Tonic arterial smooth muscle can produce strong contractions indefinitely by formation of slowly cycling crossbridges (latchbridges) that maintain force at a high energy economy. To fully understand the uniqueness of mechanisms regulating tonic arterial contraction, comparisons have been made to phasic visceral smooth muscles that do not sustain high forces. This study explored mechanisms of force maintenance in a phasic artery by comparing KCl-induced contractions in the tonic, femoral artery (FA) and its primary branch, the phasic saphenous artery (SA). KCl rapidly (5 N/m2) and [ca2+]i (250 nM) in FA and SA. By 10 min, [ca2+]i declined to 175 nM in both tissues but stress was sustained in FA (1.3 x 105N/m2) and reduced by 40% in SA (0.8 x l05 N/m2). Reduced tonic stress correlated with reduced myosin light chain (MLC) phosphorylation in SA (28% vs. 42% in FA). SA expressed more MLC phosphatase than FA, and permeabilized (β-escin) SA relaxed more rapidly than FA in the presence of MLC kinase blockade, suggesting that MLC phosphatase activity in SA was greater than that in FA. The reduction in MLC phosphorylation in SA was insufficient to account for reduced tonic force (latchbridge model), and SA expressed more "fast" myosin isoforms than did FA. Cytochalasin-D reduced force-maintenance more in FA than SA. These data support the hypothesis that strong force-maintenance is absent in SA because expressed motor proteins do not support latchbridge formation, and because actin polymerization is not stimulated.