| First Author | Zeidan A | Year | 2004 |
| Journal | FEBS Lett | Volume | 562 |
| Issue | 1-3 | Pages | 141-6 |
| PubMed ID | 15044015 | Mgi Jnum | J:88990 |
| Mgi Id | MGI:3037578 | Doi | 10.1016/S0014-5793(04)00220-0 |
| Citation | Zeidan A, et al. (2004) Ablation of SM22alpha decreases contractility and actin contents of mouse vascular smooth muscle. FEBS Lett 562(1-3):141-6 |
| abstractText | The actin-binding protein SM22alpha marks contractile differentiation in smooth muscle, but its function is unknown. We tested its role in arterial contractility and stretch-sensitive vascular protein synthesis. Active stress in depolarised mesenteric resistance arteries and portal veins was reduced by 40% in SM22alpha(-/-) mice. Passive and active arterial circumference-force relationships were shifted leftwards, whereas alpha(1)-adrenergic responses were increased. Actin contents were 10-25% lower in vessels from SM22alpha(-/-) mice, but protein composition was otherwise similar. Synthesis of SM22alpha, calponin and alpha-actin, but not beta-actin, was sensitive to stretch. Ablation of SM22alpha did not affect stretch sensitivity of any of these proteins. Thus, SM22alpha plays a role in contractility, possibly by affecting actin filament organisation. |
