Acute and Chronic Cough (Lung Biology in Health and Disease, by Anthony E. Redington, Alyn H. Morice

By Anthony E. Redington, Alyn H. Morice

A entire assessment of the clinical and medical elements of acute and persistent cough, this reference makes a speciality of contemporary advancements in our knowing of the molecular biology of putative cough receptors, the neural mechanisms focused on the afferent and efferent limbs, the vital processing of the cough reflex, and peptides and different elements which may mediate or modulate the cough reflex. With chapters wriitenby said specialists within the box, this guide covers present and strength healing brokers, a number of methodologies to degree cough reflex sensitivity, and scientific techniques for the review of continual cough in adults and kids.

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Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor. Cell 2000; 103:525–535. 42. Hoenderop JG, van der Kemp AW, Hartog A, van de Graaf SF, van Os CH, Willems PH, Bindels RJ. Molecular identification of the apical Ca2þ channel in 1, 25-dihydroxyvitamin D3-responsive epithelia. J Biol Chem 1999; 274:8375–8378. 43. Peng JB, Chen XZ, Berger UV, Vassilev PM, Tsukaguchi H, Brown EM, Hediger MA. Molecular cloning and characterization of a channel-like transporter mediating intestinal calcium absorption.

Temperature-specific sensing domains of TRPV1 have not yet been identified, although the most basic role of the channel is in fact probably the detection of noxious heat. Phosphorylation Phosphorylation is involved in the downstream signaling cascades of typical inflammatory airway diseases (7), and several lines of evidence suggest that this is the most important mechanism of TRPV1 modulation. Among putative candidates, modification of two protein kinase C (PKC) substrates (S502 between TM2 and TM3, S800 in the C-terminal domain) and two protein kinase A (PKA) substrates (S116 on the intracellular N-terminal tail, S502 between TM2 and TM3) has produced the most significant changes in TRPV1 activity (54–56).

It has been reported that four subunits of TRPV1 can associate to form a tetrameric complex (45,46), but there is no evidence of heteromultimer formation with other TRPVs. Sensor Domains Two groups have investigated capsaicin binding by TRPV1 and unexpectedly found that amino acid residues of the binding site are present on the intracellular side of the channel (47,48). Although the essential sequences reported in these studies were not identical, these results strongly suggest the presence of endogenous capsaicin-like ligands in the cytosol of sensory neurons, and indeed several promising candidates have now been identified (see later).

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