Linked Life Data

10625682

Source:http://linkedlifedata.com/resource/pubmed/id/10625682

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-2-18
pubmed:databankReference
pubmed:abstractText
A lipopolysaccharide- and beta-1,3-glucan-binding protein (LGBP) was isolated and characterized from blood cells (hemocytes) of the freshwater crayfish Pacifastacus leniusculus. The LGBP was purified by chromatography on Blue-Sepharose and phenyl-Sepharose, followed by Sephacryl S-200. The LGBP has a molecular mass of 36 kDa and 40 kDa on 10% SDS-polyacrylamide gel electrophoresis under reducing and nonreducing conditions, respectively. The calculated mass of LGBP is 39,492 Da, which corresponds to the native size of LGBP; the estimated pI of the mature LGBP is 5.80. LGBP has binding activity to lipopolysaccharides as well as to beta-1,3-glucans such as laminarin and curdlan, but peptidoglycan could not bind to LGBP. Cloning and sequencing of LGBP showed significant homology with several putative Gram-negative bacteria-binding proteins and beta-1, 3-glucanases. Interestingly, LGBP also has a structure and functions similar to those of the coelomic cytolytic factor-1, a lipopolysaccharide- and glucan-binding protein from the earthworm Eisenia foetida. To evaluate the involvement of LGBP in the prophenoloxidase (proPO) activating system, a polyclonal antibody against LGBP was made and used for the inhibition of phenoloxidase (PO) activity triggered by the beta-1,3-glucan laminarin in the hemocyte lysate of crayfish. The PO activity was blocked completely by the anti-LGBP antibody. Moreover, the PO activity could be recovered by the addition of purified LGBP. These results suggest that the 36-kDa LGBP plays a role in the activation of the proPO activating system in crayfish and thus seems to play an important role in the innate immune system of crayfish.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1337-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10625682-Amino Acid Sequence, pubmed-meshheading:10625682-Animals, pubmed-meshheading:10625682-Astacoidea, pubmed-meshheading:10625682-Base Sequence, pubmed-meshheading:10625682-Carrier Proteins, pubmed-meshheading:10625682-Chromatography, Affinity, pubmed-meshheading:10625682-Chromatography, Gel, pubmed-meshheading:10625682-Cloning, Molecular, pubmed-meshheading:10625682-DNA, Complementary, pubmed-meshheading:10625682-Fresh Water, pubmed-meshheading:10625682-Glucans, pubmed-meshheading:10625682-Gram-Negative Bacteria, pubmed-meshheading:10625682-Hemocytes, pubmed-meshheading:10625682-Kinetics, pubmed-meshheading:10625682-Lectins, pubmed-meshheading:10625682-Lipopolysaccharides, pubmed-meshheading:10625682-Molecular Sequence Data, pubmed-meshheading:10625682-Molecular Weight, pubmed-meshheading:10625682-Oligochaeta, pubmed-meshheading:10625682-Recombinant Proteins, pubmed-meshheading:10625682-Sequence Alignment, pubmed-meshheading:10625682-Sequence Homology, Amino Acid
pubmed:year
2000
pubmed:articleTitle
A lipopolysaccharide- and beta-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus. Purification, characterization, and cDNA cloning.
pubmed:affiliation
Department of Comparative Physiology, Evolutionary Biology Center, Uppsala University, Norbyvägen 18A, S-75236, Uppsala, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't