摘要：

The role of the membrane protein caveolin-1 (a component of caveolae) in the localization of the glycolytic enzyme phosphofructokinase (PFK) to the plasma membrane was previously described in smooth and skeletal muscle. Glial cells which remove glutamate from the synapse and play a critical role in the metabolic support of neurons represent an excellent model for investigating the organizational role of scaffold protein caveolin-1 (CAV-1) for glycolytic enzymes. We sought to determine whether CAV-1 localizes with glycolytic enzymes pyruvate kinase (PK), and phosphofructokinase (PFK), and whether the glucose transporter GLUT-1 is also found with CAV-1 in the isolated pig retinal cells. Using confocal immunofluourescence microscopy we measured colocalization PK, and PFK with CAV-1. We also measured the distribution of GLUT-1 with CAV-1. We find that there is high colocalization between PK and PFK with CAV-1 largely close to the plasma membrane in the soma and endfoot region of the isolated retinal Müller cell. We also find a similar distribution between the transporter GLUT-1 with CAV-1 in. the retina muller cells, a characteristic previously observed in culture mouse astrocytes. We think the CAV-1 labeling likely corresponds to caveolar regions that may represent a glycolytic microdomain. Understanding the organization of glycolytic metabolism in the glial cell can help us better understand the dysfunction that occurs to glutamate metabolism during disease. We propose that CAV-1 plays a role in the organization of glycolytic metabolism in the glial cell.

展开