Linked Life Data

21140394

Source:http://linkedlifedata.com/resource/pubmed/id/21140394

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-12-28
pubmed:abstractText
The chemokine stromal cell-derived factor-1? (SDF1?) is strongly involved in organogenesis, as well as inflammation and tissue repair, and acts by attracting different kinds of stem and progenitor cells. Therefore, it constitutes an interesting compound for drug development in regenerative medicine. However, it is prone to inactivation by proteolytic cleavage in human serum. Accordingly, it has to be stabilized against enzymatic degradation for any therapeutic application. We synthesized a palmitoylated SDF1? analogue by native chemical ligation. Both the N-terminal thioester and the C-terminal palmitoylated fragment were prepared by solid-phase peptide synthesis. The activity of the refolded and pure compound was determined by an inositol phosphate turnover assay and revealed no loss in receptor activation. Additionally, resistance to proteolytic degradation was investigated in porcine liver homogenates and showed a near sevenfold increased half time. This study is a proof of principle approach for the lipidation of SDF1? and provides a basis for further engineering of the chemokine in order to increase its therapeutic value.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1860-7187
pubmed:author
pubmed:issnType
Electronic
pubmed:day
3
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-200
pubmed:dateRevised
2011-9-5
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Palmitoylated SDF1? shows increased resistance against proteolytic degradation in liver homogenates.
pubmed:affiliation
Institute of Biochemistry, Leipzig University, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't