Preparation of Recombinant Gilthead Seabream (Sparus aurata) Growth Hormone and Its Use for Stimulation of Larvae Growth by Oral Administration

Ben‐Atia, Isashar; Fine, Mira; Tandler, A.; Funkenstein, Bruria; Maurice, Sarah; Cavari, Benzion; Gertler, Arieh

doi:10.1006/gcen.1998.7192

Cited by 39 publications

(20 citation statements)

References 42 publications

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“…The IC 50 value from the competitive binding assay was 3.06 nM, comparable to the value of ϳ2 nM reported for other fish GHs, such as that of gilthead sea bream GH (15,45). The K a calculated from the homologous experiment in which both the ligand and the receptor originated from dolphin fish was 0.77 nM Ϫ1 .…”

Section: Biological Activity In Vitro and In Vivosupporting

confidence: 61%

“…This latter method does not provide information on whether the purified hormone exists as a monomer or as a mixture of monomers, noncovalent dimers, or oligomers that cannot be identified by SDS-PAGE (11). In contrast, the reports from our laboratory regarding the preparation of three, to date prepared, fish GHs (12)(13)(14)(15) or other proteins (11,16 -22) are always accompanied by a determination of monomer content using a sensitive gel-filtration method. In many cases (12,13,16 -20), we have shown that only the monomers are biologically active despite the other forms' apparent purity on an SDS-polyacrylamide gel or their ability to interact with antibodies.…”

mentioning

confidence: 74%

“…Another problem that may hamper the application of GH therapy is a lack of homologous hormones. Although heterologous GHs or related hormones, such as ruminant placental lactogen, have been found to be active in vivo (13,15,(25)(26)(27)(28)(29)(30)(31), their prolonged use may be problematic, as it may elicit an undesired immunological response. Therefore, preparation of homologous GH seems to be quite important.…”

mentioning

confidence: 99%

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Preparation and Characterization of Recombinant Dolphin Fish (Coryphaena hippurus) Growth Hormone

Chapnik-Cohen

Gertler

Elizur

1999

Protein Expression and Purification

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Section: Biological Activity In Vitro and In Vivosupporting

confidence: 61%

mentioning

confidence: 74%

mentioning

confidence: 99%

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Preparation and Characterization of Recombinant Dolphin Fish (Coryphaena hippurus) Growth Hormone

Chapnik-Cohen

Gertler

Elizur

1999

Protein Expression and Purification

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“…In gilthead sea bream, the presence of specific GH-bindings sites at 5 dah (Martí-Palanca and Pérez-Sánchez 1994) and the increase of body weight following oral administration of GH suggest a growth-promoting effect of GH during early development (Ben-Atia et al 1999). As a support of the key role of GHRs in muscle and bone development, Fuentes et al (2008) reported the presence of GHR-I mRNA in Chilean flounder larvae (Paralichthys adspersus) at 8 dah in somites and head and at 9.5 dah in almost the whole larvae including brain, intestines, eyes, somites and the notochord.…”

Section: Nutritional Regulation Of the Gh-igf Axismentioning

confidence: 97%

Regulation of somatic growth and gene expression of the GH–IGF system and PRP-PACAP by dietary lipid level in early juveniles of a teleost fish, the pejerrey (Odontesthes bonariensis)

2012

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Growth and mRNA levels of the pituitary adenylate cyclase-activating polypeptide (PACAP) and its related peptide (PRP), and the system controlled by the growth hormone (GH) and insulin-like growth factors (IGFs) were analyzed in pejerrey fry fed with graded levels of dietary lipids: 10% (L10), 13% (L13) and 21% (L21). First, the full sequence of pejerrey PRP-PACAP was obtained by RT-PCR, using primers based on conserved fragments of teleosts PACAP sequences. The growth of the fish at 83 days after hatching (dah) and the GH mRNA levels were not significantly affected by the dietary treatment. Conversely, PRP-PACAP expression significantly decreased with increasing dietary lipids (L10 > L21). While GH receptor (GHR)-I and IGF-I transcripts did not differ among groups, GHR-II transcripts decreased in group L21. IGF-II expression apparently followed the same trend. These results in combination with the lower expression of the anorexigenic PRP-PACAP in fish fed diet L21 and the correlation analysis evidencing a particularly fine tuning of the GH-IGF system in group L13, suggest that this diet may cover the energy demands for growing pejerrey from 27 dah onwards. Our results show for first time in fish a differential response of PRP-PACAP transcripts to dietary manipulations, and confirm the sensitivity of the pejerrey GH-IGF system to changes in diet composition despite the lack of (or in advance to) a clear response of somatic growth.

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“…GH, together with prolactin, placental, lactogen and somatolactin, form a family of polypeptide hormones with similar structure and biological characteristics (Chen et al 1994). In fish farming industry, GH is often used as a potential growth promoting agent (Cavri et al 1993;McLean et al 1993;Ben-Atia et al 2000). IGF-I, which was firstly described by Rinderknecht and Humbel (1978), also plays a key role in the growth axis (Reineck et al 2005).…”

Section: Introductionmentioning

confidence: 97%

Growth hormone and two forms of insulin-like growth factors I in the giant grouper (Epinephelus lanceolatus): molecular cloning and characterization of tissue distribution

Dong

Zeng

Duan

et al. 2008

Fish Physiol Biochem

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Growth hormone and insulin-like growth factors play important roles in the growth, development and metabolism of vertebrates. In this study, we used reverse transcription and rapid amplification of cDNA ends (RACE) to obtain the three full-length cDNA sequences encoding GH and two forms of IGF-I from the giant grouper (Epinephelus lanceolatus), a coral fish of high commercial value cultured in Southeast Asia. GH precursor cDNA consists of 938 bp in size with an open-reading frame (ORF) encoding 204 amino acid (aa), a 65 bp 5'-untranslated region and a 236 bp 3'-untranslated region. The sequence of giant grouper GH shared 98.6% nucleotide sequence homology with orange-spotted grouper (E. coioides) GH. Two forms of IGF-I precursor cDNA were cloned from giant grouper, IGF-I a consisting of 159 aa, and IGF-I b with 186 aa. They shared 98.4 and 98.7% aa identity with IGF-I reported in the orange-spotted grouper, respectively. Giant grouper IGF-I a and b have the same signal peptide and B-C-A-D domains, but they are different in the E domain. Using real-time reverse transcription PCR strategy, tissue distribution profile showed that GH and IGF-I mRNA signals were all observed in pituitary, brain, liver, ovary and spleen. GH mRNA in pituitary was the most abundant, and IGF-I mRNA level in liver was found to be more abundant than that in other selected tissues. These findings will contribute to the understanding of the evolution of GH and IGF-I, and provide some basic information about the characterization of GH and IGF-I in the giant grouper.

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Preparation of Recombinant Gilthead Seabream (Sparus aurata) Growth Hormone and Its Use for Stimulation of Larvae Growth by Oral Administration

Cited by 39 publications

References 42 publications

Preparation and Characterization of Recombinant Dolphin Fish (Coryphaena hippurus) Growth Hormone

Preparation and Characterization of Recombinant Dolphin Fish (Coryphaena hippurus) Growth Hormone

Regulation of somatic growth and gene expression of the GH–IGF system and PRP-PACAP by dietary lipid level in early juveniles of a teleost fish, the pejerrey (Odontesthes bonariensis)

Growth hormone and two forms of insulin-like growth factors I in the giant grouper (Epinephelus lanceolatus): molecular cloning and characterization of tissue distribution

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