Linked Life Data

3535903

Source:http://linkedlifedata.com/resource/pubmed/id/3535903

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-1-7
pubmed:abstractText
Human neutrophils can be permeabilized with the cholesterol complexing agent digitonin and then induced to secrete lysosomal constituents by increases in free Ca2+ alone. In order of increasing requirements for Ca2+, vitamin B-12 binding protein, lysozyme and beta-glucuronidase were released. A variety of guanine nucleotides were examined with respect to their abilities to modulate this response. GTP, along with its analogues 5'-guanylylimidodiphosphate (Gpp[NH]p) and guanosine-5'-O-[3-thio]-triphosphate (GTP[gamma S]) decreased the Ca2+ requirements for secretion of all three granule constituents by one third to one order of magnitude. This synergy was dependent upon the concentration of guanine nucleotides employed. The effects of Gpp[NH]p could be blocked with the inactive derivative GDP[beta-S]. The active guanine nucleotides, particularly GTP, served as stimuli in their own right. At high concentrations of Ca2+ and GTP, degranulation was strikingly inhibited; inhibition was also achieved with high concentrations of guanylyl[beta, gamma-methylene]diphosphate (Gpp[CH2]p). Both GDP and GMP were without any effect. When neutrophils were pretreated with pertussis toxin, granule discharge induced by fMet-Leu-Phe was almost completely blocked, as reported by others. If the neutrophils pretreated with pertussis toxin were then permeabilized with digitonin, the synergy between Ca2+ and the stimulatory guanine nucleotides was maintained. These data suggest the involvement of G-proteins in secretion induced by Ca2+; however, this response either uses a different G-protein or a different pool of G-proteins from those responses triggered by fMet-Leu-Phe.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Glucuronidase, http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate), http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Guanylyl Imidodiphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Muramidase, http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Thionucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
889
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Guanine nucleotides reduce the free calcium requirement for secretion of granule constituents from permeabilized human neutrophils.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't