Linked Life Data

12782180

Source:http://linkedlifedata.com/resource/pubmed/id/12782180

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2003-6-3
pubmed:abstractText
The peptides for-Met-Leu-Tyr-OMe, for-Met-Leu-Glu-OMe, for-Met-Leu-Asp-OMe and for-Met-Leu-Ser-OMe were synthesized to investigate the importance of a hydrophilic side chain of the residue at position 3 on biological activities of human neutrophils. A number of in vitro essays were carried out, including: chemotaxis, superoxide anion production, lysozyme release and receptor binding. Our results highlight that for-Met-Leu-Asp-OMe acts as a full agonist with a higher efficacy than formyl-Met-Leu-Phe-OMe, the tripeptide normally used as a model chemoattractant for the study of cell functions. The other analogs show efficacies that are in the same range or a little less than the prototype. The main point emerging from this study is that the role of Phe substitution needs to be re-hypothesised.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2999
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
469
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Hydrophilic residues at position 3 highlight unforeseen features of the fMLP receptor pocket.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, University of Ferrara, Via L. Borsari 46, 44100 Ferrara, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't