Co-localization of superoxide generation and NADP formation in plasma membrane fractions from human neutrophils
In order to resolve discrepancies in the literature concerning the subcellular localization of NADPH oxidase, we disrupted human neutrophils by nitrogen cavitation and fractionated the subcellular organelles on a discontinuous sucrose density gradient. The lightest fraction was 20- to 40-fold enrich...
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| Veröffentlicht in: | Inflammation 1984-09, Vol.8 (3), p.323-335 |
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| creator | SHIRLEY, P. S BASS, D. A LEES, C. J PARCE, J. W WAITE, B. M DECHATELET, L. R |
| description | In order to resolve discrepancies in the literature concerning the subcellular localization of NADPH oxidase, we disrupted human neutrophils by nitrogen cavitation and fractionated the subcellular organelles on a discontinuous sucrose density gradient. The lightest fraction was 20- to 40-fold enriched for plasma membranes as determined by the marker enzymes alkaline phosphatase and phosphodiesterase I as well as by the ratio of lipid phosphorus to protein. There was a significant decrease in the specific activities of the granule markers myeloperoxidase, lysozyme, and beta-glucuronidase. An intermediate fraction was enriched in membrane markers but not to the extent the lightest fraction was enriched. This fraction contained more granular contamination, as shown by the marker enzymes. In contrast, the densest bands of the gradient were enriched for granule markers with little contamination by plasma membrane. Superoxide generation and NADP formation were primarily associated with the two membrane-enriched fractions from polymorphonuclear leukocytes stimulated with phorbol myristate acetate. The NADP formation associated with a dense granule fraction observed previously in our laboratory was probably due to a cyanide-stimulated oxidation of NADPH by myeloperoxidase. |
| doi_str_mv | 10.1007/BF00916420 |
| format | Article |
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This fraction contained more granular contamination, as shown by the marker enzymes. In contrast, the densest bands of the gradient were enriched for granule markers with little contamination by plasma membrane. Superoxide generation and NADP formation were primarily associated with the two membrane-enriched fractions from polymorphonuclear leukocytes stimulated with phorbol myristate acetate. 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There was a significant decrease in the specific activities of the granule markers myeloperoxidase, lysozyme, and beta-glucuronidase. An intermediate fraction was enriched in membrane markers but not to the extent the lightest fraction was enriched. This fraction contained more granular contamination, as shown by the marker enzymes. In contrast, the densest bands of the gradient were enriched for granule markers with little contamination by plasma membrane. Superoxide generation and NADP formation were primarily associated with the two membrane-enriched fractions from polymorphonuclear leukocytes stimulated with phorbol myristate acetate. The NADP formation associated with a dense granule fraction observed previously in our laboratory was probably due to a cyanide-stimulated oxidation of NADPH by myeloperoxidase.</description><subject>Alkaline Phosphatase - metabolism</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Cell physiology</subject><subject>Cell Separation - methods</subject><subject>Cyanides - pharmacology</subject><subject>Endocytosis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucuronidase - metabolism</subject><subject>Humans</subject><subject>leukocytes (neutrophilic)</subject><subject>man</subject><subject>Molecular and cellular biology</subject><subject>Muramidase - metabolism</subject><subject>NADP</subject><subject>NADP - biosynthesis</subject><subject>Neutrophils - cytology</subject><subject>Neutrophils - enzymology</subject><subject>Peroxidase - metabolism</subject><subject>Phosphoric Diester Hydrolases - metabolism</subject><subject>plasma membranes</subject><subject>respiratory burst</subject><subject>superoxide</subject><subject>Superoxides - biosynthesis</subject><issn>0360-3997</issn><issn>1573-2576</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1r3DAQxUVoSDcfl9wLOpQcCk70YUue43bTTQsh6aE9G8kaZx0sy5HW0PSvj8Iu22NPM8z78RjeI-SSs2vOmL75umYMuCoFOyILXmlZiEqrD2TBpGKFBNAfyWlKz4yxGmp5Qk4UAyG0WpCwCsUQWjP0f822DyMNHU3zhDH86R3SJxwx7gQzOvqwvP1JuxD97tSPdBpM8oZ69DaaEWkXTfuupbwFTzezNyMdcd7GMG36IZ2T484MCS_284z8Xn_7tfpe3D_e_Vgt74tWlmJbgCuVQW0NutIxVlYIte0qtE6pfJClttA5AJBaK3CmqlDYmjvFbS2d7eQZudr5TjG8zJi2je9Ti8OQnwxzamouQACI_4K8lKoGqDL4ZQe2MaQUsWum2HsTXxvOmvcamn81ZPjT3nW2Ht0B3eee9c973aQcfk5tbPt0wCDbKaHlG9tVkII</recordid><startdate>198409</startdate><enddate>198409</enddate><creator>SHIRLEY, P. 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There was a significant decrease in the specific activities of the granule markers myeloperoxidase, lysozyme, and beta-glucuronidase. An intermediate fraction was enriched in membrane markers but not to the extent the lightest fraction was enriched. This fraction contained more granular contamination, as shown by the marker enzymes. In contrast, the densest bands of the gradient were enriched for granule markers with little contamination by plasma membrane. Superoxide generation and NADP formation were primarily associated with the two membrane-enriched fractions from polymorphonuclear leukocytes stimulated with phorbol myristate acetate. The NADP formation associated with a dense granule fraction observed previously in our laboratory was probably due to a cyanide-stimulated oxidation of NADPH by myeloperoxidase.</abstract><cop>New York, NY</cop><pub>Springer</pub><pmid>6092276</pmid><doi>10.1007/BF00916420</doi><tpages>13</tpages></addata></record> |
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| subjects | Alkaline Phosphatase - metabolism Biological and medical sciences Cell Membrane - metabolism Cell physiology Cell Separation - methods Cyanides - pharmacology Endocytosis Fundamental and applied biological sciences. Psychology Glucuronidase - metabolism Humans leukocytes (neutrophilic) man Molecular and cellular biology Muramidase - metabolism NADP NADP - biosynthesis Neutrophils - cytology Neutrophils - enzymology Peroxidase - metabolism Phosphoric Diester Hydrolases - metabolism plasma membranes respiratory burst superoxide Superoxides - biosynthesis |
| title | Co-localization of superoxide generation and NADP formation in plasma membrane fractions from human neutrophils |
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