Value of Thermography in the Diagnosis of Malignant Melanomas of the Skin

Cristofolini, Mario; Boi, Sebastiana; Perani, Bruna; Recchia, G; Zumiani, Giuseppe

doi:10.1007/978-1-4684-7697-2_92

Cited by 1 publication

(1 citation statement)

References 2 publications

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“…Although 8-MOP failed to induce a Cl 0 secretory response on its own lieved that this inhibition of DNA synthesis was responsible for the therapeutic effect observed, more recent in the T84 cell line, it both potentiated the Cl 0 secretory effect of the muscarinic agonist carbachol as well as in-evidence has demonstrated that the angelicins also possess therapeutic potential while failing to form the bifunc-duced a sustained plateau phase to the carbachol response. These results are consistent with the activation tional adducts required to inhibit DNA synthesis (80). A second photochemical reaction involves the transfer of of an apical membrane Cl 0 conductance by the psoralens in the absence of any change in basolateral K / conduc-energy to molecular oxygen resulting in reactive oxygen species and free radicals.…”

Section: S132supporting

confidence: 81%

Pharmacology of CFTR Chloride Channel Activity

Schultz

Singh

Devor

et al. 1999

Physiological Reviews

260

251

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Pharmacology of CFTR Chloride Channel Activity. Physiol. Rev. 79, Suppl.: S109-S144, 1999. - The pharmacology of cystic fibrosis transmembrane conductance regulator (CFTR) is at an early stage of development. Here we attempt to review the status of those compounds that modulate the Cl- channel activity of CFTR. Three classes of compounds, the sulfonylureas, the disulfonic stilbenes, and the arylaminobenzoates, have been shown to directly interact with CFTR to cause channel blockade. Kinetic analysis has revealed the sulfonylureas and arylaminobenzoates interact with the open state of CFTR to cause blockade. Suggestive evidence indicates the disulfonic stilbenes act by a similar mechanism but only from the intracellular side of CFTR. Site-directed mutagenesis studies indicate the involvement of specific amino acid residues in the proposed transmembrane segment 6 for disulfonic stilbene blockade and segments 6 and 12 for arylaminobenzoate blockade. Unfortunately, these compounds (sulfonylureas, disulfonic stilbenes, arylaminobenzoate) also act at a number of other cellular sites that can indirectly alter the activity of CFTR or the transepithelial secretion of Cl-. The nonspecificity of these compounds has complicated the interpretation of results from cellular-based experiments. Compounds that increase the activity of CFTR include the alkylxanthines, phosphodiesterase inhibitors, phosphatase inhibitors, isoflavones and flavones, benzimidazolones, and psoralens. Channel activation can arise from the stimulation of the cAMP signal transduction cascade, the inhibition of inactivating enzymes (phosphodiesterases, phosphatases), as well as the direct binding to CFTR. However, in contrast to the compounds that block CFTR, a detailed understanding of how the above compounds increase the activity of CFTR has not yet emerged.

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Section: S132supporting

confidence: 81%