Brief Report: Ultrastructural Localization of Myeloperoxidase in Human Neutrophil and Rabbit Heterophil and Eosinophil Leukocytes

Dunn, Warwick B.; Hardin, J. H.; Spicer, Samuel S.

doi:10.1182/blood.v32.6.935.935

Cited by 84 publications

(27 citation statements)

References 6 publications

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“…In polymorphonuclear leukocytes the first step in cyanide formation is oxidative chlorination of glycine or other amino acids by the enzyme myeloperoxidase. This enzyme is contained in azurophil granules in the cytoplasm of resting leukocytes (Dunn et al, 1968;Bainton and Farquhar, 1968) but is released into the phagocytic vacuole during phagocytosis (Klebanoff, 1970). Based on results in rat brain fractions, neural tissue may similarly have a cyanide-generating system contained mainly in a subcellular particle that sediments with mitochondria.…”

Section: Discussionmentioning

confidence: 99%

Endogenous generation of cyanide in neuronal tissue: Involvement of a peroxidase system

et al. 2000

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In a study of the mechanism by which cyanide is produced in neural tissue, it was hypothesized that nerve cells generate cyanide in a manner similar to that in leukocytes. As in white blood cells, glycine addition enhanced cyanide production in rat pheochromocytoma cells. Because myeloperoxidase catalyses cyanide production in leukocytes, a selective myeloperoxidase inhibitor (aminobenzoic acid hydrazide) was tested and found to inhibit opiate agonist‐induced cyanide production in pheochromocytoma cells and also in rat brain. In addition, hydrogen peroxide enhanced cyanide release in pheochromocytoma cells, further suggesting that the process is oxidative in nature. Sonicated rat pheochromocytoma cells did not generate cyanide in response to an agonist acting on surface receptors even though disrupted cells responded to glycine. The mitochondrial fraction from rat brain produced more cyanide in response to glycine than any other fraction. Thus glycine seems to act at an intracellular site to enhance cyanide production and the process seems to involve a peroxidase mechanism similar to that reported for white blood cells. J. Neurosci. Res. 61:570–575, 2000. © 2000 Wiley‐Liss, Inc.

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Section: Discussionmentioning

confidence: 99%

Endogenous generation of cyanide in neuronal tissue: Involvement of a peroxidase system

et al. 2000

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“…Ultrastructurally, these granules contain a central crystalloid (Breton-Gorius, 1966;Hudson, 1966a;Wetzel et al, 1967a;Scott and Horn, 1970), which consists of a highly basic protein that is helminthotoxic and responsible for the eosinophilia of the granules (Horn and Spicer, 1964;Dunn and Spicer, 1969;Olsson et al, 1977;Lewis et al, 1978;Gleich et al, 1980). The granule matrix surrounding the crystalloid contains peroxidase, acid phosphatase, and other hydrolytic enzymes (Wetzel et al, 196713;Dunn et al, 1968;Miller and Herzog, 1969;Bainton and Farquhar, 1970;Bass et al, 1981) and demonstrates cytochemical affinity for uranyl acetate (Hudson, 1967) and phos-photungstic acid (Hudson, 1966b). Early eosinophils (promyelocyte-myelocyte) in marrow specimens contain several basophilic granules (Dunn and Spicer, 1969).…”

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confidence: 99%

“…Early eosinophils (promyelocyte-myelocyte) in marrow specimens contain several basophilic granules (Dunn and Spicer, 1969). Ultrastructurally these latter granules lack crystalloids but contain lysosomal enzymes similar to those seen in eosinophil crystalloid granules (Wetzel et al, 1967b;Fedorko, 1968;Dunn et al, 1968;Bainton and Farquhar, 1970). The presence of transition forms from granules lacking crystalloids to those containing crystalloids (Hudson, 1966a;Wetzel et al, 1967a) has indicated that the crystalloid-free basophilic granules represent an immature form of crystalloid granules.…”

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confidence: 99%

Ultrastructural visualization of complex carbohydrates in eosinophilic leukocytes

et al. 1982

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Complex carbohydrates in eosinophils from human, rabbit, and rat marrow were identified and localized by cytochemical and radioautographic methods. The high iron diamine-thiocarbohydrazide-silver proteinate (HID-TCH-SP), low iron diamine (LID)-TCH-SP, and periodate (PA)-TCH-SP methods were used for the localization of sulfate, sulfate and carboxyl, and vicinal glycol- containing complex carbohydrates, respectively. Golgi vesicles and small precursor granules (0.2-0.4 micrometer in diameter) demonstrated strong HID-TCH-SP staining and labeled intensely after a 10-minute pulse with 35SO4(2). Crystalloid-free or immature specific granules (0.5-0.9 micrometers in diameter) labeled heavily after a 60-minute incubation and 60-minute chase with 35SO4(2). Immature granules were graded according to their HID-TCH-SP staining. Type I granules demonstrated strong rim staining and similar or somewhat less central staining, whereas type 2 granules only demonstrated rim staining, and type 3 granules lacked staining. Fully mature crystalloid-containing granules lacked staining. LID-TCH-SP similarly stained the HID-positive sulfated material in cytoplasmic granules. PA-TCH-SP stained some Golgi vesicles and diffusely stained all precursor granules and type 1 granules. Weaker staining was observed in type 2 granules and staining was very weak or absent in type 3 and crystalloid-containing granules. In early eosinophils, tubulovesicular structures (TVS) were observed rosetting and contacting precursor and type 1 granules. These TVS contained material with strong PA-TCH-SP staining but lacked HID-TCH-SP or LID-TCH-SP-reactive acidic glycoconjugates. Flattened Golgi saccules or early eosinophils stained weakly or not at all with the PA-TCH-SP method. Small granules and TVS in late (bilobed) eosinophils displayed PA-TCH-SP reactivity and lacked HID-TCH-SP staining but differed from TVS in early eosinophils in that they were not associated as rosettes with specific granules. These results indicate that sulfated and vicinal glycol-containing complex carbohydrates are differently disturbed in immature specific granules of eosinophils and presumably become masked to staining as the granule matures.

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“…In contrast, when the buffy coat was treated by method I , all blasts were unreactive (Fig 5 ) . Rare neutrophil promyelocytes showed a positive reaction in the perinuclear space, ER, Golgi zone and azurophil granules as in normal marrow promyelocytes synthesizing myeloperoxidase (Ackerman & Clark, 1971;Bainton et al, 1971;Breton-Gorius & Guichard, 1969;Dunn et al, 1968;Breton-Gorius & Reyes, 1976b). As stated above, the majority of blast cells, fixed with diluted aldehydes (method 2) contained a peroxidase-like activity.…”

Section: Cytochemical and Electron Microscopic Studymentioning

confidence: 69%

The Blast Crisis of Chronic Granulocytic Leukaemia: Megakaryoblastic Nature of Cells as Revealed by the Presence of Platelet‐Peroxidase—A Cytochemical Ultrastructural Study

et al. 1978

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The origin of cells in the blast crisis of some cases of chronic granulocytic leukaemia (CGL) remains controversial. Difficulties arise from the lack of cytochemical characteristics of differentiation. This report concerns the nature of cells in the blast crisis of a case of CGL in which blast cells exhibited an undifferentiated or lymphoid appearance by light and electron microscopy. The majority (90%) of such cells contained a peroxidase in the endoplasmic reticulum distinct from myeloperoxidase. In addition, some micromegakaryocytes could be recognized among the peroxidase reactive cells, by the presence of typical granules and demarcation membranes. Since this peroxidase exhibited identical characteristics to that of normal megakaryocytic precursors, these blast cells could be identified as megakaryoblasts. These data emphasize the possible megakaryoblastic nature of cells occurring in other cases of CGL blast crisis.

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Brief Report: Ultrastructural Localization of Myeloperoxidase in Human Neutrophil and Rabbit Heterophil and Eosinophil Leukocytes

Cited by 84 publications

References 6 publications

Endogenous generation of cyanide in neuronal tissue: Involvement of a peroxidase system

Endogenous generation of cyanide in neuronal tissue: Involvement of a peroxidase system

Ultrastructural visualization of complex carbohydrates in eosinophilic leukocytes

The Blast Crisis of Chronic Granulocytic Leukaemia: Megakaryoblastic Nature of Cells as Revealed by the Presence of Platelet‐Peroxidase—A Cytochemical Ultrastructural Study

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