Anesthesia & Clinical Research
Open Access

Laura Cipp

Publications

• Research Article
  Effect of n-Alkanols on G-Protein a Subunits
  Author(s): Srinivas Pentyala, Kavita Tanguturi, Anas Sawas, Amulya Veerraju, Sandeep Annam, Laura Cipp and Mario Rebecchi Srinivas Pentyala, Kavita Tanguturi, Anas Sawas, Amulya Veerraju, Sandeep Annam, Laura Cipp and Mario Rebecchi
  
  Guanine nucleotide binding (G)-proteins are GTP-driven allosteric proteins consisting of a single ? subunit and a ? and ? heterodimer. G? subunits function as on/off switches based on the occupancy of the nucleotide-binding site, GTP or GDP, such that any alteration in nucleotide exchange modulates signal output. Our previous work has shown that haloalkanes and ethers inhibit GDP/GTP exchange on ?i1, ?i2 and ?i3 subunits, but not the closely related ao. To test whether individual G-protein sensitivity correlates with n-alkanols potency and hydrophobicity, we studied the effects of n-alkanols of varied chain lengths on GDP/GTP exchange by G? subunits. n-alkanols (ethanol, butanol, pentanol, hexanol, heptanol, octanol and nonanol) showed differential effects on guanine nucleotide exchange by G?i1, G?i2 and G?o. Based on our observations, we conclude that n-alkanols interact and modulate.. View More»
  DOI: 10.4172/2155-6148.1000153

  Abstract PDF

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