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Search: WFRF:(Fredriksson P. J.) > (2005-2009) > Origin of the prola...

Origin of the prolactin-releasing hormone (PRLH) receptors : Evidence of coevolution between PRLH and a redundant neuropeptide Y receptor during vertebrate evolution

Lagerström, Malin C. (author)
Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
Fredriksson, Robert (author)
Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
Bjarnadottir, Thora (author)
Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
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Fridmanis, Davids (author)
Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
Holmquist, Tomas (author)
Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
Andersson, Jan (author)
Karolinska Institutet,Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
Yan, Yi-Lin (author)
Raudsepp, Terje (author)
Zoorob, Rima (author)
Kukkonen, Jyrki P. (author)
Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
Lundin, LG (author)
Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
Klovins, J (author)
Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
Chowdhary, BP (author)
Pistlethwait, JH (author)
Schiöth, Helgi (author)
Uppsala universitet,Institutionen för neurovetenskap,Farmakologi 3
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 (creator_code:org_t)
Elsevier BV, 2005
2005
English.
In: Genomics. - : Elsevier BV. - 0888-7543 .- 1089-8646. ; 85:6, s. 688-703
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  • Journal article (peer-reviewed)
Abstract Subject headings
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  • We present seven new vertebrate homologs of the prolactin-releasing hormone receptor (PRLHR) and show that these are found as two separate subtypes, PRLHR1 and PRLHR2. Analysis of a number of vertebrate sequences using phylogeny, pharmacology, and paralogon analysis indicates that the PRLHRs are likely to share a common ancestry with the neuropeptide Y (NPY) receptors. Moreover, a micromolar level of NPY was able to bind and inhibit completely the PRLH-evoked response in PRLHR1-expressing cells. We suggest that an ancestral PRLH peptide started coevolving with a redundant NPY binding receptor, which then became PRLHR, approximately 500 million years ago. The PRLHR1 subtype was shown to have a relatively high evolutionary rate compared to receptors with fixed peptide preference, which could indicate a drastic change in binding preference, thus supporting this hypothesis. This report suggests how gene duplication events can lead to novel peptide ligand/receptor interactions and hence spur the evolution of new physiological functions.

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