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Hyperglycaemic Hormones Inhibit Protein and mRNA Synthesis in in Vitro -Incubated Ovarian Fragments of the Marine Shrimp Penaeus semisulcatus

Identifieur interne : 001076 ( Istex/Corpus ); précédent : 001075; suivant : 001077

Hyperglycaemic Hormones Inhibit Protein and mRNA Synthesis in in Vitro -Incubated Ovarian Fragments of the Marine Shrimp Penaeus semisulcatus

Auteurs : M. Khayat ; W.-J. Yang ; K. Aida ; H. Nagasawa ; A. Tietz ; B. Funkenstein ; E. Lubzens

Source :

RBID : ISTEX:69DA17B7940554A91CE7F58F6CFB6010D0260A27

Abstract

The present work shows for the first time that peptides belonging to the Crustacean hyperglycaemic hormone family (CHH-family hormones) fromPenaeus japonicusaffect protein and mRNA synthesis inin vitro-incubated ovarian explant fragments removed from vitellogenic females ofPenaeus semisulcatus.Reduced levels of protein synthesis, determined by TCA-precipitable35S-labeled proteins, were found in the presence of crude sinus gland extracts from bothP. semisulcatusandP. japonicus.A similar inhibitory effect compared to controls was found with each of the seven CHH-family peptides. Non-CHH-family peptides did not reduce protein synthesis. Crude sinus gland extracts prepared fromP. semisulcatuswere at least 20-fold more effective than sinus gland extracts ofP. japonicus.The inhibition level was directly related to the concentration of the peptide in the incubation media, but its degree varied among the different tested peptides. The profile of proteins synthesized duringin vitroincubation was analyzed using polyacrylamide gel electrophoresis under denatured and reduced conditions (SDS-PAGE), followed by autoradiography. Synthesis of several proteins was reduced, including proteins with electrophoretic mobility similar to that of vitellin. Immunoprecipitation with antiserum prepared against native ovarian vitellin confirmed the inhibitory effect of CHH-family peptides on vitellin synthesis. The crude sinus gland extract and CHH-family peptides also inhibited RNA synthesis, as determined by [3H]uridine incorporation into mRNA of ovarian fragments. It is concluded that in addition to their role in carbohydrate metabolism, CHH-family peptides may also influence ovarian physiology in crustaceans.

Url:
DOI: 10.1006/gcen.1998.7078

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ISTEX:69DA17B7940554A91CE7F58F6CFB6010D0260A27

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<ce:surname>Lubzens</ce:surname>
<ce:cross-ref refid="GC987078A2">
<ce:sup>b</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:affiliation id="GC987078A1">
<ce:label>a</ce:label>
<ce:textfn>Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv, 69978, Israel</ce:textfn>
</ce:affiliation>
<ce:affiliation id="GC987078A2">
<ce:label>b</ce:label>
<ce:textfn>Israel Oceanographic and Limnological Research, Tel-Shikmona, P.O.B. 8030, Haifa, 31080, Israel</ce:textfn>
</ce:affiliation>
<ce:affiliation id="GC987078A3">
<ce:label>c</ce:label>
<ce:textfn>Department of Aquatic Bioscience, The University of Tokyo, Bunkyo-ku, Tokyo, 113, Japan</ce:textfn>
</ce:affiliation>
<ce:affiliation id="GC987078A4">
<ce:label>d</ce:label>
<ce:textfn>Department of Applied Biological Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo, 113, Japan</ce:textfn>
</ce:affiliation>
</ce:author-group>
<ce:date-accepted day="6" month="2" year="1998"></ce:date-accepted>
<ce:abstract>
<ce:section-title>Abstract</ce:section-title>
<ce:abstract-sec>
<ce:simple-para>The present work shows for the first time that peptides belonging to the Crustacean hyperglycaemic hormone family (CHH-family hormones) from
<ce:italic>Penaeus japonicus</ce:italic>
affect protein and mRNA synthesis in
<ce:italic>in vitro</ce:italic>
-incubated ovarian explant fragments removed from vitellogenic females of
<ce:italic>Penaeus semisulcatus.</ce:italic>
Reduced levels of protein synthesis, determined by TCA-precipitable
<ce:sup>35</ce:sup>
S-labeled proteins, were found in the presence of crude sinus gland extracts from both
<ce:italic>P. semisulcatus</ce:italic>
and
<ce:italic>P. japonicus.</ce:italic>
A similar inhibitory effect compared to controls was found with each of the seven CHH-family peptides. Non-CHH-family peptides did not reduce protein synthesis. Crude sinus gland extracts prepared from
<ce:italic>P. semisulcatus</ce:italic>
were at least 20-fold more effective than sinus gland extracts of
<ce:italic>P. japonicus.</ce:italic>
The inhibition level was directly related to the concentration of the peptide in the incubation media, but its degree varied among the different tested peptides. The profile of proteins synthesized during
<ce:italic>in vitro</ce:italic>
incubation was analyzed using polyacrylamide gel electrophoresis under denatured and reduced conditions (SDS-PAGE), followed by autoradiography. Synthesis of several proteins was reduced, including proteins with electrophoretic mobility similar to that of vitellin. Immunoprecipitation with antiserum prepared against native ovarian vitellin confirmed the inhibitory effect of CHH-family peptides on vitellin synthesis. The crude sinus gland extract and CHH-family peptides also inhibited RNA synthesis, as determined by [
<ce:sup>3</ce:sup>
H]uridine incorporation into mRNA of ovarian fragments. It is concluded that in addition to their role in carbohydrate metabolism, CHH-family peptides may also influence ovarian physiology in crustaceans.</ce:simple-para>
</ce:abstract-sec>
</ce:abstract>
</head>
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<title>Hyperglycaemic Hormones Inhibit Protein and mRNA Synthesis in in Vitro -Incubated Ovarian Fragments of the Marine Shrimp Penaeus semisulcatus</title>
</titleInfo>
<titleInfo type="alternative" lang="en" contentType="CDATA">
<title>Hyperglycaemic Hormones Inhibit Protein and mRNA Synthesis in</title>
</titleInfo>
<name type="personal">
<namePart type="given">M.</namePart>
<namePart type="family">Khayat</namePart>
<affiliation>Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv, 69978, Israel</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">W.-J.</namePart>
<namePart type="family">Yang</namePart>
<affiliation>Department of Aquatic Bioscience, The University of Tokyo, Bunkyo-ku, Tokyo, 113, Japan</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">K.</namePart>
<namePart type="family">Aida</namePart>
<affiliation>Department of Aquatic Bioscience, The University of Tokyo, Bunkyo-ku, Tokyo, 113, Japan</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">H.</namePart>
<namePart type="family">Nagasawa</namePart>
<affiliation>Department of Applied Biological Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo, 113, Japan</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">A.</namePart>
<namePart type="family">Tietz</namePart>
<affiliation>Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv, 69978, Israel</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">B.</namePart>
<namePart type="family">Funkenstein</namePart>
<affiliation>Israel Oceanographic and Limnological Research, Tel-Shikmona, P.O.B. 8030, Haifa, 31080, Israel</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">E.</namePart>
<namePart type="family">Lubzens</namePart>
<affiliation>Israel Oceanographic and Limnological Research, Tel-Shikmona, P.O.B. 8030, Haifa, 31080, Israel</affiliation>
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<dateIssued encoding="w3cdtf">1998</dateIssued>
<copyrightDate encoding="w3cdtf">1998</copyrightDate>
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<languageTerm type="code" authority="iso639-2b">eng</languageTerm>
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<abstract lang="en">The present work shows for the first time that peptides belonging to the Crustacean hyperglycaemic hormone family (CHH-family hormones) fromPenaeus japonicusaffect protein and mRNA synthesis inin vitro-incubated ovarian explant fragments removed from vitellogenic females ofPenaeus semisulcatus.Reduced levels of protein synthesis, determined by TCA-precipitable35S-labeled proteins, were found in the presence of crude sinus gland extracts from bothP. semisulcatusandP. japonicus.A similar inhibitory effect compared to controls was found with each of the seven CHH-family peptides. Non-CHH-family peptides did not reduce protein synthesis. Crude sinus gland extracts prepared fromP. semisulcatuswere at least 20-fold more effective than sinus gland extracts ofP. japonicus.The inhibition level was directly related to the concentration of the peptide in the incubation media, but its degree varied among the different tested peptides. The profile of proteins synthesized duringin vitroincubation was analyzed using polyacrylamide gel electrophoresis under denatured and reduced conditions (SDS-PAGE), followed by autoradiography. Synthesis of several proteins was reduced, including proteins with electrophoretic mobility similar to that of vitellin. Immunoprecipitation with antiserum prepared against native ovarian vitellin confirmed the inhibitory effect of CHH-family peptides on vitellin synthesis. The crude sinus gland extract and CHH-family peptides also inhibited RNA synthesis, as determined by [3H]uridine incorporation into mRNA of ovarian fragments. It is concluded that in addition to their role in carbohydrate metabolism, CHH-family peptides may also influence ovarian physiology in crustaceans.</abstract>
<note type="content">Section title: Regular Article</note>
<relatedItem type="host">
<titleInfo>
<title>General and Comparative Endocrinology</title>
</titleInfo>
<titleInfo type="abbreviated">
<title>YGCEN</title>
</titleInfo>
<genre type="journal">journal</genre>
<originInfo>
<dateIssued encoding="w3cdtf">199806</dateIssued>
</originInfo>
<identifier type="ISSN">0016-6480</identifier>
<identifier type="PII">S0016-6480(00)X0045-7</identifier>
<part>
<date>199806</date>
<detail type="volume">
<number>110</number>
<caption>vol.</caption>
</detail>
<detail type="issue">
<number>3</number>
<caption>no.</caption>
</detail>
<extent unit="issue pages">
<start>227</start>
<end>346</end>
</extent>
<extent unit="pages">
<start>307</start>
<end>318</end>
</extent>
</part>
</relatedItem>
<identifier type="istex">69DA17B7940554A91CE7F58F6CFB6010D0260A27</identifier>
<identifier type="DOI">10.1006/gcen.1998.7078</identifier>
<identifier type="PII">S0016-6480(98)97078-2</identifier>
<accessCondition type="use and reproduction" contentType="copyright">©1998 Academic Press</accessCondition>
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<recordOrigin>Academic Press, ©1998</recordOrigin>
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