Journal
JOURNAL OF MOLECULAR ENDOCRINOLOGY
Volume 41, Issue 3-4, Pages 219-228Publisher
SOC ENDOCRINOLOGY
DOI: 10.1677/JME-08-0030
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Funding
- NSF [IBN-0421923]
- New Hampshire Agriculture Experiment Station [2342]
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [0849569] Funding Source: National Science Foundation
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The specificity of the vertebrate hypothalamic-pituitary-gonadal and hypothalamic-pituitary-thyroid axes is explained by the evolutionary refinement of the specificity of expression and selectivity of interaction between the glycoprotein hormones GpH (FSH, LH, and TSH) and their cognate receptors GpH-R (FSH-R, LH-R, and TSH-R). These two finely tuned signaling pathways evolved by gene duplication and functional divergence from an ancestral GpH/GpH-R pair. Comparative analysis of the protochordate and gnathostome endocrine systems suggests that this process took place prior or concomitantly with the emergence of the gnathostome lineage. Here, we report identification and characterization of a novel glycoprotein hormone receptor (IGpH-R II) in the Agnathan sea lamprey. This 781 residue protein was found similar to 43% identical with mammalian TSH-R and FSH-R representative sequences, and similarly with these two classes of mammalian receptors it is assembled from ten exons. A synthetic ligand containing the lamprey glycoprotein hormone beta-chain tethered upstream of a mammalian alpha-chain activated the IGpH-R II expressed in COS-7 cells but in a lesser extent than IGpH-R I. Molecular phylogenetic analysis of vertebrate GpH-R protein sequences suggests a closer relationship between IGpH-R II and gnathostome thyrotropin receptors. Overall, the presence and characteristics of the lamprey glycoprotein hormone receptors suggest existence of a primitive functionally overlapping glycoprotein hormone/glycoprotein hormone receptor system in this animal.
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