Duality of Gonadotropins in Gnathostomes
Identifieur interne : 000165 ( France/Analysis ); précédent : 000164; suivant : 000166Duality of Gonadotropins in Gnathostomes
Auteurs : Bruno Quérat [France] ; Caroline Tonnerre-Doncarli [France] ; Florence Géniès [France] ; Christian Salmon [France]Source :
- General and Comparative Endocrinology [ 0016-6480 ] ; 2001.
English descriptors
- KwdEn :
Abstract
The glycoprotein hormone α subunit and two β subunits were cloned from the ventral lobe of the pituitary gland of an elasmobranch fish, Scyliorhinus canicula. The mature α subunit was 96 amino acids long and showed 64–76 amino acid residues in common with α subunit sequences of representatives of sarcopterygians (tetrapods and dipnoi) and actinopterigyans (chondrostei and teleostei). The Scyliorhinus β1 subunit was 115 amino acid long and had characteristics specific to FSH β subunits and, in particular, the two potential N-linked glycosylation sites in conserved positions. The β2 sequence was 112 amino acids long. The Scyliorhinus β2 subunit had only one potential N-linked glycosylation site at the same position as that in LH. None of the two β subunits from Scyliorhinus displayed the two amino acid insertions shared by TSH β subunit sequences between the fith and the sixth cysteines as compared to actinopterygian and sarcopterygian gonadotropins. These data indicate that Scyliorhinus β1 and β2 subunits are orthologous to FSH and LH β subunits, respectively. It is concluded that the two FSH and LH lineages were already individualized at the emergence of chondrichthyans.
Url:
DOI: 10.1006/gcen.2001.7715
Affiliations:
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ISTEX:45CAB93523A1D7D586D5990940C3D78F935D05FCLe document en format XML
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xml:lang="en"><term>FSH</term><term>LH</term><term>elasmobranchs</term><term>gonadotropins</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The glycoprotein hormone α subunit and two β subunits were cloned from the ventral lobe of the pituitary gland of an elasmobranch fish, Scyliorhinus canicula. The mature α subunit was 96 amino acids long and showed 64–76 amino acid residues in common with α subunit sequences of representatives of sarcopterygians (tetrapods and dipnoi) and actinopterigyans (chondrostei and teleostei). The Scyliorhinus β1 subunit was 115 amino acid long and had characteristics specific to FSH β subunits and, in particular, the two potential N-linked glycosylation sites in conserved positions. The β2 sequence was 112 amino acids long. The Scyliorhinus β2 subunit had only one potential N-linked glycosylation site at the same position as that in LH. None of the two β subunits from Scyliorhinus displayed the two amino acid insertions shared by TSH β subunit sequences between the fith and the sixth cysteines as compared to actinopterygian and sarcopterygian gonadotropins. These data indicate that Scyliorhinus β1 and β2 subunits are orthologous to FSH and LH β subunits, respectively. It is concluded that the two FSH and LH lineages were already individualized at the emergence of chondrichthyans.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Paris</li></settlement></list><tree><country name="France"><region name="Île-de-France"><name sortKey="Querat, Bruno" sort="Querat, Bruno" uniqKey="Querat B" first="Bruno" last="Quérat">Bruno Quérat</name></region><name sortKey="Genies, Florence" sort="Genies, Florence" uniqKey="Genies F" first="Florence" last="Géniès">Florence Géniès</name><name sortKey="Salmon, Christian" sort="Salmon, Christian" uniqKey="Salmon C" first="Christian" last="Salmon">Christian Salmon</name><name sortKey="Tonnerre Doncarli, Caroline" sort="Tonnerre Doncarli, Caroline" uniqKey="Tonnerre Doncarli C" first="Caroline" last="Tonnerre-Doncarli">Caroline Tonnerre-Doncarli</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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