Evidence for a LPS-binding protein in medfly hemocyte surface: mediation in LPS internalization but not in LPS signaling.
A doublet of medfly hemocyte proteins with a molecular mass of about 55 and 50 kDa were precipitated with LPS. Antibodies raised against human CD14 recognize the same doublet of proteins. These results support that mammalian CD14 and the doublet of protein bands in medfly hemocytes share common epitopes. This doublet of protein bands is released from hemocytes upon LPS triggering. A portion of the released protein is clustered on the surface of a distinct hemocyte type and the other remains soluble. The membrane-bound LPS-binding protein is involved in LPS internalization and Escherichia coli phagocytosis but not in LPS signaling.
Metheniti
Aristea
A
Department of Biology, University of Patras, Patras, Greece.
Giannakas
Nikos
N
Katsoulas
Haralabos L
HL
Soldatos
Anastasios N
AN
Tsakas
Sotiris
S
Lambropoulou
Maria
M
D000209:Acute-Phase Proteins; D000818:Animals; D015153:Blotting, Western; D002352:Carrier Proteins / Q000378:metabolism*; D033622:Ceratitis capitata / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004705:Endocytosis / Q000502:physiology; D005434:Flow Cytometry; D006434:Hemocytes / Q000378:metabolism*; D006801:Humans; D019476:Insect Proteins / Q000378:metabolism*; D018950:Lipopolysaccharide Receptors / Q000378:metabolism; D008070:Lipopolysaccharides / Q000378:metabolism*; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D011485:Protein Binding / Q000502:physiology; D000099231:Lipopolysaccharide-Binding Protein
D000209:Acute-Phase Proteins; D002352:Carrier Proteins; D019476:Insect Proteins; D018950:Lipopolysaccharide Receptors; D008070:Lipopolysaccharides; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D000099231:Lipopolysaccharide-Binding Protein; C440499:lipopolysaccharide, Escherichia coli O111 B4