| First Author | Boittin FX | Year | 2006 |
| Journal | J Cell Sci | Volume | 119 |
| Issue | Pt 18 | Pages | 3733-42 |
| PubMed ID | 16926189 | Mgi Jnum | J:113111 |
| Mgi Id | MGI:3664512 | Doi | 10.1242/jcs.03184 |
| Citation | Boittin FX, et al. (2006) Ca2+-independent phospholipase A2 enhances store-operated Ca2+ entry in dystrophic skeletal muscle fibers. J Cell Sci 119(Pt 18):3733-42 |
| abstractText | Duchenne muscular dystrophy is caused by deficiency of dystrophin and leads to progressive weakness. It has been proposed that the muscle degeneration occurring in this disease is caused by increased Ca(2+) influx due to enhanced activity of cationic channels that are activated either by stretch of the plasma membrane (stretch-activated channels) or by Ca(2+)-store depletion (store-operated channels). Using both cytosolic Ca(2+) measurements with Fura-2 and the manganese quench method, we show here that store-operated Ca(2+) entry is greatly enhanced in dystrophic skeletal flexor digitorum brevis fibers isolated from mdx(5cv) mice, a mouse model of Duchenne muscular dystrophy. Moreover, we show for the first time that store-operated Ca(2+) entry in these fibers is under the control of the Ca(2+)-independent phospholipase A(2) and that the exaggerated Ca(2+) influx can be completely attenuated by inhibitors of this enzyme. Enhanced store-operated Ca(2+) entry in dystrophic fibers is likely to be due to a near twofold overexpression of Ca(2+)-independent phospholipase A(2). The Ca(2+)-independent phospholipase A(2) pathway therefore appears as an attractive target to reduce excessive Ca(2+) influx and subsequent degeneration occurring in dystrophic fibers. |
