The interaction of Escherichia coli with normal human serum: factors affecting the capacity of serum to mediate lipopolysaccharide release

1988 ◽  
Vol 4 (3) ◽  
pp. 175-187 ◽  
Author(s):  
Vernon L. Tesh ◽  
David C. Morrison
Keyword(s):  
Escherichia Coli ◽  
Human Serum ◽  
Normal Human Serum ◽  
Serum Factors ◽  
Factors Affecting ◽  
Normal Human

scholarly journals RECEPTOR FOR SOLUBLE C3 AND C3b ON HUMAN LYMPHOBLASTOID (RAJI) CELLS

1974 ◽  
Vol 139 (3) ◽  
pp. 696-711 ◽  
Author(s):  
Argyrios N. Theofilopoulos ◽  
Viktor A. Bokisch ◽  
Frank J. Dixon
Keyword(s):  
Cell Membrane ◽  
Human Serum ◽  
Cell Membranes ◽  
Raji Cell ◽  
Membrane Damage ◽  
Normal Human Serum ◽  
Serum Factors ◽  
Raji Cells ◽  
Immune Adherence ◽  
Normal Human

This study describes the presence of a receptor for fluid phase human C3 and C3b on Raji cell membranes. The binding of C3 and C3b was demonstrated indirectly by a fluoresceinated anti-C3 serum and directly by using radioiodinated proteins. No other complement proteins or serum factors were needed to mediate binding of C3 and C3b to the receptor. The possibility of enzymatic cleavage of C3 before or after its attachment on the cell membrane was ruled out by the demonstration of antigenically intact C3 on Raji cells. Inhibition and dissociation of Raji cell-EAC1423 rosettes by C3 and C3b indicated that both of these proteins bind to the same receptor site or closely associated receptor sites on Raji cells. C3b-bearing Raji cells were immune adherence negative, indicating that C3b binding to the receptor is brought about through the immune adherence region of the molecule and not the C3d portion. The C3 receptor on Raji cell membranes is uniformly distributed and can move on the membrane plane. Approximately 4 x 105 molecules of C3 or C3b bind per Raji cell. The receptor had a higher affinity for C3 than C3b, as was shown by uptake experiments and inhibition of Raji cell-EAC1423 rosette formation. Apart from the described receptor for C3 and C3b another specific receptor for C3b inactivator-cleaved C3b (C3d) bound to red cells was shown to be present on Raji cells. Raji cells cultured in medium containing fresh normal human serum and cobra venom factor were lysed. Similar results were obtained when C3b-bearing Raji cells were cultured in medium with fresh normal human serum. The lytic effect could be abolished by inactivating serum C3 proactivator (C3PA) and required C6. It was concluded that C3b bound to the Raji cell membrane activates the complement system through the alternate pathway and results in membrane damage and cytolysis. It is postulated that cell destruction by this mechanism may play an important role in vivo in controlling cell growth.

THE COMPLEMENT-DEPENDENT BACTERIOLYTIC ACTIVITY OF NORMAL HUMAN SERUM: II. CELL WALL COMPOSITION OF SENSITIVE AND RESISTANT STRAINS

1963 ◽  
Vol 9 (1) ◽  
pp. 41-52 ◽  
Author(s):  
A. C. Wardlaw
Keyword(s):  
Cell Wall ◽  
Human Serum ◽  
Resistant Strain ◽  
Cell Walls ◽  
Sensitive Strain ◽  
Normal Human Serum ◽  
Serum Factors ◽  
Rough Strain ◽  
Normal Human ◽  
Smooth Strain

A comparative study has been made of the chemical composition of cell walls from two strains of Escherichia coli—one rough strain which was very sensitive to killing and lysis by normal human serum, and one smooth strain which was relatively insensitive to killing and was not lysed at all. The major components in the cell walls of both strains were protein and (or) polypeptide (70–80%) and lipid (14%), no significant differences in either component being detected between the two strains. A marked difference was, however, detected in the lipopolysaccharide fraction which was present to the extent of only 1% in the walls of the rough, serum-sensitive strain and 9% in the smooth, serum-resistant strain. Moreover, the two lipopolysaccharides were qualitatively different in sugar composition, that from the resistant strain yielding glucose, galactose, rhamnose, and two minor sugar components, while that from the sensitive strain yielded glucose only. These findings are discussed in relation to the three-layer theory for the structure of the coli cell wall and in relation to the serum factors (antibody, properdin, complement, and lysozyme) which may participate in the destruction of bacteria by serum.

Evaluation of a commercially available radioimmunoassay kit for measurement of doxorubicin in plasma.

1982 ◽  
Vol 28 (1) ◽  
pp. 119-121 ◽  
Author(s):  
E Piall ◽  
G W Aherne ◽  
V Marks
Keyword(s):  
Human Serum ◽  
Normal Human Serum ◽  
Nonspecific Effects ◽  
Normal Human ◽  
Doxorubicin Concentration

Abstract We evaluated a commercially available (Diagnostic Biochemistry Inc.) doxorubicin 125I radioimmunoassay kit. This kit gave a high apparent doxorubicin concentration (greater than 12 micrograms/L), which was not linearly related to dilution, for two pools of normal human serum and plasma and also for samples collected from patients before they received the drug. In contrast, a doxorubicin 3H radioimmunoassay developed by us gave a low blank (2 micrograms/L), which was linearly related to dilution, for the same pools and patients' samples. Doxorubicin concentrations in the plasma of patients receiving the drug were compared by the two methods; the kit gave results five- to 10-fold those obtained with our assay. High nonspecific interference by serum and plasma as measured by the 125I radioimmunoassay must therefore be borne in mind by users of the kit, and we suggest that results should be corrected for these nonspecific effects.

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