Linked Life Data

16454673

Source:http://linkedlifedata.com/resource/pubmed/id/16454673

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2006-2-3
pubmed:abstractText
Shrimp High Density Lipoprotein-beta-Glucan Binding Protein (HDL/BGBP) has been studied by its role in nutrition and innate defense. Although the mechanisms of lipid loading are still unknown, HDL-BGBP binds and aggregates phospholipids vesicles in vitro. To gain insights into the HDL-BGBP mechanism of interaction with membranes, we have used fluorescence spectroscopy and electron microscopy. Data show that HDL-BGBP does not induce membrane fusion, leakage nor lipid exchange, although microstructural changes are clearly observed. This work supports a model where protein aggregation leads to liposome clustering. Such interaction may be a critical factor for the activation of the shrimp blood cell in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0929-8665
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-5
pubmed:dateRevised
2011-3-31
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Biophysical characterization of the non-fusogenic interaction between liposomes and the shrimp bifunctional lipoprotein-beta-glucan binding protein HDL/BGBP.
pubmed:affiliation
Aquatic Molecular Biology Laboratory, Centro de Investigación en Alimentación y Desarrollo, A.C. PO Box 1735, Hermosillo Sonora, 83000 México.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't