Publications by authors named "V J Wesley"

Neuropathic pain (NP) affects approximately 4 million people in the United States with spinal cord injury (SCI) being a common cause. Matrix metalloproteinases (MMPs) play an integral role in mediating inflammatory responses, cellular signaling, cell migration, extracellular matrix degradation and tissue remodeling and repair. As such, they are major components in the pathogenesis of secondary injury within the central nervous system.

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GPCRs (G-protein-coupled receptors) are a large family of structurally related proteins which mediate their effects by coupling to G-proteins. The V(1a)R (V(1a) vasopressin receptor) is a member of a family of related GPCRs that are activated by vasopressin {AVP ([Arg(8)]vasopressin)}, OT (oxytocin) and related peptides. These receptors are members of a subfamily of Family A GPCRs called the neurohypophysial peptide hormone receptor family.

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Brenda King conducted an audit to identify how many patients do not have adequate footwear as a consequence of wearing bandages and dressings on their feet and legs, and discusses the impact this has on quality of life.

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It is fundamentally important to define how agonist-receptor interaction differs from antagonist-receptor interaction. The V1a vasopressin receptor (V1aR) is a member of the neurohypophysial hormone subfamily of G protein-coupled receptors. Using alanine-scanning mutagenesis of the N-terminal juxtamembrane segment of the V1aR, we now establish that Glu54 (1.

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Article Synopsis
  • Understanding the differences between agonist and antagonist interactions with receptors is crucial for cell signaling, specifically with the V1a vasopressin receptor (V1aR), which is activated by vasopressin hormone.
  • Research shows that an arginyl residue at the N-terminus of V1aR is essential for high-affinity binding of agonists, while not affecting antagonist binding, making it a key player in receptor activation.
  • Mutant experiments reveal that while substitutions at this arginyl site reduce agonist affinity and signaling, they increase the likelihood of receptor activation upon agonist binding, indicating that the arginyl constrains the receptor's inactive form until activated by a hormone like AVP.
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