Cytokine production by peripheral blood cells in postmenopausal osteoporosis

1991 ◽  
Vol 14 (2) ◽  
pp. 161-167 ◽  
Author(s):  
Maria T. Zarrabeitia ◽  
Jose A. Riancho ◽  
Jose A. Amado ◽  
Jose Napal ◽  
Jesus Gonzalez-Macias
Keyword(s):  
Postmenopausal Osteoporosis ◽  
Peripheral Blood ◽  
Blood Cells ◽  
Cytokine Production ◽  
Peripheral Blood Cells

scholarly journals Impact of Short-Term Systemic Hypoxia on Phagocytosis, Cytokine Production, and Transcription Factor Activation in Peripheral Blood Cells

2011 ◽  
Vol 2011 ◽  
pp. 1-9 ◽  
Author(s):  
Michael Fritzenwanger ◽  
Christian Jung ◽  
Bjoern Goebel ◽  
Alexander Lauten ◽  
Hans R. Figulla
Keyword(s):  
Peripheral Blood ◽  
Blood Cells ◽  
Cytokine Production ◽  
Interferon Γ ◽  
Peripheral Blood Cells ◽  
Immune Functions ◽  
Cellular Functions ◽  
Short Term ◽  
Transcription Factor Activation ◽  
Systemic Hypoxia

Hypoxia frequently associated with certain physiologic and pathologic conditions influences numerous cellular functions. Because the effects of short-term hypoxia are incompletely understood, we examined phagocytosis and cytokine production as well as the activation of the transcription factors HIF-1 and NFκB in peripheral blood cells of healthy volunteers exposed to an oxygen concentration equivalent to that found at a height of 5500 m. Furthermore, we analysed plasma HIF-1 and serum concentrations of various HIF-1-dependent genes. Results showed that short-term hypoxia increased phagocytosis in neutrophils without affecting monocyte phagocytosis. Hypoxia decreased basal TNFα concentration in monocytes and basal interferon γ concentration in CD4+T lymphocytes. In contrast, plasma HIF and serum VEGF concentrations were not affected by hypoxia, although serum EPO concentration was raised. In PBMC, hypoxia increased cytosolic HIF-1 concentration without affecting nuclear HIF-1 concentration and led to a rise in the nuclear NFκB in PBMC. Our results show that short-term hypoxia affects immune functions in healthy individuals. Furthermore, we speculate that the effects of hypoxia are not due to HIF-1, but are caused by the activation of NFκB .

On the combined effect of statins and lycopene on cytokine production by human peripheral blood cells

2010 ◽  
Vol 25 (5) ◽  
pp. 426-431 ◽  
Author(s):  
Michael Bergman ◽  
Meir Djaldetti ◽  
Hertzel Salman ◽  
Hanna Bessler
Keyword(s):  
Peripheral Blood ◽  
Blood Cells ◽  
Cytokine Production ◽  
Human Peripheral Blood ◽  
Combined Effect ◽  
Peripheral Blood Cells

Nicotine modulates cytokine production by Chlamydia pneumoniae infected human peripheral blood cells

2005 ◽  
Vol 5 (4) ◽  
pp. 749-756 ◽  
Author(s):  
Yukimitsu Mamata ◽  
Amal Hakki ◽  
Yoshimasa Yamamoto ◽  
Catherine Newton ◽  
Thomas W. Klein ◽  
...  
Keyword(s):  
Peripheral Blood ◽  
Blood Cells ◽  
Chlamydia Pneumoniae ◽  
Cytokine Production ◽  
Human Peripheral Blood ◽  
Peripheral Blood Cells

Receptor Mediated Binding of the Fibrinolytic Components, Plasminogen and Urokinase, to Peripheral Blood Cells

1987 ◽  
Vol 58 (03) ◽  
pp. 936-942 ◽  
Author(s):  
Lindsey A Miles ◽  
Edward F Plow
Keyword(s):  
T Cells ◽  
B Cell ◽  
Peripheral Blood ◽  
Binding Sites ◽  
Blood Cells ◽  
High Capacity ◽  
Red Cells ◽  
Peripheral Blood Cells ◽  
Cellular Functions ◽  
Fibrinolytic Proteins

SummaryGlu-plasminogen binds to platelets; the monocytoid line, U937, and the human fetal fibroblast line, GM1380 bind both plasminogen and its activator, urokinase. This study assesses the interaction of these fibrinolytic proteins with circulating human blood cells. Plasminogen bound minimally to red cells but bound saturably and reversibly to monocytes, granulocytes and lymphocytes with apparent Kd values of 0.9-1.4 μM. The interactions were of high capacity with 1.6 to 49 × 105 sites/cell and involved the lysine binding sites of plasminogen. Both T cells and non-rosetting lymphocytes and two B cell lines saturably bound plasminogen. Urokinase bound saturably to gianulocytes, monocytes, non-rosetting lymphocytes and a B cell line, but minimally to T cells, platelets and red cells. Therefore, plasminogen binding sites of high capacity, of similar affinities, and with common recognition specificities are expressed by many peripheral blood cells. Urokinase receptors are also widely distributed, but less so than plasminogen binding sites. The binding ol plasminogen and/ or urokinase to these cells may lead to generation of cell- associated proteolytic activity which contributes to a variety of cellular functions.

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