Linked Life Data

3657801

Source:http://linkedlifedata.com/resource/pubmed/id/3657801

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1987-11-9
pubmed:abstractText
The ability of various compounds to inhibit the lytic activity of purified cytoplasmic granules from LGL tumors was tested. The lytic activity of granule cytolysin was modestly inhibited by inorganic phosphate, and various monophosphoesters, with I50 values in the range of 8-20 mM. Among monophosphoesters, choline phosphate was exceptionally potent, with an I50 of 1.4 mM. In contrast to the inhibition by phosphate esters, the parent compounds such as neutral sugars, glycerol, and choline, showed no detectable inhibition at 50 mM. A lysolipid bearing a short aliphatic chain and some detergents were inhibitory with I50 values in the range of 1 mM. Lysolipids with longer aliphatic chains, phospholipids as liposomes, and related lipid compounds were found to display potent inhibition of the hemolytic activity of LGL granule cytolysin, with I50 values in the range of 0.2-30 microM. Soluble globular proteins inhibited LGL granule cytolysin hemolytic activity with I50 of 0.07-0.4 mg/ml. However, lipoproteins were 2-3 orders of magnitude more potent inhibitors, with L50 values of less than 1 microgram/ml. The observed potent inhibition by lipid compounds lends support to a model of the lytic action of granule cytolysin in which soluble cytolysin molecules insert into the membrane lipid bilayer during the course of the lytic event.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
647-53
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Inhibition of cytolysin activity in large granular lymphocyte granules by lipids: evidence for a membrane insertion mechanism of lysis.
pubmed:affiliation
Immunology Branch, National Cancer Institute, Bethesda, MD 20892.
pubmed:publicationType
Journal Article