Biological activity of lipophilic derivatives of peptide 562–572 of rat luteinizing hormone receptor
A study investigated the biological activity of lipophilic derivatives of peptide 562-572 of the rat luteinizing hormone receptor. This is the first study to demonstrate that the modification of the peptide corresponding to the C terminal region of the third intracellular loop of LHR with lipophilic...
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Veröffentlicht in: | Doklady. Biochemistry and biophysics 2013-09, Vol.452 (1), p.248-250 |
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creator | Shpakova, E. A. Derkach, K. V. Shpakov, A. O. |
description | A study investigated the biological activity of lipophilic derivatives of peptide 562-572 of the rat luteinizing hormone receptor. This is the first study to demonstrate that the modification of the peptide corresponding to the C terminal region of the third intracellular loop of LHR with lipophilic residues of decanoic and palmitic acids greatly enhances their ability to influence the basal and hCG stimulated activity of adenylyl cyclase signaling system in rat testes and that this modification is effective only if the hydrophobic radical is located at the C terminus of the peptide, mimicking the sixth transmembrane domain of LHR and being comparable to that domain in size and hydrophobicity. |
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This is the first study to demonstrate that the modification of the peptide corresponding to the C terminal region of the third intracellular loop of LHR with lipophilic residues of decanoic and palmitic acids greatly enhances their ability to influence the basal and hCG stimulated activity of adenylyl cyclase signaling system in rat testes and that this modification is effective only if the hydrophobic radical is located at the C terminus of the peptide, mimicking the sixth transmembrane domain of LHR and being comparable to that domain in size and hydrophobicity.</description><identifier>ISSN: 1607-6729</identifier><identifier>EISSN: 1608-3091</identifier><identifier>DOI: 10.1134/S1607672913050116</identifier><identifier>PMID: 24150584</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Adenylyl Cyclases - metabolism ; Animals ; Biochemistry ; Biological and Medical Physics ; Biomedical and Life Sciences ; Biophysics ; Biophysics and Molecular Biology ; Hormones ; Life Sciences ; Molecular biology ; Oligopeptides - chemistry ; Oligopeptides - metabolism ; Peptides ; Protein Structure, Tertiary ; Rats ; Receptors, LH - chemistry ; Receptors, LH - metabolism ; Rodents</subject><ispartof>Doklady. 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This is the first study to demonstrate that the modification of the peptide corresponding to the C terminal region of the third intracellular loop of LHR with lipophilic residues of decanoic and palmitic acids greatly enhances their ability to influence the basal and hCG stimulated activity of adenylyl cyclase signaling system in rat testes and that this modification is effective only if the hydrophobic radical is located at the C terminus of the peptide, mimicking the sixth transmembrane domain of LHR and being comparable to that domain in size and hydrophobicity.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>24150584</pmid><doi>10.1134/S1607672913050116</doi><tpages>3</tpages></addata></record> |
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subjects | Adenylyl Cyclases - metabolism Animals Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biophysics Biophysics and Molecular Biology Hormones Life Sciences Molecular biology Oligopeptides - chemistry Oligopeptides - metabolism Peptides Protein Structure, Tertiary Rats Receptors, LH - chemistry Receptors, LH - metabolism Rodents |
title | Biological activity of lipophilic derivatives of peptide 562–572 of rat luteinizing hormone receptor |
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