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Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone

In 1971 Schally and co-workers (Schally et al., 1971) isolated gonadotropin-releasing hormone (now called luteinizing hormone-releasing hormone (LH-RH)) from sheep hypothalami and established that the hormone was a decapeptide with the amino acid sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH...

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Main Author: King, Judy A
Other Authors: Millar, Robert P
Format: Thesis
Language:English
Published: Division of Chemical Pathology 2018
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access_status_str Open Access
author King, Judy A
author2 Millar, Robert P
author_browse King, Judy A
Millar, Robert P
author_facet Millar, Robert P
King, Judy A
author_sort King, Judy A
collection Thesis
description In 1971 Schally and co-workers (Schally et al., 1971) isolated gonadotropin-releasing hormone (now called luteinizing hormone-releasing hormone (LH-RH)) from sheep hypothalami and established that the hormone was a decapeptide with the amino acid sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH₂. The peptide was subsequently synthesised (Matsuo et al., 1971b) and shown to stimulate the release of gonadotropins (luteinizing hormone and follicle-stimulating hormone) in a wide range of mammalian species (Schally et al., 1973, 1976). With the exception of amphibians, nonmammalian vertebrates have a poor gonadotropin response to synthetic mammalian LH-RH (for reviews, see Ball, 1981; Jackson, 1981; King and Millar, 1981a). Since there is considerable molecular heterogeneity in the related neurohypophysial nonapeptide hormones (oxytocin-vasopressin) amongst vertebrates (Acher et al., 1972), we postulated that differences might exist in the structure of hypothalamic LH-RH in different vertebrate classes, Utilising a combination of regionspecific antisera and chromatographic techniques, we established that amphibian hypothalamic LH-RH is identical to the mammalian peptide while avian, reptilian, and piscine hypothalamic LH-RHs differ structurally in the region Gly⁶-Leu⁷-Arg⁸ (King and Millar, 1979a, 1980), We have now conducted further studies on avian hypothalamic LH-RH, which indicate that the arginine residue in position eight of mammalian LH-RH is substituted by glutamine in this vertebrate class. Purification of LH-RH from chicken hypothalami and determination of the amino acid composition have confirmed that the structure of avian LH-RH is: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Gln-Pro-Gly-NH₂.
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institution University of Cape Town (South Africa)
language eng
last_indexed 2026-06-10T12:34:17.944Z
license_str Not specified — see source repository
provenance_str_mv Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository
publishDate 2018
publishDateRange 2018
publishDateSort 2018
publisher Division of Chemical Pathology
publisherStr Division of Chemical Pathology
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source_str UCTD — University of Cape Town Open Access Repository
spelling oai:open.uct.ac.za:11427/27260 Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone King, Judy A Millar, Robert P Hypothalamic hormones Gonadorelin Chickens In 1971 Schally and co-workers (Schally et al., 1971) isolated gonadotropin-releasing hormone (now called luteinizing hormone-releasing hormone (LH-RH)) from sheep hypothalami and established that the hormone was a decapeptide with the amino acid sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH₂. The peptide was subsequently synthesised (Matsuo et al., 1971b) and shown to stimulate the release of gonadotropins (luteinizing hormone and follicle-stimulating hormone) in a wide range of mammalian species (Schally et al., 1973, 1976). With the exception of amphibians, nonmammalian vertebrates have a poor gonadotropin response to synthetic mammalian LH-RH (for reviews, see Ball, 1981; Jackson, 1981; King and Millar, 1981a). Since there is considerable molecular heterogeneity in the related neurohypophysial nonapeptide hormones (oxytocin-vasopressin) amongst vertebrates (Acher et al., 1972), we postulated that differences might exist in the structure of hypothalamic LH-RH in different vertebrate classes, Utilising a combination of regionspecific antisera and chromatographic techniques, we established that amphibian hypothalamic LH-RH is identical to the mammalian peptide while avian, reptilian, and piscine hypothalamic LH-RHs differ structurally in the region Gly⁶-Leu⁷-Arg⁸ (King and Millar, 1979a, 1980), We have now conducted further studies on avian hypothalamic LH-RH, which indicate that the arginine residue in position eight of mammalian LH-RH is substituted by glutamine in this vertebrate class. Purification of LH-RH from chicken hypothalami and determination of the amino acid composition have confirmed that the structure of avian LH-RH is: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Gln-Pro-Gly-NH₂. 2018-02-05T12:35:52Z 2018-02-05T12:35:52Z 1982 Doctoral Thesis Doctoral PhD http://hdl.handle.net/11427/27260 eng application/pdf Division of Chemical Pathology Faculty of Health Sciences University of Cape Town
spellingShingle Hypothalamic hormones
Gonadorelin
Chickens
King, Judy A
Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone
thesis_degree_str Doctoral
title Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone
title_full Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone
title_fullStr Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone
title_full_unstemmed Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone
title_short Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone
title_sort structure and biological activity of avian hypothalamic luteinizing hormone releasing hormone
topic Hypothalamic hormones
Gonadorelin
Chickens
url http://hdl.handle.net/11427/27260
work_keys_str_mv AT kingjudya structureandbiologicalactivityofavianhypothalamicluteinizinghormonereleasinghormone