Fu-ling, a chinese herbal drug, modulates cytokine secretion by human peripheral blood monocytes

1996 ◽  
Vol 18 (1) ◽  
pp. 37-44 ◽  
Author(s):  
Shu-Jiuan Yu ◽  
Jerming Tseng
Keyword(s):  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Cytokine Secretion ◽  
Herbal Drug ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Chinese Herbal

scholarly journals RANTES Modulates TLR4-Induced Cytokine Secretion in Human Peripheral Blood Monocytes

2006 ◽  
Vol 177 (8) ◽  
pp. 5077-5087 ◽  
Author(s):  
Shiva Shahrara ◽  
Christy C. Park ◽  
Vladislav Temkin ◽  
Jared W. Jarvis ◽  
Michael V. Volin ◽  
...  
Keyword(s):  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Cytokine Secretion ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes

scholarly journals Interleukin 7 induces cytokine secretion and tumoricidal activity by human peripheral blood monocytes.

1991 ◽  
Vol 173 (4) ◽  
pp. 923-930 ◽  
Author(s):  
M R Alderson ◽  
T W Tough ◽  
S F Ziegler ◽  
K H Grabstein
Keyword(s):  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Optimal Concentration ◽  
Cytokine Secretion ◽  
Tnf Alpha ◽  
Northern Hybridization ◽  
Blood Monocytes ◽  
Tumoricidal Activity ◽  
Peripheral Blood Monocytes ◽  
Interleukin 7

Peripheral blood monocytes can be induced by stimuli such as bacterial lipopolysaccharide (LPS) to secrete an array of cytokines. We have studied the effects of interleukin 7 (IL-7) on human peripheral blood mononuclear cells (PBMC) and found that IL-7 is a relatively potent inducer of IL-6 secretion IL-6 protein levels were determined either by the B9 hybridoma growth factor assay or by enzyme-linked immunosorbent assay, and mRNA for IL-6 was analyzed by Northern hybridization. Detailed examination revealed that, among PBMC, monocytes, rather than lymphocytes, were secreting IL-6 in response to IL-7. In contrast to the low concentrations of IL-7 required to stimulate T cell growth and differentiation (as low as 0.1 ng/ml), relatively high concentrations of IL-7 were necessary to induce IL-6 secretion by monocytes (at least 10 ng/ml). An optimal concentration of IL-7 (100 ng/ml) induced monocytes to secrete 10-fold more IL-6 than an optimal concentration of IL-1 beta (10 ng/ml), and almost as much as LPS. However, significantly more IL-7 than IL-1 beta was required to induce detectable levels of IL-6. The kinetics of IL-6 secretion by monocytes were identical in response to IL-7, IL-1 beta, or LPS, with IL-6 protein detectable in culture supernatants as early as 2 h after the initiation of culture. IL-4 was found to markedly inhibit the ability of IL-7 or LPS to induce IL-6 mRNA and IL-6 secretion. In addition to promoting IL-6 production, IL-7 induced the secretion of immunoreactive IL-1 alpha, IL-1 beta, and tumor necrosis factor alpha (TNF-alpha) by monocytes. IL-7 also induced monocyte/macrophage tumoricidal activity against a human melanoma cell target, an activity that may be related to the secretion of IL-1 alpha, IL-1 beta, and TNF-alpha. Finally, we used a whole blood culture system as a bridge to in vivo analysis to demonstrate that IL-7 induces cytokine secretion in the absence of culture medium, fetal calf serum, and adherence to plastic. Our data suggest that IL-7, in addition to regulating lymphocyte growth and differentiation, has potent effects on cells of the monocytic lineage. Thus, IL-7 may be an important mediator in inflammation and in the macrophage immune response to tumors.

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.

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