Uterine smooth muscle contraction is determined by the state of myosin (MYL) phosphorylation which is regulated by the calcium dependent myosin light chain kinase (MYLK) and a protein phosphatase called myosin phosphatase. Agonist induced increases in intracellular calcium ([Ca²?]i)activates MYLK which phosphorylates MYL enabling it to bind to actin to cause contraction. Myosin phosphatase is a protein phosphatase that dephosphorylates phosphorylated MYL to induce relaxation. The state of MYL phosphorylation and contraction is therefore determined the equilibrium between MYLK and myosin phosphatase. The mechanisms that regulate these two enzymes in the human uterus remain poorly understood.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:492581 |
| Date | January 2007 |
| Creators | Lartey, Dr Jonathan Paul Akueteh |
| Publisher | University of Bristol |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
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