Linked Life Data

12097327

Source:http://linkedlifedata.com/resource/pubmed/id/12097327

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
2002-9-2
pubmed:abstractText
MARCO is a type II transmembrane protein of the class A scavenger receptor family. It has a short N-terminal cytoplasmic domain, a transmembrane domain, and a large extracellular part composed of a 75-residue long spacer domain, a 270-residue collagenous domain, and a 99-residue long scavenger receptor cysteine-rich (SRCR) domain. Previous studies have indicated a role for this receptor in anti-microbial host defense functions. In this work we have produced the extracellular part of MARCO as a recombinant protein, and analyzed its binding properties. The production of this protein, soluble MARCO (sMARCO), has made it possible for the first time to study MARCO and its binding properties in a cell-free system. Using circular dichroism analyses, a protease-sensitive assay, and rotary shadowing electron microscopy, sMARCO was shown to have a triple-helical collagenous structure. Rotary shadowing also demonstrated that the molecules often associate with each other via the globes. sMARCO was found to bind avidly both heat-killed and living bacteria. Lipopolysaccharide, an important component of the outer membrane of Gram-negative bacteria, was shown to be a ligand of MARCO. Studies with different bacterial strains indicated that the O-side chain of lipopolysaccharide is not needed for the bacterial recognition. Finally, the C-terminal SRCR domain was also produced as a recombinant protein, and its bacteria-binding capability was studied. Although the transfection experiments with transmembrane MARCO variants have indicated a crucial role for this domain in bacterial binding, the monomeric domain exhibited low, barely detectable bacteria-binding activity. Thus, it is possible that cooperation between the SRCR domain and the collagenous domain is needed for high-affinity bacterial binding, or that the SRCR domain has to be in a trimeric form to effectively bind to bacteria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33378-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12097327-Amidohydrolases, pubmed-meshheading:12097327-Cell Line, pubmed-meshheading:12097327-Circular Dichroism, pubmed-meshheading:12097327-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:12097327-Escherichia coli, pubmed-meshheading:12097327-Humans, pubmed-meshheading:12097327-Ligands, pubmed-meshheading:12097327-Lipopolysaccharides, pubmed-meshheading:12097327-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, pubmed-meshheading:12097327-Protein Binding, pubmed-meshheading:12097327-Protein Conformation, pubmed-meshheading:12097327-Protein Folding, pubmed-meshheading:12097327-Protein Structure, Tertiary, pubmed-meshheading:12097327-Receptors, Immunologic, pubmed-meshheading:12097327-Recombinant Proteins, pubmed-meshheading:12097327-Transfection, pubmed-meshheading:12097327-Trypsin
pubmed:year
2002
pubmed:articleTitle
Characterization of recombinant soluble macrophage scavenger receptor MARCO.
pubmed:affiliation
Division of Matrix Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't