Ablation of SM22α decreases contractility and actin contents of mouse vascular smooth muscle

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• 作者：Zeidan ; Asad ; Swä ; rd ; Karl ; Nordstr&ouml ; m ; Ina ; Ekblad ; Eva ; Zhang ; Janet C.L. ; Parmacek ; Michael S. ; et. al.
• 关键词：Actin ; Calponin ; Stretch ; Differentiation ; Resistance artery ; Portal vein
• 刊名：FEBS Letters
• 出版年：2004
• 出版时间：March 26, 2004
• 年：2004
• 卷：562
• 期：1-3
• 页码：141-146
• 全文大小：336 K

文摘

The actin-binding protein SM22α 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 SM22α^−/− mice. Passive and active arterial circumference–force relationships were shifted leftwards, whereas α₁-adrenergic responses were increased. Actin contents were 10–25 % lower in vessels from SM22α^−/− mice, but protein composition was otherwise similar. Synthesis of SM22α, calponin and α-actin, but not β-actin, was sensitive to stretch. Ablation of SM22α did not affect stretch sensitivity of any of these proteins. Thus, SM22α plays a role in contractility, possibly by affecting actin filament organisation.