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Heather G Marco - One of the best experts on this subject based on the ideXlab platform.
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biochemically identified neuropeptides in a caddisfly trichoptera and a pygmy mole cricket orthoptera caelifera tridactyloidea
Archives of Insect Biochemistry and Physiology, 2021Co-Authors: Gerd Gade, Petr Šimek, Gerd Gade, Heather G MarcoAbstract:One representative of the order Trichoptera, namely the caddisfly Chaetopteryx villosa, was investigated along with the pygmy mole cricket Xya capensis which is a representative of the most basal superFamily of the caeliferan Orthoptera, that is, the Tridactyloidea. From both clades neuropeptides have not been biochemically characterized before this study. Here, members of the adipokinetic Hormone Family (AKHs) are sequenced via liquid chromatography (LC)-ion trap mass spectrometry from methanolic extracts from the corpora cardiaca of respective species. The corpora cardiaca were dissected, methanolic extracts prepared, peptides separated by liquid chromatography (LC), and AKHs detected and sequenced by ion trap mass spectrometry. Both species investigated contain an octapeptide AKH: the trichopteran species has the peptide with the sequence pGlu-Leu-Thr-Phe-Thr-Pro-Ser-Trp amide; the ambiguity of the isobaric amino acids Leu and Ile at position two was solved by comparing retention times on LC and by co-elution with the synthetic Leu2 -form. This peptide is known as Aedae-AKH and found in certain dipteran species and in an alderfly (Megaloptera). The tridactyloid species contains the peptide with the sequence pGlu-Val-Asn-Phe-Ser-Pro-Gly-Trp amide which had first been identified in a member of the order Mantophasmatodea and is called Manto-CC. Comparisons are made between the AKH complements of the sister groups Trichoptera and Lepidoptera and their possible relatedness and, on the other hand, between the AKH of X. capensis with those of closely related caeliferan superfamilies. The biology of the two studied species is used to speculate about a possible function of the elucidated Hormones. Lastly, the use of a larval stage as starting material for structural neuropeptide information is discussed.
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unique members of the adipokinetic Hormone Family in butterflies and moths insecta lepidoptera
Frontiers in Physiology, 2020Co-Authors: Heather G Marco, Petr Šimek, Gerd GadeAbstract:Lepidoptera is amongst one of the four most speciose insect orders and ecologically very successful because of their ability to fly. Insect flight is always aerobic and exacts a high metabolic demand on the animal. A Family of structurally related neuropeptides, generically referred to as adipokinetic Hormones (AKHs), play a key role in triggering the release of readily utilizable fuel metabolites into the hemolymph from the storage forms in the fat body. We used mass spectrometry to elucidate AKH sequences from 34 species of Lepidoptera and searched the literature and publicly available databases to compile (in a phylogenetic context) a comprehensive list of all Lepidoptera sequences published/predicted from a total of 76 species. We then used the resulting set of 15 biochemically characterized AKHs in a physiological assay that measures lipid or carbohydrate mobilization in three different lepidopteran species to learn about the functional cross-activity (receptor-ligand interactions) amongst the different butterfly/moth families. Our results include novel peptide structures, demonstrate structural diversity, phylogenetic trends in peptide distribution and order-specificity of Lepidoptera AKHs. There is almost an equal occurrence of octa-, nona-, and decapeptides, with an unparalleled emphasis on nonapeptides than in any insect order. Primitive species make Peram-CAH-II, an octapeptide found also in other orders; the lepidopteran signature peptide is Manse-AKH. Not all of the 15 tested AKHs are active in Pieris brassicae; this provides insight into structure-activity specificity and could be useful for further investigations into possible biorational insecticide development.
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two novel tyrosine containing peptides tyr 4 of the adipokinetic Hormone Family in beetles of the families coccinellidae and silphidae
Amino Acids, 2015Co-Authors: Petr Šimek, Heather G MarcoAbstract:Novel members of the adipokinetic Hormone Family of peptides have been identified from the corpora cardiaca (CC) of two species of beetles representing two families, the Silphidae and the Coccinellidae. A crude CC extract (0.3 gland equivalents) of the burying beetle, Nicrophorus vespilloides, was active in mobilizing trehalose in a heterologous assay using the cockroach Periplaneta americana, whereas the CC extract (0.5 gland equivalents) of the ladybird beetle, Harmonia axyridis, exhibited no hypertrehalosemic activity. Primary sequences of one adipokinetic Hormone from each species were elucidated by liquid chromatography coupled to electrospray mass spectrometry (LC–MS). The multiple MSN electrospray mass data revealed an octapeptide with an unusual tyrosine residue at position 4 for each species: pGlu-Leu-Thr-Tyr-Ser-Thr-Gly-Trp amide for N. vespilloides (code-named Nicve-AKH) and pGlu-Ile-Asn-Tyr-Ser-Thr-Gly-Trp amide for H. axyridis (code-named Harax-AKH). Assignment of the correct sequences was confirmed by synthesis of the peptides and co-elution in reversed-phase high-performance liquid chromatography with fluorescence detection or by LC–MS. Moreover, synthetic peptides were shown to be active in the heterologous cockroach assay system, but Harax-AKH only at a dose of 30 pmol, which explains the negative result with the crude CC extract. It appears that the tyrosine residue at position 4 can be used as a diagnostic feature for certain beetle adipokinetic peptides, because this feature has not been found in another order other than Coleoptera.
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The adipokinetic Hormones of African water bugs of the Heteropteran families Nepidae and Belostomatidae
Physiological Entomology, 2013Co-Authors: Gerd Gade, Heather G MarcoAbstract:Four African species of true water bugs (Nepomorpha: Hemiptera: Heteroptera) are studied by mass spectrometry and biological assays to gain information on the presence, structure and function of peptides from the adipokinetic Hormone (AKH) Family, which are produced in the corpora cardiaca (CC). The water scorpion Laccotrephes fabricii Stal (Nepidae) has the peptide code-named Peram-CAH-I with the sequence pGlu-Val-Asn-Phe-Ser-Pro-Asn-Trp amide, whereas Appasus grassei Poisson (Belostomatidae) produces Anaim-AKH, which is a Ser7 analogue of Peram-CAH-I (pGlu-Val-Asn-Phe-Ser-Pro-Ser-Trp amide). The giant water bug Hydrocyrius columbiae Spinola (Belostomatidae) has two adipokinetic Hormone Family members: Anaim-AKH and Letin-AKH, which again differ only at position 7 (Ser7 versus Tyr7). When the sequence data are compared with current molecular phylogenetic analyses of Nepomorpha, they are essentially in agreement with the newest ideas on phylogenetic relationships among the families. Functional investigation of these peptides reveals a mainly lipid-based energy metabolism in these insects, as demonstrated by a hyperlipaemic response after injecting crude CC extract or the appropriate peptide into the respective species. The carbohydrate concentration in the haemolymph is not affected by such injections, and the carbohydrate level in most cases is lower than that of the circulating lipids. During physical exercise, such as swimming for 1 h, carbohydrates may contribute to some extent to the provision of energy; the substantial increase in the concentration of lipids in the haemolymph, however, is a strong indicator that the peptides are released from the CC and act primarily as true adipokinetic Hormones during this period of intense muscular activity.
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the adipokinetic Hormone Family in chrysomeloidea structural and functional considerations
ZooKeys, 2011Co-Authors: Heather G MarcoAbstract:The presented work is a hybrid of an overview and an original research paper on peptides belonging to the adipokinetic Hormone (AKH) Family that are present in the corpora cardiaca of Chrysomeloidea. First, we introduce the AKH/red pigment-concentrating Hormone (RPCH) peptide Family. Second, we collate the available primary sequence data on AKH peptides in Cerambycidae and Chrysomelidae, and we present new sequencing data (from previously unstudied species) obtained by liquid-chromatography coupled with ion trap electrospray ionisation mass spectrometry. Our expanded data set encompasses the primary structure of AKHs from seven species of Cerambycidae and three species of Chrysomelidae. All of these species synthesise the octapeptide code-named Peram-CAH-I (pGlu-Val-Asn-Phe-Ser-Pro-Asn-Trp amide). Whereas this is the sole AKH peptide in Cerambycidae, Chrysomelidae demonstrate a probable event of AKH gene duplication, thereby giving rise to an additional AKH. This second AKH peptide may be either Emppe-AKH (pGlu-Val-Asn-Phe-Thr-Pro-Asn-Trp amide) or Peram-CAH-II (pGlu-Leu-ThrPhe-Thr-Pro-Asn-Trp amide). The peptide distribution and structural data suggest that both families are closely related and that Peram-CAH-I is the ancestral peptide. We hypothesise on the molecular evolution of Emppe-AKH and Peram-CAH-II from the ancestral peptide due to nonsynonymous missense single nucleotide polymorphism in the nucleotide coding sequence of prepro-AKH. Finally, we review the biological significance of the AKH peptides as hyperprolinaemic Hormones in Chrysomeloidea, i.e. they cause an increase in the circulating concentration of proline. The mobilisation of proline has been demonstrated during flight in both cerambycid and chrysomelid beetles.
Gerd Gade - One of the best experts on this subject based on the ideXlab platform.
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biochemically identified neuropeptides in a caddisfly trichoptera and a pygmy mole cricket orthoptera caelifera tridactyloidea
Archives of Insect Biochemistry and Physiology, 2021Co-Authors: Gerd Gade, Petr Šimek, Gerd Gade, Heather G MarcoAbstract:One representative of the order Trichoptera, namely the caddisfly Chaetopteryx villosa, was investigated along with the pygmy mole cricket Xya capensis which is a representative of the most basal superFamily of the caeliferan Orthoptera, that is, the Tridactyloidea. From both clades neuropeptides have not been biochemically characterized before this study. Here, members of the adipokinetic Hormone Family (AKHs) are sequenced via liquid chromatography (LC)-ion trap mass spectrometry from methanolic extracts from the corpora cardiaca of respective species. The corpora cardiaca were dissected, methanolic extracts prepared, peptides separated by liquid chromatography (LC), and AKHs detected and sequenced by ion trap mass spectrometry. Both species investigated contain an octapeptide AKH: the trichopteran species has the peptide with the sequence pGlu-Leu-Thr-Phe-Thr-Pro-Ser-Trp amide; the ambiguity of the isobaric amino acids Leu and Ile at position two was solved by comparing retention times on LC and by co-elution with the synthetic Leu2 -form. This peptide is known as Aedae-AKH and found in certain dipteran species and in an alderfly (Megaloptera). The tridactyloid species contains the peptide with the sequence pGlu-Val-Asn-Phe-Ser-Pro-Gly-Trp amide which had first been identified in a member of the order Mantophasmatodea and is called Manto-CC. Comparisons are made between the AKH complements of the sister groups Trichoptera and Lepidoptera and their possible relatedness and, on the other hand, between the AKH of X. capensis with those of closely related caeliferan superfamilies. The biology of the two studied species is used to speculate about a possible function of the elucidated Hormones. Lastly, the use of a larval stage as starting material for structural neuropeptide information is discussed.
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unique members of the adipokinetic Hormone Family in butterflies and moths insecta lepidoptera
Frontiers in Physiology, 2020Co-Authors: Heather G Marco, Petr Šimek, Gerd GadeAbstract:Lepidoptera is amongst one of the four most speciose insect orders and ecologically very successful because of their ability to fly. Insect flight is always aerobic and exacts a high metabolic demand on the animal. A Family of structurally related neuropeptides, generically referred to as adipokinetic Hormones (AKHs), play a key role in triggering the release of readily utilizable fuel metabolites into the hemolymph from the storage forms in the fat body. We used mass spectrometry to elucidate AKH sequences from 34 species of Lepidoptera and searched the literature and publicly available databases to compile (in a phylogenetic context) a comprehensive list of all Lepidoptera sequences published/predicted from a total of 76 species. We then used the resulting set of 15 biochemically characterized AKHs in a physiological assay that measures lipid or carbohydrate mobilization in three different lepidopteran species to learn about the functional cross-activity (receptor-ligand interactions) amongst the different butterfly/moth families. Our results include novel peptide structures, demonstrate structural diversity, phylogenetic trends in peptide distribution and order-specificity of Lepidoptera AKHs. There is almost an equal occurrence of octa-, nona-, and decapeptides, with an unparalleled emphasis on nonapeptides than in any insect order. Primitive species make Peram-CAH-II, an octapeptide found also in other orders; the lepidopteran signature peptide is Manse-AKH. Not all of the 15 tested AKHs are active in Pieris brassicae; this provides insight into structure-activity specificity and could be useful for further investigations into possible biorational insecticide development.
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The adipokinetic Hormones of African water bugs of the Heteropteran families Nepidae and Belostomatidae
Physiological Entomology, 2013Co-Authors: Gerd Gade, Heather G MarcoAbstract:Four African species of true water bugs (Nepomorpha: Hemiptera: Heteroptera) are studied by mass spectrometry and biological assays to gain information on the presence, structure and function of peptides from the adipokinetic Hormone (AKH) Family, which are produced in the corpora cardiaca (CC). The water scorpion Laccotrephes fabricii Stal (Nepidae) has the peptide code-named Peram-CAH-I with the sequence pGlu-Val-Asn-Phe-Ser-Pro-Asn-Trp amide, whereas Appasus grassei Poisson (Belostomatidae) produces Anaim-AKH, which is a Ser7 analogue of Peram-CAH-I (pGlu-Val-Asn-Phe-Ser-Pro-Ser-Trp amide). The giant water bug Hydrocyrius columbiae Spinola (Belostomatidae) has two adipokinetic Hormone Family members: Anaim-AKH and Letin-AKH, which again differ only at position 7 (Ser7 versus Tyr7). When the sequence data are compared with current molecular phylogenetic analyses of Nepomorpha, they are essentially in agreement with the newest ideas on phylogenetic relationships among the families. Functional investigation of these peptides reveals a mainly lipid-based energy metabolism in these insects, as demonstrated by a hyperlipaemic response after injecting crude CC extract or the appropriate peptide into the respective species. The carbohydrate concentration in the haemolymph is not affected by such injections, and the carbohydrate level in most cases is lower than that of the circulating lipids. During physical exercise, such as swimming for 1 h, carbohydrates may contribute to some extent to the provision of energy; the substantial increase in the concentration of lipids in the haemolymph, however, is a strong indicator that the peptides are released from the CC and act primarily as true adipokinetic Hormones during this period of intense muscular activity.
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an invertebrate hydroxyproline modified neuropeptide further evidence for a close evolutionary relationship between insect adipokinetic Hormone and mammalian gonadotropin Hormone Family
Biochemical and Biophysical Research Communications, 2011Co-Authors: Gerd Gade, Petr Šimek, Heather G MarcoAbstract:Abstract An octapeptide of the adipokinetic Hormone (AKH) peptide Family is identified in the corpora cardiaca of the stink bug, Nezara viridula, by ESI-MSN (electrospray ionization multistage MS). This is the second AKH in N. viridula and it has a hydroxyproline residue at position 6, whereas the major AKH (known as Panbo-RPCH) has Pro as the sixth amino acid residue. The correct sequence assignment of [Hyp6]-Panbo-RPCH is confirmed by retention time and MS spectra of the synthetic peptide. Various extraction procedures were followed to ascertain whether the hydroxylation is an artefact of extraction, or whether it is due to a true post-translational modification at the proHormone level. The proline hydroxylation is unique for invertebrate neuropeptides, while it has been described in the vertebrate gonadotropin-releasing Hormone (GnRH). The current finding is another piece of evidence that AKH and GnRH form a peptide superFamily and are closely related evolutionarily. Biologically, [Hyp6]-Panbo-RPCH is active in vivo as an AKH, causing hyperlipaemia in the stink bug at low doses, indicating again that it is an endogenous, mature and functional Hormone in this insect species.
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a novel member of the adipokinetic peptide Family in a living fossil the ice crawler galloisiana yuasai is the first identified neuropeptide from the order grylloblattodea
Peptides, 2010Co-Authors: Gerd Gäde, Gerd Gade, Petr ŠimekAbstract:Abstract This is the first report on the structural identity of a neuropeptide of the insect order Grylloblattodea. A peptide was isolated and sequenced from the retrocerebral corpora cardiaca–corpora allata complex of the ice crawler, Galloisiana yuasai . The sequence of the peptide was deduced from the multiple MS N electrospray mass data as that of an octapeptide: pGlu-Val-Asn-Phe-Ser-Pro-Thr-Trp amide. The retention time on reversed-phase HPLC and the CID MS 2 mass spectra of a synthetic peptide with the same primary structure were exactly the same as of the natural peptide. The sequence represents a novel peptide of the adipokinetic Hormone Family which contains presently 50 members. The primary structure differs in only one position to a few previously discovered AKHs. A scenario is outlined that makes it likely that the most recently discovered insect order, the Mantophasmatodea, and the Grylloblattodea are closely related.
Akiyoshi Takahashi - One of the best experts on this subject based on the ideXlab platform.
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evolutionary origin of a functional gonadotropin in the pituitary of the most primitive vertebrate hagfish
Proceedings of the National Academy of Sciences of the United States of America, 2010Co-Authors: Katsuhisa Uchida, Shunsuke Moriyama, Toyokazu Shimotani, Kaori Honda, Stacia A Sower, Makoto Miki, Hiroaki Chiba, Akiyoshi Takahashi, Masumi NozakiAbstract:Hagfish, which lack both jaws and vertebrae, are considered the most primitive vertebrate known, living or extinct. Hagfish have long been the enigma of vertebrate evolution not only because of their evolutionary position, but also because of our lack of knowledge on fundamental processes. Key elements of the reproductive endocrine system in hagfish have yet to be elucidated. Here, the presence and identity of a functional glycoprotein Hormone (GPH) have been elucidated from the brown hagfish Paramyxine atami. The hagfish GPH consists of two subunits, α and β, which are synthesized and colocalized in the same cells of the adenohypophysis. The cellular and transcriptional activities of hagfish GPHα and -β were significantly correlated with the developmental stages of the gonad. The purified native GPH induced the release of gonadal sex steroids in vitro. From our phylogenetic analysis, we propose that ancestral glycoprotein α-subunit 2 (GPA2) and β-subunit 5 (GPB5) gave rise to GPHα and GPHβ of the vertebrate glycoprotein Hormone Family, respectively. The identified hagfish GPHα and -β subunits appear to be the typical gnathostome GPHα and -β subunits based on the sequence and phylogenetic analyses. We hypothesize that the identity of a single functional GPH of the hagfish, hagfish GTH, provides critical evidence for the existence of a pituitary-gonadal system in the earliest divergent vertebrate that likely evolved from an ancestral, prevertebrate exclusively neuroendocrine mechanism by gradual emergence of a previously undescribed control level, the pituitary, which is not found in the Protochordates.
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a systematic immunohistochemical survey of the distribution patterns of gh prolactin somatolactin β tsh β fsh β lh acth and α msh in the adenohypophysis of oreochromis niloticus the nile tilapia
Cell and Tissue Research, 2006Co-Authors: Romano Silvio Kasper, Akiyoshi Takahashi, Natallia Shved, Manfred Reinecke, Elisabeth EpplerAbstract:Fish pituitary plays a central role in the control of growth, development, reproduction and adaptation to the environment. Several types of Hormone-secreting adenohypophyseal cells have been characterised and localised in diverse teleost species. The results suggest a similar distribution pattern among the species investigated. However, most studies deal with a single Hormone or Hormone Family. Thus, we studied adjacent sections of the pituitary of Oreochromis niloticus, the tilapia, by conventional staining and immunohistochemistry with specific antisera directed against growth Hormone (GH), prolactin (PRL), somatolactin (SL), thyrotropin (beta-TSH), follicle-stimulating Hormone (beta-FSH), luteinising Hormone (beta-LH), adrenocorticotropic Hormone (ACTH) and melanocyte-stimulating Hormone (alpha-MSH). The pituitary was characterised by a close interdigitating neighbourhood of neurohypophysis (PN) and adenohypophysis. PRL-immunoreactive and ACTH-immunoreactive cells were detected in the rostral pars distalis. GH-immunoreactive cells were present in the proximal pars distalis (PPD). A small region of the PPD contained beta-TSH-immunoreactive cells, and beta-LH-immunoreactive cells covered approximately the remaining parts. Centrally, beta-FSH-immunoreactive cells were detected in the vicinity of the GH-containing cells. Some of these cells also displayed beta-LH immunoreactivity. The pars intermedia was characterised by branches of the PN surrounded by SL-containing and alpha-MSH-immunoreactive cells. The ACTH and alpha-MSH antisera were observed to cross-react with the respective antigens. This cross-reactivity was abolished by pre-absorption. We present a complete map of the distinct localisation sites for the classical pituitary Hormones, thereby providing a solid basis for future research on teleost pituitary.
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identification of growth Hormone in the sea lamprey an extant representative of a group of the most ancient vertebrates
Endocrinology, 2002Co-Authors: Hiroshi Kawauchi, Shunsuke Moriyama, Masumi Nozaki, Akiyoshi Takahashi, Kunimasa Suzuki, Tomohide Yamazaki, Kiyoko Yamaguchi, John H Youson, Stacia A SowerAbstract:GH was identified in the sea lamprey, an extant representative of a group of the most ancient vertebrates, the Agnatha. A putative GH-cDNA was cloned from the pituitary by RTPCR. The entire coding region comprised an open-reading frame of 203 amino acids (aa). The mature protein was also isolated from pituitaries, and fractionated by gel filtration and reverse-phase HPLC. A putative GH was monitored by Western blotting with a rabbit antiserum against a synthetic peptide corresponding to pre-GH sequence (aa 29 – 45). Sequence analysis of the purified protein demonstrated that the preHormone consists of a signal peptide of 22 aa and the mature protein of 181 aa, which shows 25% sequence identity with sturgeon GH. The site of production was identified through immunohistochemistry to be cells of the dorsal half of the proximal pars distalis of the pituitary. Following cDNA cloning of lamprey IGF cDNA, it was shown using RT-PCR that lamprey GH stimulates IGF expression in lamprey liver. This is the first study in which a member of the GH/prolactin/ somatolactin Family has been identified in an agnathan. In addition, GH appears to be the only member of this Hormone Family in the sea lamprey. Evidence suggests that GH is the ancestral Hormone in the molecular evolution of the GH Family and that the endocrine mechanism for growth stimulation was established at an early stage of vertebrate evolution. (Endocrinology 143: 4916 – 4921, 2002)
C. Salmon - One of the best experts on this subject based on the ideXlab platform.
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Phylogenetic Analysis of the Vertebrate Glycoprotein Hormone Family Including New Sequences of Sturgeon (Acipenser baeri) b Subunits of the Two Gonadotropins
2016Co-Authors: The Thyroid-stimulating Hormone, Abdellah Sellouk, C. SalmonAbstract:The b subunits of the two gonadotropins (GTH1 and GTH2) and of the thyroid-stimulating Hormone (TSH) of a chondrostean fish, Acipenser baeri, were cloned. These new sequences and selected representative members of b subunits of vertebrate gly-coprotein Hormones, including tetrapod follicle-stimulating hor-mones (FSH) and luteinizing Hormones (LH), allowed us to infer the phylogenetic relationships within this Family. Both distance matrix and maximum parsimony methods were used on both nucleotide and amino acid sequences, with bootstrapping eval-uation over 1000 replicates. The four trees obtained had highly similar topologies. In each case, three monophylogenetic line-ages, TSH, GTH1-FSH, and GTH2-LH were clearly identified. The three monophylogenetic lineages were supported by 21–23 specific characters at the amino acid level, out of a total of 121 characters. The resolved topologies within each monophyletic Hormone cluster were congruent with the known phylogenetic relationships between the related species. The inferred parental relationships within gonadotropins are in agreement with data concerning their biological functions. The present study dem-onstrates that GTH1 and GTH2 are the actinopterygian homo-logues of tetrapod FSH and LH, respectively. anterior pituitary, FSH, LH, pituitary, TS
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Phylogenetic Analysis of the Vertebrate Glycoprotein Hormone Family Including New Sequences of Sturgeon (Acipenser baeri) β Subunits of the Two Gonadotropins and the Thyroid-Stimulating Hormone
Biology of reproduction, 2000Co-Authors: Bruno Quérat, Abdellah Sellouk, C. SalmonAbstract:Abstract The β subunits of the two gonadotropins (GTH1 and GTH2) and of the thyroid-stimulating Hormone (TSH) of a chondrostean fish, Acipenser baeri, were cloned. These new sequences and selected representative members of β subunits of vertebrate glycoprotein Hormones, including tetrapod follicle-stimulating Hormones (FSH) and luteinizing Hormones (LH), allowed us to infer the phylogenetic relationships within this Family. Both distance matrix and maximum parsimony methods were used on both nucleotide and amino acid sequences, with bootstrapping evaluation over 1000 replicates. The four trees obtained had highly similar topologies. In each case, three monophylogenetic lineages, TSH, GTH1-FSH, and GTH2-LH were clearly identified. The three monophylogenetic lineages were supported by 21–23 specific characters at the amino acid level, out of a total of 121 characters. The resolved topologies within each monophyletic Hormone cluster were congruent with the known phylogenetic relationships between the related...
Elisabeth Eppler - One of the best experts on this subject based on the ideXlab platform.
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a systematic immunohistochemical survey of the distribution patterns of gh prolactin somatolactin β tsh β fsh β lh acth and α msh in the adenohypophysis of oreochromis niloticus the nile tilapia
Cell and Tissue Research, 2006Co-Authors: Romano Silvio Kasper, Akiyoshi Takahashi, Natallia Shved, Manfred Reinecke, Elisabeth EpplerAbstract:Fish pituitary plays a central role in the control of growth, development, reproduction and adaptation to the environment. Several types of Hormone-secreting adenohypophyseal cells have been characterised and localised in diverse teleost species. The results suggest a similar distribution pattern among the species investigated. However, most studies deal with a single Hormone or Hormone Family. Thus, we studied adjacent sections of the pituitary of Oreochromis niloticus, the tilapia, by conventional staining and immunohistochemistry with specific antisera directed against growth Hormone (GH), prolactin (PRL), somatolactin (SL), thyrotropin (beta-TSH), follicle-stimulating Hormone (beta-FSH), luteinising Hormone (beta-LH), adrenocorticotropic Hormone (ACTH) and melanocyte-stimulating Hormone (alpha-MSH). The pituitary was characterised by a close interdigitating neighbourhood of neurohypophysis (PN) and adenohypophysis. PRL-immunoreactive and ACTH-immunoreactive cells were detected in the rostral pars distalis. GH-immunoreactive cells were present in the proximal pars distalis (PPD). A small region of the PPD contained beta-TSH-immunoreactive cells, and beta-LH-immunoreactive cells covered approximately the remaining parts. Centrally, beta-FSH-immunoreactive cells were detected in the vicinity of the GH-containing cells. Some of these cells also displayed beta-LH immunoreactivity. The pars intermedia was characterised by branches of the PN surrounded by SL-containing and alpha-MSH-immunoreactive cells. The ACTH and alpha-MSH antisera were observed to cross-react with the respective antigens. This cross-reactivity was abolished by pre-absorption. We present a complete map of the distinct localisation sites for the classical pituitary Hormones, thereby providing a solid basis for future research on teleost pituitary.