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Open Access Research article

Functional characterization and evolution of PTH/PTHrP receptors: insights from the chicken

Pedro LC Pinheiro, João CR Cardoso*, Deborah M Power and Adelino V M Canário

Author Affiliations

Centre of Marine Sciences, Comparative Molecular Endocrinology, Universidade do Algarve, Campus de Gambelas, 8005-139, Faro, Portugal

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BMC Evolutionary Biology 2012, 12:110  doi:10.1186/1471-2148-12-110

Published: 6 July 2012

Additional files

Additional file 1:

Nucleotide and deduced amino acid sequence of the chicken PTH1R. Deduced sequence for PTH1R is based upon EST data and PCR amplification. Primer localization is represented by horizontal arrows and the exons change by vertical arrows. The TM domains are represented by bound lines and signal peptide in italic and bold. Cysteine residues are circled and putative N-glycosylation sites are boxed.

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Open Data

Additional file 2:

Nucleotide and deduced amino acid sequence of the chicken PTH3R. Sequence deduced based upon EST data and PCR amplification. Primer localization is represented by horizontal arrows and the exons change by vertical arrows. The TM domains are represented by bound lines and signal peptide by in italic and bold. Cysteine residues are circles and putative N-glycosylation sites are boxed.

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Open Data

Additional file 3:

Comparison of the vertebrate TIP39 and PTH gene environments. Only homologue genes are represented with the exception of the zebrafish TIP39 gene environment to demonstrate the lack of gene synteny with other vertebrate homologue regions. Dashed boxes represent putative gene locus in lamprey.

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Open Data

Additional file 4:

Accumulation of cAMP in HEK293 cells transfected with chicken PTH1R and PTH3R. Human PTH and TIP39 peptides were used at 10 nM and 100 nM. Values represent means ± SEM of a single experiment carried out in triplicate.

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Open Data