digested microsomes.
• Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes.
• NADPH-dependent superoxide-forming oxidase in phagocytic vesicles of human monocytes.
• On functional role of cytochrome b5. I. NADH-linked cytochrome c reductase in microsomes.
• On functional role of cytochrome b5. II. NADH-linked ascorbate radical reductase activity in microsomes.
• Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes.
• Presence of apo-cytochrome beta 5 in microsomes. Incorporation of radioactive heme to the cytochrome in vitro.
• Quantitative separation of triphosphothiamine in biological materials and its formation from S35-thiamine in rat liver.
• Spontaneous induction of superoxide release and degranulation of neutrophils in isotonic potassium medium: the role of intracellular calcium.
• Studies on erythrocyte glycolysis. 8. Kinetics of 2,3-diphosphoglycerate changes.
• Studies on erythrocyte glycolysis. V. Change of the glycolytic intermediate pattern of reticulocytes during maturation.
• Studies on erythrocyte glycolysis. VI. Control of glycolysis by ATP level in human erythrocytes.
• Studies on leukocyte metabolism. I.
• Synthesis of catalase in liver slices from aminotriazole-pretreated rats.
• The role of Ca2+ and Ca2+-activated phospholipid-dependent protein kinase in degranulation of human neutrophils.
• Turnover of hepatic catalase modified by aminotriazole.