Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 410 (1987), S. 304-312 
    ISSN: 1432-2013
    Keywords: Myosin phosphatase ; Smooth muscle ; Skinned fibers ; Ca2+ and contractility ; Myosin light chain phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The influence of a purified holoenzyme form of polycation-modulable (PCM-) myosin phosphatase on Ca2+-dependent actin-myosin interactions was studied in detergent-skinned smooth muscle fibers from chicken gizzard. The concentration of Ca2+ required for half maximal isometric contraction (A0.5; 0.26 μM) of fibers incubated in the absence of phosphatase was increased 2-fold when PCM-phosphatase (13 U/ml) was included in the medium. Removal of the phosphatase restored A0.5 to control level showing that the enzyme-mediated decrease in Ca2+-sensitivity was reversible. Two-dimensional electrophoresis of fiber homogenates revealed that PCM-phosphatase decreased Ca2+-sensitivity for phosphorylation of the regulatory myosin light chains in parallel fashion. Ca2+-dependent increases in isometric force were directly correlated to increases in the extent of light chain phosphorylation up to about 0.35 mol PO4/mol light chain; further increases in phosphorylation were not associated with further increases in force. Addition of PCM-phosphatase to fibers which had been contracted with a suboptimal concentration of Ca2+ (0.35 μM) resulted in rapid relaxation. Unloaded shortening velocity, reflecting cross-bridge cycling rate, was reduced by 92% in the presence of PCM-phosphatase and light chain phosphorylation was decreased by 50%. These data show that both tension and unloaded shortening velocity may be related to Ca2+-dependent phosphorylation of the light chains. The results indicate that the level of phosphorylation attained in the fiber preparations studied probably reflects the ratio of myosin kinase to phosphatase activities. Since protein phosphatases are regulated enzymes the results also suggest that modulation of phosphatase activity may participate in control of smooth muscle contractility.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1432-2013
    Keywords: Myocardial ischaemia ; Myocardium ; Vascular smooth muscle ; Dog ; Contractile proteins ; Calcium dependence ; Myosin phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The influence of prolonged ischaemia on the regulation of contraction in the myocardium and in the smooth muscle of coronary arteries was investigated. Chemically skinned preparations were used which enabled the contraction to be studied with the environment of the contractile filaments controlled. Myocardial ischaemia was produced in anaesthetized adult beagle dogs by occlusion of the left anterior descending artery for 3 h and followed by 30 min reperfusion. Myocardial tissue and segments from coronary arteries were obtained from the ischaemic infarcted wall region (“in vivo ischaemic”) and compared with control preparations from perfused coronary arteries and from the free wall of the left ventricle. Coronary and myocardial preparations were also obtained from the heart after a 3 h period in vitro under anoxic conditions at 37°C (“in vitro ischaemic”) simulating a state of extreme ischaemia. Control myocardial fibres were fully relaxed at pCa (-log-[Ca2+]) 9 and developed 24±5% (n=7) of maximum force at intermediate calcium concentration (pCa 5.5). In contrast, the in vivo and in vitro ischaemic preparations produced force at pCa 9 (28±13 and 39±8%, respectively, n=5 and 7) and showed an increased force development at pCa 5.5 (53±11 and 75±5%). The in vivo and in vitro ischaemic coronary arteries relaxed more slowly following calcium removal than control vessels. The in vitro ischaemic vascular preparations developed active force at pCa 9 and showed increased levels of myosin light chain phosphorylation and reduced phosphatase activity. This suggests a reduced rate of dephosphorylation as a cause for the changes in contracile behaviour of the smooth muscle. In conclusion, extreme ischaemia in vitro is associated with a loss of calcium regulation and an increased calcium sensitivity of the contractile system in myocardium and changes in the phosphorylation/dephosphorylation reactions of coronary arteries. The changes in myocardium appear to occur also during ischaemia in vivo, and might contribute to contracture development in cells under conditions when adenosine triphosphate synthesis is reestablished after reperfusion.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...