Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-6-29
pubmed:abstractText
The effect of phagocytosis on the H(2)O(2) production and myeloperoxidase (MPO) activities of leukocytes from various species was investigated. The intracellular distribution of MPO, reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase (6PGDH) of resting and phagocytizing guinea pig polymorphonuclear leukocytes has also been studied. Phagocytizing cells produce more H(2)O(2) than the corresponding resting cells. This has been found to be true for human peripheral polymorphonuclear leukocytes, mouse peritoneal macrophage, and guinea pig and rat peritoneal polymorphonuclear leukocytes. All of these cells, except rabbit alveolar macrophages, have significant MPO activity. Generally an increased activity is noted with phagocytizing cells. Homogenization and differential centrifugation of guinea pig peritoneal polymorphonuclear leukocytes indicate that the whole homogenate and its fractions from phagocytizing cells have significantly higher MPO and NADPH oxidase activities, when compared to the corresponding fractions from the resting cells. The 27,000 x g supernatant fluid from phagocytizing cells has 6-fold more MPO and 2.5-fold more NADPH oxidase activity than similar supernatant fractions from resting cells. The enzyme 6PGDH was unaffected by phagocytosis. The relationship of these stimulated activities to the intracellular bactericidal function of the phagocytes has been discussed.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-13319580, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-13654378, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-13727273, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-13879306, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-13957122, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4160029, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4182532, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4285172, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4380197, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4381885, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4383408, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4384488, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4864533, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4868928, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4881700, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4883937, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4892384, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4964478, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4964565, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-4970226, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-5337539, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-5344114, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-5661632, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-5662845, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-5765020, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-5788695, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-5817553, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-5934974, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-5969807, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-6036538, http://linkedlifedata.com/resource/pubmed/commentcorrection/16557739-6077040
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Apr
pubmed:issn
0019-9567
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
338-44
pubmed:dateRevised
2010-9-14
pubmed:year
1970
pubmed:articleTitle
Function of h(2)o(2), myeloperoxidase, and hexose monophosphate shunt enzymes in phagocytizing cells from different species.
pubmed:affiliation
Department of Pathology and Medical Research, St. Margaret's Hospital, and Department of Obstetrics and Gynecology, Tufts University Medical School, Boston, Massachusetts 02125.
pubmed:publicationType
Journal Article