Abstract
Ca2+ is a primary second messenger that binds to an intracellular receptor protein, calmodulin. Increases in cytosolic Ca2+ concentration mediated by activation of cell surface receptors result in the formation of a Ca2+ calmodulin complex that regulates many Ca2+-dependent cellular processes. In smooth muscle, Ca2+/calmodulin activates myosin light chain kinase, which phosphorylates the regulatory light chain of myosin. This phosphorylation reaction increases the actin-activated MgATPase activity of myosin and is associated with increases in contractile properties, including force, stiffness, and maximal shortening velocity. These biochemical and biomechanical responses occur rapidly (seconds) in response to physiological stimulation involving neurotransmitter activation of smooth muscle cells. Thus, the Ca2+-dependent phosphorylation of the myosin light chain is a primary event in activation of smooth muscle contraction.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 241-245 |
| Number of pages | 5 |
| Journal | American Journal of the Medical Sciences |
| Volume | 296 |
| Issue number | 4 |
| State | Published - 1988 |
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ASJC Scopus subject areas
- Medicine(all)
Cite this
Calcium control of smooth muscle contractility. / Stull, J. T.; Kamm, K. E.; Taylor, D. A.
In: American Journal of the Medical Sciences, Vol. 296, No. 4, 1988, p. 241-245.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Calcium control of smooth muscle contractility
AU - Stull, J. T.
AU - Kamm, K. E.
AU - Taylor, D. A.
PY - 1988
Y1 - 1988
N2 - Ca2+ is a primary second messenger that binds to an intracellular receptor protein, calmodulin. Increases in cytosolic Ca2+ concentration mediated by activation of cell surface receptors result in the formation of a Ca2+ calmodulin complex that regulates many Ca2+-dependent cellular processes. In smooth muscle, Ca2+/calmodulin activates myosin light chain kinase, which phosphorylates the regulatory light chain of myosin. This phosphorylation reaction increases the actin-activated MgATPase activity of myosin and is associated with increases in contractile properties, including force, stiffness, and maximal shortening velocity. These biochemical and biomechanical responses occur rapidly (seconds) in response to physiological stimulation involving neurotransmitter activation of smooth muscle cells. Thus, the Ca2+-dependent phosphorylation of the myosin light chain is a primary event in activation of smooth muscle contraction.
AB - Ca2+ is a primary second messenger that binds to an intracellular receptor protein, calmodulin. Increases in cytosolic Ca2+ concentration mediated by activation of cell surface receptors result in the formation of a Ca2+ calmodulin complex that regulates many Ca2+-dependent cellular processes. In smooth muscle, Ca2+/calmodulin activates myosin light chain kinase, which phosphorylates the regulatory light chain of myosin. This phosphorylation reaction increases the actin-activated MgATPase activity of myosin and is associated with increases in contractile properties, including force, stiffness, and maximal shortening velocity. These biochemical and biomechanical responses occur rapidly (seconds) in response to physiological stimulation involving neurotransmitter activation of smooth muscle cells. Thus, the Ca2+-dependent phosphorylation of the myosin light chain is a primary event in activation of smooth muscle contraction.
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UR - http://www.scopus.com/inward/citedby.url?scp=0023815476&partnerID=8YFLogxK
M3 - Article
C2 - 2973750
AN - SCOPUS:0023815476
VL - 296
SP - 241
EP - 245
JO - The American journal of the medical sciences
JF - The American journal of the medical sciences
SN - 0002-9629
IS - 4
ER -