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Titolo:
ANALYSIS OF LIPOPOLYSACCHARIDE-BINDING BY CD14
Autore:
KIRKLAND TN; FINLEY F; LETURCQ D; MORIARTY A; LEE JD; ULEVITCH RJ; TOBIAS PS;
Indirizzi:
VET ADM MED CTR,111F,3350 LA JOLLA VILLAGE DR SAN DIEGO CA 92161 UNIV CALIF SAN DIEGO,DEPT PATHOL SAN DIEGO CA 92103 UNIV CALIF SAN DIEGO,DEPT MED SAN DIEGO CA 92103 RW JOHNSON PHARMACEUT RES INST SAN DIEGO CA 92121 SCRIPPS CLIN & RES FDN,RES INST LA JOLLA CA 92037
Titolo Testata:
The Journal of biological chemistry
fascicolo: 33, volume: 268, anno: 1993,
pagine: 24818 - 24823
SICI:
0021-9258(1993)268:33<24818:AOLBC>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
LPS BINDING; BACTERIAL LIPOPOLYSACCHARIDE; 70Z/3 CELLS; PROTEIN; RECEPTOR; SITES; IDENTIFICATION; ENDOTOXINS; PHAGOCYTES; COMPLEXES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
T.N. Kirkland et al., "ANALYSIS OF LIPOPOLYSACCHARIDE-BINDING BY CD14", The Journal of biological chemistry, 268(33), 1993, pp. 24818-24823

Abstract

The cell surface protein CD14 binds bacterial lipopolysaccharide (LPS) in the presence of the serum protein, LPS-binding protein (LBP). This interaction is important for LPS-induced activation of mammalian myeloid cells. We performed quantitative studies of H-3-labeled LPS binding to human CD14 expressed on Chinese hamster ovary cells and on a human macrophage cell line (THP-1). At the concentrations studied (20-100nM) LPS binding required the expression of CD14 and could be inhibited by a subset of anti-CD14 monoclonal antibodies. LBP was required forLPS binding to CD14. The binding occurred within 10 min and was relatively unaffected by temperature over the range of 4-37-degrees-C. Quantitative binding assays were performed at 10-degrees-C, or at 37-degrees-C, using Chinese hamster ovary cells depleted of ATP. In both cases, 75-90% of the LPS could be released by treatment with phosphatidylinositol-specific phospholipase C, suggesting that it remains associatedwith the glycosyl phosphatidylinostol-anchored CD14. The apparent dissociation constant of recombinant human CD14 expressed on Chinese hamster ovary cells for LPS at 10-degrees-C was 2.74 (+/- 0.99) x 10(-8) M; the apparent dissociation constant of CD14 expressed on THP-1 cells at 10-degrees-C was 4.89 (+/- 1.42) x 10(-8) M. In both cell lines, atsaturating LPS concentrations, the molar ratio of LPS bound per surface CD14 was approximately 20:1. At 37-degrees-C the apparent dissociation constant of recombinant human CD14 for LPS at 37-degrees-C was 2.7(+/- 1.2) x 10(-8) M, and the molar ratio of LPS bound per surface CD14 was approximately 8:1. Although the difference in molar ratio of LPS bound per surface CD14 at the two temperatures is difficult to interpret, it is clear that at both temperatures the molar ratio is not 1:1. The basis of this phenomenon is unclear, but may involve the repeated leucine-rich motifs, which are found within CD14.

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Documento generato il 19/10/18 alle ore 20:42:27