Linked Life Data

9852202

Source:http://linkedlifedata.com/resource/pubmed/id/9852202

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-3-16
pubmed:abstractText
The effects of the antibacterial protein Drosophila cecropin A on developmental forms of Leishmania were compared with the effect of Hyalophora cecropin A in vitro. Both cecropins had a potent lytic activity on the promastigotes at concentrations not far from those occurring in vivo in the respective insect. Drosophila cecropin A had strong differential effects on the two maturation forms of Leishmania aethiopica at high concentrations: inhibiting intracellular amastigotes and stimulating extracellular promastigotes to take up thymidine. Hyalophora cecropin A also inhibited amastigotes by up to 50% at concentrations of 0.250 mg/ml, and inhibited promastigotes at high concentrations but had no enhancing effects at any of the concentrations tested. In contrast to the results with Leishmania, Drosophila cecropin A had no discernible effect on any developmental stage of P. falciparium and showed no lytic effects on haemocytes. The two enantiomers of a synthetic amphipathic peptide, D- and L-KALA, were also tested. D- and L-KALA had some in vitro antimalarial effects at 0.025 and 0.05 mg/ml respectively but both forms were haemolytic at 0.1 mg/ml. Potential uses of naturally occurring proteins and their derivatives in the control of insect born infections and topical use of cecropins against leishmaniasis are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1107-3756
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
77-82
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Drosophila antibacterial protein, cecropin A, differentially affects non-bacterial organisms such as Leishmania in a manner different from other amphipathic peptides.
pubmed:affiliation
Microbiology and Tumor Biology Centre, Karolinska Institute, 17177 Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't