Endotoxin Antagonism by a Synthetic Lipid A Analog, DT-5461, with Low Endotoxicity in Human Peripheral Blood Monocytes

1995 ◽  
Vol 216 (1) ◽  
pp. 367-374
Author(s):  
K. Sato ◽  
M. Fujihara ◽  
T.A. Takahashi ◽  
Y.C. Yoo ◽  
K. Hata ◽  
...  
Keyword(s):  
Peripheral Blood ◽  
Lipid A ◽  
Human Peripheral Blood ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes

scholarly journals Characteristics of lipopolysaccharide interaction with human peripheral-blood monocytes

1985 ◽  
Vol 232 (2) ◽  
pp. 379-383 ◽  
Author(s):  
S J Warner ◽  
N Savage ◽  
D Mitchell
Keyword(s):  
Cell Membrane ◽  
Peripheral Blood ◽  
Lipid A ◽  
Human Peripheral Blood ◽  
Human Monocyte ◽  
Polymyxin B ◽  
Salmonella Typhi ◽  
Apparent Difference ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes

The interaction between radioiodinated lipopolysaccharide from Escherichia coli 0111:B4 (125I-LPS) and human peripheral-blood monocytes was studied. The association of 125I-LPS with monocytes at 37 degrees C appeared to depend on binding to the cell membrane with subsequent internalization of the molecule, and was not saturable with time (up to 2 h) or 125I-LPS concentration (up to 10 micrograms/ml). There was no apparent difference in the behaviour of unlabelled LPS and 125I-LPS with respect to monocyte association. 125I-LPS association with monocytes was inhibited by LPS and O-polysaccharide from E. coli 0111:B4 and Salmonella typhi 0901, but not by lipid A or polymyxin B. We propose that the mechanism of human monocyte stimulation by LPS involves polysaccharide-dependent binding to the cell membrane followed by internalization of the LPS molecule. We were unable to demonstrate a specific LPS receptor such as that found on murine B-lymphocytes.

scholarly journals Identification of normal human peripheral blood monocytes and liver as sites of synthesis of coagulation factor XIII a-chain

Blood ◽  
1987 ◽  
Vol 70 (2) ◽  
pp. 579-582
Author(s):  
LJ Weisberg ◽  
DT Shiu ◽  
PR Conkling ◽  
MA Shuman
Keyword(s):  
Peripheral Blood ◽  
Factor Xiii ◽  
Human Peripheral Blood ◽  
Cdna Probe ◽  
Coagulation Factor ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Normal Human ◽  
Normal Human Peripheral Blood ◽  
A Chain

Factor XIII is the fibrin-stabilizing factor that covalently cross- links fibrin monomers to form a highly organized, stable fibrin clot. The plasma form of factor XIII is a heterodimer, a2b2, consisting of two a-chains and two b-chains; the intracellular form, such as in platelets and placenta, is a dimer, a2, consisting of a-chains only. The catalytic function of factor XIII, a transglutaminase, resides in the a-chain. To address questions regarding sites of synthesis of factor XIII a-chain, an EcoRI restriction fragment from the protein- coding region of the factor XIII a-chain cDNA was used as a probe for Northern blot analysis. The cDNA probe showed hybridization with a single approximately 4.0-kilobase (kb) message in poly (A)+ mRNA prepared from normal human peripheral blood monocytes and normal human liver. The results demonstrate conclusively that factor XIII a-chains are actively synthesized in circulating monocytes and in liver. To our knowledge, these data represent the first demonstration of synthesis of any blood coagulation factor in primary uncultured and unstimulated monocytes or macrophage cells.

scholarly journals Peroxynitrite reduces endotoxin-induced tissue factor expression in human peripheral blood monocytes

Critical Care ◽  
10.1186/cc29 ◽  
1997 ◽  
Vol 1 (Suppl 1) ◽  
pp. P023
Author(s):  
M Gerlach ◽  
D Keh ◽  
S Spielmann ◽  
T Kerner ◽  
R Peter ◽  
...  
Keyword(s):  
Tissue Factor ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Tissue Factor Expression ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Factor Expression

scholarly journals Evidence for specific annexin I-binding proteins on human monocytes

1996 ◽  
Vol 316 (2) ◽  
pp. 593-597 ◽  
Author(s):  
Nicolas J. GOULDING ◽  
L PAN ◽  
Kathleen WARDWELL ◽  
Veronica C. GUYRE ◽  
Paul M. GUYRE
Keyword(s):  
Monoclonal Antibody ◽  
Peripheral Blood ◽  
Binding Proteins ◽  
Human Peripheral Blood ◽  
Flow Cytometric Analysis ◽  
Blood Monocytes ◽  
Surface Binding ◽  
Peripheral Blood Monocytes ◽  
Cell Functions ◽  
Annexin I

Recombinant human annexin I and a monoclonal antibody specific for this protein (mAb 1B) were used to investigate surface binding of this member of the annexin family of proteins to peripheral blood monocytes. Flow cytometric analysis demonstrated trypsin-sensitive, saturable binding of annexin I to human peripheral blood monocytes but not to admixed lymphocytes. A monoclonal antibody that blocks the anti-phospholipase activity of annexin I also blocked its binding to monocytes. These findings suggest the presence of specific binding sites on monocytes. Furthermore, surface iodination, immunoprecipitation and SDS/PAGE analysis were used to identify two annexin I-binding proteins on the surface of monocytes with molecular masses of 15 kDa and 18 kDa respectively. The identification and characterization of these annexin I-binding molecules should help us to better understand the specific interactions of annexin I with monocytes that lead to down-regulation of pro-inflammatory cell functions.

Sign in / Sign up

Export Citation Format

Share Document