The Venus bow shock location has been measured at nearly 2000 shock crossings, and its dependence on solar EUV, solar wind conditions, and the interplanetary magnetic field determined. The shock position at the terminator varies from about 2.14 Venus radii at solar minimum to 2.40 Venus radii at solar maximum. The location of the shock varies little with solar wind dynamic pressure but strongly with solar wind Mach number. The shock is farthest from Venus on the side of the planet in which newly created ions gyrate away from the ionosphere. When the interplanetary magnetic field is perpendicular to the flow, the cross section of the shock is quite elliptical.This effect appears to be due to the anisotropic propagation of the fast magnetosonic wave.When the interplanetary magnetic field is aligned with the flow, the bow shock cross section is circular and only weakly sensitive to changing EUV flux.

Sarcospan signals through Akt to increase cell surface levels of utrophin and glycosylated α-dystroglycan and promote muscle repair after injury.

No abstract

Sarcospan (SSPN) is a core component of the major adhesion complexes in skeletal muscle, the dystrophin- and utrophin (Utr)-glycoprotein complexes (DGC and UGC). We performed a rigorous analysis of SSPN-null mice and discovered that loss of SSPN decreased DGC and UGC abundance, leading to impaired laminin-binding activity and susceptibility to eccentric contraction-induced injury in skeletal muscle. We show that loss of SSPN increased levels of α7β1 integrin. To genetically test whether integrin compensates for the loss of DGC and UGC function in SSPN-nulls, we generated mice lacking both SSPN and α7 integrin (DKO, double knockout). Muscle regeneration, sarcolemma integrity and fibrosis were exacerbated in DKO mice and were remarkably similar to muscle from Duchenne muscular dystrophy (DMD) patients, suggesting that secondary loss of integrin contributes significantly to pathogenesis. Expression of the DGC and UGC, laminin binding and Akt signaling were negatively impacted in DKO muscle, resulting in severely diminished specific force properties. We demonstrate that SSPN is a necessary component of dystrophin and Utr function and that SSPN modulation of integrin signaling is required for extracellular matrix attachment and muscle force development.

No abstract