The N-Linked Glycosylation Site N191 Is Necessary for PKA Signal Transduction in Eel Follicle-Stimulating Hormone Receptor
The follicle-stimulating hormone receptor (FSHR) contains several N-linked glycosylation sites in its extracellular region. We conducted the present study to determine whether conserved glycosylated sites in eel FSHR are necessary for cyclic adenosine monophosphate (cAMP) signal transduction. We use...
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Published in | International journal of molecular sciences Vol. 23; no. 21; p. 12792 |
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Abstract | The follicle-stimulating hormone receptor (FSHR) contains several N-linked glycosylation sites in its extracellular region. We conducted the present study to determine whether conserved glycosylated sites in eel FSHR are necessary for cyclic adenosine monophosphate (cAMP) signal transduction. We used site-directed mutagenesis to induce four mutations (N120Q, N191Q, N272Q, and N288Q) in the N-linked glycosylation sites of eel FSHR. In the eel FSHR wild-type (wt), the cAMP response was gradually increased in a dose-dependent manner (0.01–1500 ng/mL), displaying a high response (approximately 57.5 nM/104 cells) at the Rmax level. Three mutants (N120Q, N272Q, and N288Q) showed a considerably decreased signal transduction as a result of high-ligand treatment, whereas one mutant (N191Q) exhibited a completely impaired signal transduction. The expression level of the N191Q mutant was only 9.2% relative to that of the eel FSHR-wt, indicating a negligible expression level. The expression levels of the N120Q and N272Q mutants were approximately 35.9% and 24% of the FSHG-wt, respectively. The N288Q mutant had an expression level similar to that of the eel FSHR-wt, despite the mostly impaired cAMP responsiveness. The loss of the cell surface agonist-receptor complexes was very rapid in the cells expressing eel FSHR-wt and FSHR-N288Q mutants. Specifically, the N191Q mutant was completely impaired by the loss of cell surface receptors, despite treatment with a high concentration of the agonist. Therefore, we suggest that the N191 site is necessary for cAMP signal transduction. This finding implies that the cAMP response, mediated by G proteins, is directly related to the loss of cell surface receptors as a result of high-agonist treatment. |
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AbstractList | The follicle-stimulating hormone receptor (FSHR) contains several N-linked glycosylation sites in its extracellular region. We conducted the present study to determine whether conserved glycosylated sites in eel FSHR are necessary for cyclic adenosine monophosphate (cAMP) signal transduction. We used site-directed mutagenesis to induce four mutations (N120Q, N191Q, N272Q, and N288Q) in the N-linked glycosylation sites of eel FSHR. In the eel FSHR wild-type (wt), the cAMP response was gradually increased in a dose-dependent manner (0.01–1500 ng/mL), displaying a high response (approximately 57.5 nM/104 cells) at the Rmax level. Three mutants (N120Q, N272Q, and N288Q) showed a considerably decreased signal transduction as a result of high-ligand treatment, whereas one mutant (N191Q) exhibited a completely impaired signal transduction. The expression level of the N191Q mutant was only 9.2% relative to that of the eel FSHR-wt, indicating a negligible expression level. The expression levels of the N120Q and N272Q mutants were approximately 35.9% and 24% of the FSHG-wt, respectively. The N288Q mutant had an expression level similar to that of the eel FSHR-wt, despite the mostly impaired cAMP responsiveness. The loss of the cell surface agonist-receptor complexes was very rapid in the cells expressing eel FSHR-wt and FSHR-N288Q mutants. Specifically, the N191Q mutant was completely impaired by the loss of cell surface receptors, despite treatment with a high concentration of the agonist. Therefore, we suggest that the N191 site is necessary for cAMP signal transduction. This finding implies that the cAMP response, mediated by G proteins, is directly related to the loss of cell surface receptors as a result of high-agonist treatment. The follicle-stimulating hormone receptor (FSHR) contains several N-linked glycosylation sites in its extracellular region. We conducted the present study to determine whether conserved glycosylated sites in eel FSHR are necessary for cyclic adenosine monophosphate (cAMP) signal transduction. We used site-directed mutagenesis to induce four mutations (N120Q, N191Q, N272Q, and N288Q) in the N-linked glycosylation sites of eel FSHR. In the eel FSHR wild-type (wt), the cAMP response was gradually increased in a dose-dependent manner (0.01–1500 ng/mL), displaying a high response (approximately 57.5 nM/10 4 cells) at the Rmax level. Three mutants (N120Q, N272Q, and N288Q) showed a considerably decreased signal transduction as a result of high-ligand treatment, whereas one mutant (N191Q) exhibited a completely impaired signal transduction. The expression level of the N191Q mutant was only 9.2% relative to that of the eel FSHR-wt, indicating a negligible expression level. The expression levels of the N120Q and N272Q mutants were approximately 35.9% and 24% of the FSHG-wt, respectively. The N288Q mutant had an expression level similar to that of the eel FSHR-wt, despite the mostly impaired cAMP responsiveness. The loss of the cell surface agonist-receptor complexes was very rapid in the cells expressing eel FSHR-wt and FSHR-N288Q mutants. Specifically, the N191Q mutant was completely impaired by the loss of cell surface receptors, despite treatment with a high concentration of the agonist. Therefore, we suggest that the N191 site is necessary for cAMP signal transduction. This finding implies that the cAMP response, mediated by G proteins, is directly related to the loss of cell surface receptors as a result of high-agonist treatment. |
Author | Min, Kwan-Sik Lee, Jong-Hyuk Park, Hong-Kyu Kang, Myung-Hwa Byambaragchaa, Munkhzaya Kim, Dae-Jung |
AuthorAffiliation | 2 Animal Biotechnology, Graduate School of Future Convergence Technology, Hankyong National University, Ansung 17579, Korea 4 College of Pharmacy, Chung-Ang University, Seoul 06974, Korea 1 Institute of Genetic Engineering, Hankyong National University, Ansung 17579, Korea 5 Department of Food Science and Nutrition, Hoseo University, Asan 31499, Korea 3 Aquaculture Industry Division, South Sea Fisheries Research Institute, National Institute of Fisheries Science (NIFS), Yeosu 59780, Korea 6 Carbon-Neutral Resources Research Center, Hankyong National University, Ansung 17579, Korea |
AuthorAffiliation_xml | – name: 3 Aquaculture Industry Division, South Sea Fisheries Research Institute, National Institute of Fisheries Science (NIFS), Yeosu 59780, Korea – name: 2 Animal Biotechnology, Graduate School of Future Convergence Technology, Hankyong National University, Ansung 17579, Korea – name: 4 College of Pharmacy, Chung-Ang University, Seoul 06974, Korea – name: 1 Institute of Genetic Engineering, Hankyong National University, Ansung 17579, Korea – name: 6 Carbon-Neutral Resources Research Center, Hankyong National University, Ansung 17579, Korea – name: 5 Department of Food Science and Nutrition, Hoseo University, Asan 31499, Korea |
Author_xml | – sequence: 1 givenname: Munkhzaya surname: Byambaragchaa fullname: Byambaragchaa, Munkhzaya – sequence: 2 givenname: Hong-Kyu surname: Park fullname: Park, Hong-Kyu – sequence: 3 givenname: Dae-Jung surname: Kim fullname: Kim, Dae-Jung – sequence: 4 givenname: Jong-Hyuk orcidid: 0000-0002-9932-8879 surname: Lee fullname: Lee, Jong-Hyuk – sequence: 5 givenname: Myung-Hwa surname: Kang fullname: Kang, Myung-Hwa – sequence: 6 givenname: Kwan-Sik orcidid: 0000-0002-5451-3085 surname: Min fullname: Min, Kwan-Sik |
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Snippet | The follicle-stimulating hormone receptor (FSHR) contains several N-linked glycosylation sites in its extracellular region. We conducted the present study to... |
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SubjectTerms | Adenosine monophosphate Agonists cAMP pathway Cell surface Cyclic AMP eel FSHR Follicle-stimulating hormone Follicles Glycoproteins Glycosylation GPCR signaling Hormones Kinases Ligands loss of cell surface receptor Mammals Mutants Mutation N-linked glycosylation site Protein kinase A Proteins Signal transduction Site-directed mutagenesis |
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Title | The N-Linked Glycosylation Site N191 Is Necessary for PKA Signal Transduction in Eel Follicle-Stimulating Hormone Receptor |
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