Malondialdehyde–acetaldehyde-adducted bovine serum albumin activates protein kinase C and stimulates interleukin-8 release in bovine bronchial epithelial cells

Alcohol ◽  
2001 ◽  
Vol 25 (3) ◽  
pp. 159-166 ◽  
Author(s):  
Todd A. Wyatt ◽  
Kusum K. Kharbanda ◽  
Dean J. Tuma ◽  
Joseph H. Sisson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Bronchial Epithelial Cells ◽  
Interleukin 8 ◽  
Bronchial Epithelial ◽  
Kinase C

scholarly journals Adducin Promotes Micrometer-Scale Organization of β2-Spectrin in Lateral Membranes of Bronchial Epithelial Cells

2008 ◽  
Vol 19 (2) ◽  
pp. 536-545 ◽  
Author(s):  
Khadar M. Abdi ◽  
Vann Bennett
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Rho Kinase ◽  
Bronchial Epithelial Cells ◽  
Bronchial Epithelial ◽  
Lateral Membrane ◽  
Kinase C ◽  
Reduced Height ◽  
Interfering Rna

Adducin promotes assembly of spectrin–actin complexes, and is a target for regulation by calmodulin, protein kinase C, and rho kinase. We demonstrate here that adducin is required to stabilize preformed lateral membranes of human bronchial epithelial (HBE) cells through interaction with β2-spectrin. We use a Tet-on regulated inducible small interfering RNA (siRNA) system to deplete α-adducin from confluent HBE cells. Depletion of α-adducin resulted in increased detergent solubility of spectrin after normal membrane biogenesis during mitosis. Conversely, depletion of β2-spectrin resulted in loss of adducin from the lateral membrane. siRNA–resistant α-adducin prevented loss of lateral membrane, but only if α-adducin retained the MARCKS domain that mediates spectrin–actin interactions. Phospho-mimetic versions of adducin with S/D substitutions at protein kinase C phosphorylation sites in the MARCKS domain were not active in rescue. We find that adducin modulates long-range organization of the lateral membrane based on several criteria. First, the lateral membrane of adducin-depleted cells exhibited reduced height, increased curvature, and expansion into the basal surface. Moreover, E-cadherin-GFP, which normally is restricted in lateral mobility, rapidly diffuses over distances up to 10 μm. We conclude that adducin acting through spectrin provides a novel mechanism to regulate global properties of the lateral membrane of bronchial epithelial cells.

scholarly journals Protein Kinase C-α Activity Is Required for Respiratory Syncytial Virus Fusion to Human Bronchial Epithelial Cells

2004 ◽  
Vol 78 (24) ◽  
pp. 13717-13726 ◽  
Author(s):  
Homero San-Juan-Vergara ◽  
Mark E. Peeples ◽  
Richard F. Lockey ◽  
Shyam S. Mohapatra
Keyword(s):  
Protein Kinase C ◽  
Respiratory Syncytial Virus ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Bronchial Epithelial Cells ◽  
Human Bronchial Epithelial Cells ◽  
Bronchial Epithelial ◽  
Kinase C ◽  
Rsv Infection ◽  
Syncytial Virus

ABSTRACT Respiratory syncytial virus (RSV) infection activates protein kinase C (PKC), but the precise PKC isoform(s) involved and its role(s) remain to be elucidated. On the basis of the activation kinetics of different signaling pathways and the effect of various PKC inhibitors, it was reasoned that PKC activation is important in the early stages of RSV infection, especially RSV fusion and/or replication. Herein, the role of PKC-α during the early stages of RSV infection in normal human bronchial epithelial cells is determined. The results show that the blocking of PKC-α activation by classical inhibitors, pseudosubstrate peptides, or the overexpression of dominant-negative mutants of PKC-α in these cells leads to significantly decreased RSV infection. RSV induces phosphorylation, activation, and cytoplasm-to-membrane translocation of PKC-α. Also, PKC-α colocalizes with virus particles and is required for RSV fusion to the cell membrane. Thus, PKC-α could provide a new pharmacological target for controlling RSV infection.

Protein kinase C activity during the process of lung liquid clearance

1993 ◽  
Vol 265 (1) ◽  
pp. L57-L66 ◽  
Author(s):  
M. Sapijaszko ◽  
J. Mackenzie ◽  
M. P. Walsh ◽  
Y. Berthiaume
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Inflammatory Cells ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Heterologous Serum ◽  
Lung Liquid

Although active transport of sodium plays an important role in the resolution of pulmonary edema, the biochemical regulation of this process is still under investigation. The purpose of this study was to evaluate the activity of protein kinase C during the process of lung liquid clearance. Alveolar flooding was induced by instilling 5% bovine serum albumin solution, saline, or heterologous serum in the air spaces of rats. The activity of protein kinase C was measured in both the instilled and control lungs at 10 min and 1 and 4 h after fluid instillation. Four hours after instillation of 5% bovine serum albumin, the ratio of protein kinase C activity in the instilled lung compared with the control lung was 2.2 +/- 0.3. Similar results were obtained following instillation with heterologous serum or saline. Since we measured a clearance rate of 0.8 ml/h in anesthetized rats, we can postulate that the activation of protein kinase C occurred when > 40% of the liquid had been cleared from the lung. This increased activity of protein kinase C was not due to an increase in kinase activity in the inflammatory cells or an increase in enzyme quantity but due to a decrease of protein kinase C inhibitory activity in the lung. These results suggest that protein kinase C second messenger system may play a regulatory role in lung liquid clearance.

Stimulation of protein kinase C activity by tumor necrosis factor-α in bovine bronchial epithelial cells

1997 ◽  
Vol 273 (5) ◽  
pp. L1007-L1012 ◽  
Author(s):  
Todd A. Wyatt ◽  
Harumasa Ito ◽  
Thomas J. Veys ◽  
John R. Spurzem
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tumor Necrosis Factor ◽  
Epithelial Cells ◽  
Tumor Necrosis ◽  
Bronchial Epithelial ◽  
Calphostin C ◽  
Kinase C ◽  
Tnf Α ◽  
Necrosis Factor

Bronchial epithelial cell migration, attachment, and proliferation are important processes in response to airway injury. We have shown that tumor necrosis factor (TNF)-α stimulates the migration of bovine bronchial epithelial cells (BBEC) in vitro. We hypothesized that protein kinase C (PKC) may be one of the intracellular signaling mediators of TNF-α in BBEC. In this study, we have identified multiple PKC isoforms in BBEC and measured total cellular PKC activity. Polyclonal antibodies to the PKC-α, -β2, -δ, and -ε isoforms recognized protein bands around 80–90 kDa. BBEC primary cultures treated with either 500 U/ml TNF-α for 2–4 h or 100 ng/ml 12- O-tetradecanoylphorbol 13-acetate for 15 min resulted in three- to fivefold increases in PKC activity in the particulate fractions of crude cell lysates. This activity was inhibited by 1 μM calphostin C or 10 μM H-7. Similarly, TNF-α-stimulated BBEC migration was reduced at least twofold in the presence of H-7 or calphostin C. These studies suggest that the activation of PKC is necessary for TNF-α-stimulated BBEC migration.

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