Multicenter clinical trials on a novel polyherbal formulation in allergic rhinitis.

Allergic rhinitis is the most frequently occurring immunological disorder. It affects men, women and children and represents significant cost in terms of suffering and loss of productivity. Allergy is termed as an excessive reaction to an environmental allergen.

Identification of the adenine binding site of the human A1 adenosine receptor.

To provide new insights into ligand-A1 adenosine receptor (A1AR) interactions, site-directed mutagenesis was used to test the role of several residues in the first four transmembrane domains of the human A1AR. First, we replaced eight unique A1AR residues with amino acids present at corresponding transmembrane (TM) positions of A2AARs. We also tested the role of carboxamide amino acids in TMs 1-4, and the roles of Val-87, Leu-88, and Thr-91 in TM3.

Site-directed mutagenesis of the human A1 adenosine receptor: influences of acidic and hydroxy residues in the first four transmembrane domains on ligand binding.

To provide new insights into ligand/A1 adenosine receptor (A1 AR) interactions, site-directed mutagenesis was used to test the role of several residues in the first four transmembrane (TM) domains of the human A1 AR. Based on multiple sequence analysis of all known ARs, both acidic (glutamic acid and aspartic acid) and polar hydroxy (serine and threonine) amino acids were identified that could potentially play a role in binding adenosine. Glu16 (TM1), Asp55 (TM2), Ser93 and Ser94 (TM3), Ser135 (TM4), and Thr 141 (TM4) were identified in all ARs, and Ser6 and Ser23 (TM1) were identified in all A1 ARs.

Identification of domains of the human A1 adenosine receptor that are important for binding receptor subtype-selective ligands using chimeric A1/A2a adenosine receptors.

To provide new insights into the regions of the human A1 adenosine receptor (A1AR) involved in ligand binding, a series of chimeric human A1 and rat A2a adenosine receptors (A1/A2a) were studied. Binding studies were initially performed on acutely transfected COS cells using fixed doses of the A2aAR agonist [3H]CGS-21680, the A1AR agonist [3H]2-chloro-N6-cyclopentyladenosine (CCPA), and the A1AR antagonist [3H]8-cyclopentyl-1,3-dipropylxanthine (DPCPX). When the region of the A2aAR from the amino terminus to the end of transmembrane (TM) 1 was replaced by the corresponding region of the A1AR (A1TM1/A2a), [3H]CGS-21680 and [3H]CCPA binding was detectable.

Processing of U14 small nucleolar RNA from three different introns of the mouse 70-kDa-cognate-heat-shock-protein pre-messenger RNA.

U14 is a small nucleolar RNA required for the processing of eukaryotic rRNA precursors. The U14 genes of mouse as well as rat, hamster, human, Xenopus and trout are encoded within introns of the constitutively expressed 70-kDa-cognate-heat-shock protein gene (hsc70). We demonstrate here that U14.