Protein Kinase C-Mediated Regulation of Matrix Metalloproteinase and Tissue Inhibitor of Metalloproteinase Production in a Human Retinal Müller Cells

2012 ◽  
Vol 37 (9) ◽  
pp. 842-849 ◽  
Author(s):  
Yoshiki Miyata ◽  
Miho Kase ◽  
Yuko Sugita ◽  
Arata Shimada ◽  
Terumasa Nagase ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Matrix Metalloproteinase ◽  
Müller Cells ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Muller Cells ◽  
Tissue Inhibitor ◽  
Kinase C

Two types of mitochondria are evidenced by protein kinase C immunoreactivity in the Müller cells of the carp retina

1995 ◽  
Vol 183 (3) ◽  
pp. 202-205 ◽  
Author(s):  
Eduardo Fernández ◽  
Nicolás Cuenca ◽  
Magdalena García ◽  
Joaquín De Juan
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Müller Cells ◽  
Muller Cells ◽  
Kinase C

Activation of protein kinase C reduces GLAST in the plasma membrane of rat Müller cells in primary culture

2003 ◽  
Vol 20 (6) ◽  
pp. 611-619 ◽  
Author(s):  
ZHIQING WANG ◽  
WEI LI ◽  
CHERYL K. MITCHELL ◽  
LOUVENIA CARTER-DAWSON
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Glutamate Uptake ◽  
Müller Cells ◽  
Glutamate Transport ◽  
Cell Surface Expression ◽  
Muller Cells ◽  
Transport Activity ◽  
Kinase C

In this study, a Müller cell culture preparation from young rats was used to investigate the regulation of GLAST transport activity in native cells. Immunohistochemical analysis confirmed GLAST to be the predominant glutamate transporter expressed by the cells through five passages. [3H]-glutamate uptake assays showed the typical Na+-dependent glutamate transport which was blocked by L-(-)-threo-3-hydroxyaspartate (L-THA), a competitive inhibitor. Glutamate transport was decreased significantly in Müller cells exposed to phorbol-12-myristate-13-acetate (PMA), a protein kinase C (PKC) activator. A similar effect on [3H]-D-aspartate (nonmetabolizable glutamate analog) uptake ruled out the possibility that the decrease was a consequence of altered metabolism. However, PMA did not affect Na+-dependent [3H]-glycine transport, indicating the absence of a nonspecific change in the electrochemical gradients. The PMA effect on glutamate uptake was evidenced by partial blocking with a specific PKC inhibitor, bisindolymaleimide II (Bis II). Activation of PKC did not change the Km, but the Vmax was significantly reduced. Image analysis of Müller cells with biotinylated cell membranes immunolabeled with GLAST shows a reduction of GLAST in the plasma membrane. In conclusion, these data show that rat Müller cells in primary cultures express GLAST and that PKC activation affects GLAST transport activity by decreasing cell surface expression.

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