Respiration and glucose oxidation in human and guinea pig leukocytes: comparative studies

Robert L. Baehner; Neal Gilman; Manfred L. Karnovsky

doi:10.1172/JCI106281

^{Department of Pediatrics, Harvard Medical School, and the Division of Research Hematology, Children's Hospital Medical Center, Boston, Massachusetts 02115}

^{Department of Biological Chemistry, Harvard Medical School, and the Division of Research Hematology, Children's Hospital Medical Center, Boston, Massachusetts 02115}

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^{Department of Pediatrics, Harvard Medical School, and the Division of Research Hematology, Children's Hospital Medical Center, Boston, Massachusetts 02115}

^{Department of Biological Chemistry, Harvard Medical School, and the Division of Research Hematology, Children's Hospital Medical Center, Boston, Massachusetts 02115}

Find articles by Gilman, N. in: JCI | PubMed | Google Scholar

^{Department of Pediatrics, Harvard Medical School, and the Division of Research Hematology, Children's Hospital Medical Center, Boston, Massachusetts 02115}

^{Department of Biological Chemistry, Harvard Medical School, and the Division of Research Hematology, Children's Hospital Medical Center, Boston, Massachusetts 02115}

Find articles by Karnovsky, M. in: JCI | PubMed | Google Scholar

Published in Volume 49, Issue 4 on April 1, 1970
J Clin Invest. 1970;49(4):692–700. https://doi.org/10.1172/JCI106281.
© 1970 The American Society for Clinical Investigation

Published April 1, 1970 - Version history

A comparison has been made of the metabolic shifts in human and guinea pig leukocytes when they phagocytize. Respiration of guinea pig polymorphonuclear leukocytes (PMN) and the increment during phagocytosis were each about 2½-fold that of human PMN. This was also true of the direct oxidation of glucose-6-P (hexose monophosphate shunt). Enzymes potentially responsible for these phenomena have been compared in each species. Cyanide-insensitive NADH oxidase and NADPH oxidase were measured and only the formed exhibited adequate activity to account for the respiratory stimulus durintg phagocytosis. The hydrogen peroxide formed by this enzyme stimulates the hexose monophosphate shunt by oxidizing glutathione which upon reduction by an NADPH-linked glutathione reductase provides NADP to drive the hexose monophosphate shunt. Other linkages between respiratory stimulation and that of the hexose monophosphate shunt also pertain in the guinea pig.