Cough is one of the most important defensive reflexes. However, extensive non- productive cough is a harmful mechanism leading to the damage of human airways. Cough is initiated by activation of vagal afferents in the airways. The site of their convergence is particularly the nucleus of the solitary tract (nTS). The second-order neurons terminate in the pons, medulla and spinal cord and there is also the cortical and subcortical control of coughing.Upper airway cough syndrome (UACS) - previously postnasal drip syndrome - is one of the most common causes of chronic cough together with asthma and gastroesophageal reflux. The main mechanisms leading to cough in patients with nasal and sinus diseases are postnasal drip, direct irritation of nasal mucosa, inflammation in the lower airways, upper airway inflammation and the cough reflex sensitization. The cough demonstrated by UACS patients is probably due to hypersensitivity of the upper airways sensory nerve or lower airways sensory nerve, or a combination of both. Further studies are needed to clarify this mechanism.

• MeSH
• chronická nemoc MeSH
• kapsaicin škodlivé účinky   MeSH
• kašel chemicky indukované   patofyziologie   MeSH
• kationtové kanály TRPV agonisté   fyziologie   MeSH
• kationtový kanál TRPA1 agonisté   fyziologie   MeSH
• lidé MeSH
• nervové receptory účinky léků   fyziologie   MeSH
• nervus vagus účinky léků   patofyziologie   MeSH
• nosní sliznice účinky léků   patofyziologie   MeSH
• syndrom MeSH
• trachea účinky léků   patofyziologie   MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• přehledy MeSH
• Názvy látek
• kapsaicin MeSH
• kationtové kanály TRPV MeSH
• kationtový kanál TRPA1 MeSH
• TRPA1 protein, human MeSH Prohlížeč
• TRPV1 protein, human MeSH Prohlížeč

BACKGROUND/AIM: We report the incorporation of prospective anticancer agent hypericin into DNA and bovine serum albumin (BSA), respectively, with emphasis on comparison of the differences in interaction mode between hypericin and its model compound emodin. MATERIALS AND METHODS: Spectrophotometric methods were used for determination of the binding constants of the drug complex with biomacromolecules. Differential scanning calorimetry was applied for evaluation of drug-macromolecule complex thermal stability. RESULTS: The strength of interaction expressed by binding constants was found to be 4.0×104 l/mol for hypericin-DNA and 8.1×104 l/mol for emodin-DNA complex. Both molecules stabilize bovine serum albumin macromolecule and bind into the hydrophobic cavity in IIA subunit but their localization within the molecule is different. CONCLUSION: Anticancer agent hypericin and its derivative emodin interact with DNA with medium strength and are probably incorporated into the groove of DNA by hydrogen bonds. Bovine serum albumin can serve as a transport protein for hypericin since the binding force between both molecules is adequate.

• Klíčová slova
• DNA, Hypericin, emodin, interaction, serum albumins, thermal stability,
• MeSH
• anthraceny MeSH
• DNA chemie   metabolismus   MeSH
• emodin chemie   farmakologie   MeSH
• molekulární struktura MeSH
• perylen analogy a deriváty   chemie   farmakologie   MeSH
• protinádorové látky chemie   farmakologie   MeSH
• sérový albumin hovězí chemie   metabolismus   MeSH
• spektrální analýza MeSH
• termodynamika MeSH
• vazba proteinů MeSH
• vztahy mezi strukturou a aktivitou MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• anthraceny MeSH
• DNA MeSH
• emodin MeSH
• hypericin MeSH Prohlížeč
• perylen MeSH
• protinádorové látky MeSH
• sérový albumin hovězí MeSH