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A full pharmacological analysis of the three turkey ?-adrenoceptors and comparison with the human ?-adrenoceptors.

ABSTRACT: There are three turkey ?-adrenoceptors: the original turkey ?-adrenoceptor from erythrocytes (t?trunc, for which the X-ray crystal structure has recently been determined), t?3C and t?4C-receptors. This study examined the similarities and differences between these avian receptors and mammalian receptors with regards to binding characteristics and functional high and low affinity agonist conformations.Stable cell lines were constructed with each of the turkey ?-adrenoceptors and 3H-CGP12177 whole cell binding, CRE-SPAP production and (3)H-cAMP accumulation assays performed. It was confirmed that the three turkey ?-adrenoceptors are distinct from each other in terms of amino acid sequence and binding characteristics. The greatest similarity of any of the turkey ?-adrenoceptors to human ?-adrenoceptors is between the turkey ?3C-receptor and the human ?2-adrenoceptor. There are pharmacologically distinct differences between the binding of ligands for the t?trunc and t?4C and the human ?-adrenoceptors (e.g. with CGP20712A and ICI118551). The t?trunc and t?4C-adrenoceptors appear to exist in at least two different agonist conformations in a similar manner to that seen at both the human and rat ?1-adrenoceptor and human ?3-adrenoceptors. The t?3C-receptor, similar to the human ?2-adrenoceptor, does not, at least so far, appear to exist in more than one agonist conformation.There are several similarities, but also several important differences, between the recently crystallised turkey ?-adrenoceptor and the human ?-adrenoceptors. These findings are important for those the field of drug discovery using the recently structural information from crystallised receptors to aid drug design. Furthermore, comparison of the amino-acid sequence for the turkey and human adrenoceptors may therefore shed more light on the residues involved in the existence of the secondary ?-adrenoceptor conformation.

SUBMITTER: Baker JG

PROVIDER: S-EPMC2994877 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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A full pharmacological analysis of the three turkey β-adrenoceptors and comparison with the human β-adrenoceptors.

Baker Jillian G JG

PloS one 20101130 11

<h4>Background</h4>There are three turkey β-adrenoceptors: the original turkey β-adrenoceptor from erythrocytes (tβtrunc, for which the X-ray crystal structure has recently been determined), tβ3C and tβ4C-receptors. This study examined the similarities and differences between these avian receptors and mammalian receptors with regards to binding characteristics and functional high and low affinity agonist conformations.<h4>Methodology/principal findings</h4>Stable cell lines were constructed with ...[more]

PMID: 21152092

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Project description:BACKGROUND:Eggshell mineralization in commercially important species such as chicken, turkey or quail is of interest as a general model of calcium carbonate biomineralization. Knowledge of proteins and molecular mechanisms in eggshell assembly may also pave the way to manipulation of thickness of the calcified layer or other features. Comparison of eggshell matrix proteomes of different species may contribute to a better understanding of the mineralization process. The recent publication of the quail genome sequence now enables the proteomic analysis of the quail shell matrix and this comparison with those of chicken and turkey. RESULTS:The quail eggshell proteome comprised 622 identified proteins, 311 of which were shared with chicken and turkey eggshell proteomes. Forty-eight major proteins (iBAQ-derived abundance higher than 0.1 % of total identified proteome) together covered 94 % of total proteome mass. Fifteen of these are also among the most abundant proteins in chicken and turkey eggshell matrix. Only three proteins with a percentage higher than 1.0 % of the total had not previously been identified as eggshell matrix proteins. These were an uncharacterized member of the latexin family, an uncharacterized protease inhibitor containing a Kunitz domain, and gastric intrinsic factor. The most abundant proteins were ovocleidin-116, ovalbumin and ovocalyxin-36 representing approximately 31, 13 and 8 % of the total identified proteome, respectively. The major phosphoproteins were ovocleidin-116 and osteopontin. While osteopontin phosphorylation sites were predominantly conserved between chicken and quail sequences, conservation was less in ovocleidin-116. CONCLUSIONS:Ovocleidin-116 and ovocalyxin-36 are among the most abundant eggshell matrix proteins in all three species of the family Phasianidae analyzed so far, indicating that their presently unknown function is essential for eggshell mineralization. Evidence for other chicken eggshell-specific proteins in quail was inconclusive. Therefore measurement of additional eggshell proteomes, especially from species of different families and preferentially from outside the order Galliformes, will be necessary.

Dataset Information

A full pharmacological analysis of the three turkey ?-adrenoceptors and comparison with the human ?-adrenoceptors.

Publications

A full pharmacological analysis of the three turkey β-adrenoceptors and comparison with the human β-adrenoceptors.

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