Microgravity modifies protein kinase C isoform translocation in the human monocytic cell line U937 and human peripheral blood T-cells

2002 ◽  
Vol 87 (1) ◽  
pp. 39-50 ◽  
Author(s):  
Jason P. Hatton ◽  
Francois Gaubert ◽  
Jean-Pierre Cazenave ◽  
Didier Schmitt
Keyword(s):  
T Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Monocytic Cell ◽  
Monocytic Cell Line ◽  
Human Monocytic Cell Line ◽  
Kinase C ◽  
Human Monocytic Cell

scholarly journals Homocysteine stimulates phosphorylation of NADPH oxidase p47phox and p67phox subunits in monocytes via protein kinase Cβ activation

2006 ◽  
Vol 398 (1) ◽  
pp. 73-82 ◽  
Author(s):  
Yaw L. Siow ◽  
Kathy K. W. Au-Yeung ◽  
Connie W. H. Woo ◽  
Karmin O
Keyword(s):  
Protein Kinase ◽  
Nadph Oxidase ◽  
Superoxide Anion ◽  
Monocytic Cell ◽  
Superoxide Anion Production ◽  
Monocytic Cell Line ◽  
Protein Kinase C Inhibitors ◽  
Human Monocytic Cell Line ◽  
Anion Production ◽  
Human Monocytic Cell

Hyperhomocysteinaemia is an independent risk factor for cardiovascular diseases due to atherosclerosis. The development of atherosclerosis involves reactive oxygen species-induced oxidative stress in vascular cells. Our previous study [Wang and O (2001) Biochem. J. 357, 233–240] demonstrated that Hcy (homocysteine) treatment caused a significant elevation of intracellular superoxide anion, leading to increased expression of chemokine receptor in monocytes. NADPH oxidase is primarily responsible for superoxide anion production in monocytes. In the present study, we investigated the molecular mechanism of Hcy-induced superoxide anion production in monocytes. Hcy treatment (20–100 μM) caused an activation of NADPH oxidase and an increase in the superoxide anion level in monocytes (THP-1, a human monocytic cell line). Transfection of cells with p47phox siRNA (small interfering RNA) abolished Hcy-induced superoxide anion production, indicating the involvement of NADPH oxidase. Hcy treatment resulted in phosphorylation and subsequently membrane translocation of p47phox and p67phox subunits leading to NADPH oxidase activation. Pretreatment of cells with PKC (protein kinase C) inhibitors Ro-32-0432 (bisindolylmaleimide XI hydrochloride) (selective for PKCα, PKCβ and PKCγ) abolished Hcy-induced phosphorylation of p47phox and p67phox subunits in monocytes. Transfection of cells with antisense PKCβ oligonucleotide, but not antisense PKCα oligonucleotide, completely blocked Hcy-induced phosphorylation of p47phox and p67phox subunits as well as superoxide anion production. Pretreatment of cells with LY333531, a PKCβ inhibitor, abolished Hcy-induced superoxide anion production. Taken together, these results indicate that Hcy-stimulated superoxide anion production in monocytes is regulated through PKC-dependent phosphorylation of p47phox and p67phox subunits of NADPH oxidase. Increased superoxide anion production via NADPH oxidase may play an important role in Hcy-induced inflammatory response during atherogenesis.

Cyclosporine inhibits protein kinase C-dependent signals in human peripheral blood lymphocytes

1989 ◽  
Vol 46 (4) ◽  
pp. 292-295 ◽  
Author(s):  
Marvin A. McMillen ◽  
Harold A. Schaefer ◽  
John D. MacArthur ◽  
Thomas A. Adrian ◽  
Irvin M. Modlin
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Peripheral Blood Lymphocytes ◽  
Blood Lymphocytes ◽  
Human Peripheral Blood Lymphocytes ◽  
Kinase C
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