Journals / Turkish Journal of Zoology / 2016 / Cilt: 40 - Sayı: 3

Characteristic analysis of prolactin and its receptor genes fromRana chensinensis and expression pattern during metamorphosis

Pages
303–313
Publication Date
2022-11-05
DOI
—
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AI Summary & Key Takeaways

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⚡ TL;DR(Too Long; Didn't Read)

The results showed that the expressional tendencies of rcPRLR increased throughout stages 33 43 in the four tissues, which was probably related to tissue remodeling.

📌 3 Key Takeaways

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Objective & Hypothesis:In order to explore the role of prolactin (PRL) and the prolactin receptor (PRLR) during metamorphosis of amphibians, both cDNAs from the Chinese brown frog Rana chensinensis were identified.
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Key Findings & Data:A PRL cDNA consisting of a 645-bp open reading frame and a PRLR cDNA consisting of a 1854-bp open reading frame were obtained.
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Conclusion & Impact:The results showed that the expressional tendencies of rcPRLR increased throughout stages 33 43 in the four tissues, which was probably related to tissue remodeling.
🔬Design:Modeling & Simulation
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Abstract

In order to explore the role of prolactin (PRL) and the prolactin receptor (PRLR) during metamorphosis of amphibians, both cDNAs from the Chinese brown frog Rana chensinensis were identified. A PRL cDNA consisting of a 645-bp open reading frame and a PRLR cDNA consisting of a 1854-bp open reading frame were obtained. The amino acid sequence analysis indicated that there were 2 pairs of conserved Cys residues in both mature rcPRL and rcPRLR, and that their positions were conserved as well. Comparison of our results with those for other vertebrates implies that receptor recognition in anurans may not be pH-dependent. The relations of identity between rcPRL and other vertebrate PRLs resembled those of the identity between rcPRLR and other vertebrate PRLRs, suggesting that PRL may have coevolved with PRLR in R. chensinensis.In addition, rcPRL and rcPRLR mRNA was detected via RT-PCR in various tissues of R. chensinensis tadpoles. By using qRT-PCR, rcPRLR mRNA in the liver, skin, tail, and kidney tissue of different stages (stages 33 43) during metamorphosis was analyzed. The results showed that the expressional tendencies of rcPRLR increased throughout stages 33 43 in the four tissues, which was probably related to tissue remodeling.

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Cite This Article

ZHANG, Y., JIN, W., WANG, X., WANG, H., LI, X., DU, C. (2022). Characteristic analysis of prolactin and its receptor genes fromRana chensinensis and expression pattern during metamorphosis. Turkish Journal of Zoology, Cilt: 40 - Sayı: 3, 303–313. https://ajindex.com/articles/616267

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References (15)

  1. Bazan JF (1989). A novel family of growth factor receptors: a common binding domain in the growth hormone, prolactin, erythropoietin and IL-6 receptors, and the p75 IL-2 receptor beta-chain. Biochem Biophys Res Commun 164: 788-795.
  2. Blom N, Gammeltoft S, Brunak S (1999). Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 294: 1351-1362.
  3. Bole-Feysot C, Goffin V, Edery M, Binart N, Kelly PA (1998). Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice. Endocr Rev 19: 225-268.
  4. Bouilly J, Sonigo C, Auffret J, Gibori G, Binart N (2012). Prolactin signaling mechanisms in ovary. Mol Cell Endocrinol 356: 80-87.
  5. Buckbinder L, Brown DD (1993). Expression of the Xenopus laevisprolactin and thyrotropin genes during metamorphosis. P Natl Acad Sci USA 90: 3820-3824.
  6. Chang Y, Huang F, Lo T (1992). Molecular cloning of silver carp and bighead carp prolactin. Gen Comp Endocrinol 87: 260-265.
  7. Clarke WC, Bern HA (2012). Comparative endocrinology of prolactin. Hormonal Proteins and Peptides 8: 105-197.
  8. Dagil R, Knudsen MJ, Olsen JG, O’Shea C, Franzmann M, Goffin V, Teilum K, Breinholt J, Kragelund BB (2012). The WSXWS motif in cytokine receptors is a molecular switch involved in receptor activation: insight from structures of the prolactin receptor. Structure 20: 270-282.
  9. Demmer J (1999). The prolactin receptor from the brushtail possum (Trichosurus vulpecula): cDNA cloning, expression and functional analysis. Mol Cell Endocrinol 148: 119-127.
  10. Denver RJ (1996). Neuroendocrine control of amphibian metamorphosis. In: Gilbert LI, Tata JR, Atkinson BG, editors. Metamorphosis: Postembryonic Reprogramming of Gene Expression in Amphibian and Insect Cells. San Diego, CA, USA: Academic Press Inc., pp. 433-464.
  11. Denver RJ (1997). Proximate mechanisms of phenotypic plasticity in amphibian metamorphosis. Am Zool 37: 172-184.
  12. Denver RJ (2013). Neuroendocrinology of amphibian metamorphosis. Curr Top Dev Biol 103: 195-227.
  13. Doliana R, Argentini C, Segat D, Santarossa P, Mucignat MT, Colombo L, Bortolussi M (1994). The prolactin of European sea bass (Dicentrarchus labrax L.): cloning of cDNA and efficient expression in Escherichia coli. Biochem Mol Biol International 33: 1117-1126.
  14. Etkin W, Gona A (1967). Antagonism between prolactin and thyroid hormone in amphibian development. J Exp Zool 165: 249-258.
  15. Freeman ME, Kanyicska B, Lerant A, Nagy G (2000). Prolactin: structure, funct