Linked Life Data

2555283

Source:http://linkedlifedata.com/resource/pubmed/id/2555283

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-1-10
pubmed:abstractText
Bacteria and yeasts which are "opsonized" with cationic polyelectrolytes (poly-L-arginine, poly-L-histidine and arginine-rich histone) are avidly endocytosed by both "professional" and "non-professional" phagocytes. The cationized particles also strongly activate the respiratory burst in neutrophils and in macrophages leading to the generation of chemiluminescence, superoxide and hydrogen peroxide. On the other hand, lysine and ornithine-rich polymers are poor opsonic agents. Poly L-arginine is unique in its capacity to act synergistically with lectins, with chemotactic peptides and with cytochalasin B to generate large amounts of chemiluminescence and superoxide in human neutrophils. Unlike polyarginine, polyhistidine, in the absence of carrier particles, is one of the most potent stimulators of superoxide generations, known. Neutrophils treated with cetyltrimethylammonium bromide fail to generate superoxide, but generate strong luminol-dependent chemiluminescence which is totally inhibited by sodium azide and by thiourea. Neutrophils injured by cytolytic agents (saponin, digitonin, lysolecithin) lose their chemiluminescence and superoxide-generating capacities upon stimulation by a variety of ligands. These activities are however regained by the addition of NADPH. Lysolecithin can replace polyarginine in a "cocktail" also containing lectins and cytochalasin B, which strongly activate the respiratory burst. This suggests that polyarginine acts both as a cytolytic agent and as a ligand. Arginine and histidine-rich polyelectrolytes enhance the pathogenic effects of immune complexes in vivo (reversed Arthus phenomenon) presumably by "glueing" them to tissues. Polyhistidine complexed to catalase or to superoxide dismutase, markedly enhances their efficiency as antioxidants. On the other hand polyhistidine complexed to glucose oxidase markedly enhances injury to endothelial cells suggesting that the close association of the cationized enzyme with the plasma membrane facilitates the interaction of hydrogen peroxide with the targets. A variety of cationic agents (histone, polyarginine, polyhistidine, polymyxin B) and membrane-active agents (lysophosphatides, microbial hemolysins) act synergistically with glucose oxidase or with reagent hydrogen peroxide to kill target cells. The mechanisms by which arginine- and histidine-rich polyelectrolytes activate the respiratory burst in neutrophils might involve interaction with G-proteins, the activation of arachidonic acid metabolism and phospholipase A2, or the interaction with myeloperoxidase. Naturally-occurring cationic proteins might modulate several important functions of leukocytes and the course and outcome of the inflammatory process.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
8755-0199
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-26
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Cationic polyelectrolytes: potent opsonic agents which activate the respiratory burst in leukocytes.
pubmed:affiliation
Department of Oral Biology, Hebrew University-Hadassah School of Dental Medicine, Jerusalem, Israel.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't