Analysis of the post-translational processing of alpha-MSH in the pituitaries of the chondrostean fishes, Acipenser transmontanus and Polyodon spathula.
Identifieur interne : 000853 ( Ncbi/Curation ); précédent : 000852; suivant : 000854Analysis of the post-translational processing of alpha-MSH in the pituitaries of the chondrostean fishes, Acipenser transmontanus and Polyodon spathula.
Auteurs : H. Keller [États-Unis] ; J M Redding ; G. Moberg ; R M DoresSource :
- General and comparative endocrinology [ 0016-6480 ] ; 1994.
English descriptors
- KwdEn :
- Acetylation, Animals, Biological Evolution, Chromatography, High Pressure Liquid, Fishes (metabolism), Male, Peptide Fragments (analysis), Peptide Fragments (isolation & purification), Peptide Fragments (metabolism), Pituitary Gland (metabolism), Protein Processing, Post-Translational (physiology), Radioimmunoassay, Species Specificity, alpha-MSH (analogs & derivatives), alpha-MSH (immunology), alpha-MSH (metabolism).
- MESH :
- chemical , analogs & derivatives : alpha-MSH.
- chemical , analysis : Peptide Fragments.
- chemical , immunology : alpha-MSH.
- chemical , isolation & purification : Peptide Fragments.
- metabolism : Fishes, Peptide Fragments, Pituitary Gland, alpha-MSH.
- physiology : Protein Processing, Post-Translational.
- Acetylation, Animals, Biological Evolution, Chromatography, High Pressure Liquid, Male, Radioimmunoassay, Species Specificity.
Abstract
Multiple forms of alpha-MSH were isolated from the pituitaries of the white sturgeon, Acipenser transmontanus, and the paddlefish, Polyodon spathula, following fractionation of the pituitary extracts by reversed-phase HPLC. In both species, immunoreactive forms which eluted with the same retention times as synthetic mammalian ACTH(1-13)NH2, monoacetylated alpha-MSH, and diacetylated alpha-MSH were detected. In the pituitary of the sturgeon, N-acetylated forms of alpha-MSH represented 91% of the total alpha-MSH isolated. However, in the pituitary of the paddlefish, N-acetylated forms of alpha-MSH accounted for only 45% of the total alpha-MSH isolated. The presence of N-acetylated forms of alpha-MSH in the pituitaries of representatives of the two extant genera of chondrostean fish coupled with the observation that N-acetylated forms of alpha-MSH are present in the pituitaries of cladistian and neopterygian fishes indicates that the alpha-MSH specific N-acetylation mechanism evolved prior to the radiation of the Actinopterygii. A conspicuous feature of the chondrostean alpha-MSH N-acetylation reaction was the low levels of diacetylated alpha-MSH produced relative to the levels of monoacetylated alpha-MSH. Similar observations have been made for the cladistian fish, Calamoichthys calabaricus, and the cartilaginous fish, Hydrolagus colliei. However, in holostean fishes, lungfishes, and tetrapods, the diacetylated form of alpha-MSH is the major end product produced in the intermediate pituitary. The phylogenetic implications of these observations will be discussed.
DOI: 10.1006/gcen.1994.1071
PubMed: 7926625
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pubmed:7926625Le document en format XML
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<author><name sortKey="Redding, J M" sort="Redding, J M" uniqKey="Redding J" first="J M" last="Redding">J M Redding</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Analysis of the post-translational processing of alpha-MSH in the pituitaries of the chondrostean fishes, Acipenser transmontanus and Polyodon spathula.</title>
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<term>Fishes (metabolism)</term>
<term>Male</term>
<term>Peptide Fragments (analysis)</term>
<term>Peptide Fragments (isolation & purification)</term>
<term>Peptide Fragments (metabolism)</term>
<term>Pituitary Gland (metabolism)</term>
<term>Protein Processing, Post-Translational (physiology)</term>
<term>Radioimmunoassay</term>
<term>Species Specificity</term>
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<term>alpha-MSH (immunology)</term>
<term>alpha-MSH (metabolism)</term>
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<term>Animals</term>
<term>Biological Evolution</term>
<term>Chromatography, High Pressure Liquid</term>
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<term>Radioimmunoassay</term>
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<front><div type="abstract" xml:lang="en">Multiple forms of alpha-MSH were isolated from the pituitaries of the white sturgeon, Acipenser transmontanus, and the paddlefish, Polyodon spathula, following fractionation of the pituitary extracts by reversed-phase HPLC. In both species, immunoreactive forms which eluted with the same retention times as synthetic mammalian ACTH(1-13)NH2, monoacetylated alpha-MSH, and diacetylated alpha-MSH were detected. In the pituitary of the sturgeon, N-acetylated forms of alpha-MSH represented 91% of the total alpha-MSH isolated. However, in the pituitary of the paddlefish, N-acetylated forms of alpha-MSH accounted for only 45% of the total alpha-MSH isolated. The presence of N-acetylated forms of alpha-MSH in the pituitaries of representatives of the two extant genera of chondrostean fish coupled with the observation that N-acetylated forms of alpha-MSH are present in the pituitaries of cladistian and neopterygian fishes indicates that the alpha-MSH specific N-acetylation mechanism evolved prior to the radiation of the Actinopterygii. A conspicuous feature of the chondrostean alpha-MSH N-acetylation reaction was the low levels of diacetylated alpha-MSH produced relative to the levels of monoacetylated alpha-MSH. Similar observations have been made for the cladistian fish, Calamoichthys calabaricus, and the cartilaginous fish, Hydrolagus colliei. However, in holostean fishes, lungfishes, and tetrapods, the diacetylated form of alpha-MSH is the major end product produced in the intermediate pituitary. The phylogenetic implications of these observations will be discussed.</div>
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