Abstract
The determine the site of vitellin (Vn) synthesis in the blue crab, Callinectes sapidus, tissues (ovary, hepatopancreas, and gill) from adult female crabs were incubated in vitro with [35S]methionine. Tissue extracts were separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and radiolabeled proteins were visualized by autoradiography: Four radiolabeled ovarian proteins (188, 168, 109, and 86 kDa) comigrated with the subunits of Vn. A Western blot analysis confirmed that these ovarian proteins were the Vn subunits. Proteins in the hepatopancreas and gill were also radiolabeled but were not Vn‐immunoreactive. In vitro incorporation of [35S] methionine into ovarian proteins was inhibited by an extract of eyestalks; the inhibition was dose‐dependent and specific. Autoradiography of the electrophoretically separated ovarian proteins revealed that the eyestalk extract inhibited incorporation of [35S] methionine into numerous proteins, including the Vn subunits. These results suggest that the ovary is a site of Vn synthesis and that the eyestalks contain a factor or factors that directly inhibit the synthesis of Vn and other ovarian proteins. It is anticipated that the suppression of ovarian protein synthesis will be a useful bioassay for blue crab vitellogenesis‐inhibiting hormone. © 1995 Wiley‐Liss, Inc.
Original language | English |
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Pages (from-to) | 364-372 |
Number of pages | 9 |
Journal | Journal of Experimental Zoology |
Volume | 271 |
Issue number | 5 |
DOIs | |
Publication status | Published - 1995 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Animal Science and Zoology
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In vitro study of vitellogenesis in the blue crab (Callinectes sapidus) : Site and control of vitellin synthesis. / Lee, Chi-Ying; Watson, R. Douglas.
In: Journal of Experimental Zoology, Vol. 271, No. 5, 01.01.1995, p. 364-372.Research output: Contribution to journal › Article
TY - JOUR
T1 - In vitro study of vitellogenesis in the blue crab (Callinectes sapidus)
T2 - Site and control of vitellin synthesis
AU - Lee, Chi-Ying
AU - Watson, R. Douglas
PY - 1995/1/1
Y1 - 1995/1/1
N2 - The determine the site of vitellin (Vn) synthesis in the blue crab, Callinectes sapidus, tissues (ovary, hepatopancreas, and gill) from adult female crabs were incubated in vitro with [35S]methionine. Tissue extracts were separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and radiolabeled proteins were visualized by autoradiography: Four radiolabeled ovarian proteins (188, 168, 109, and 86 kDa) comigrated with the subunits of Vn. A Western blot analysis confirmed that these ovarian proteins were the Vn subunits. Proteins in the hepatopancreas and gill were also radiolabeled but were not Vn‐immunoreactive. In vitro incorporation of [35S] methionine into ovarian proteins was inhibited by an extract of eyestalks; the inhibition was dose‐dependent and specific. Autoradiography of the electrophoretically separated ovarian proteins revealed that the eyestalk extract inhibited incorporation of [35S] methionine into numerous proteins, including the Vn subunits. These results suggest that the ovary is a site of Vn synthesis and that the eyestalks contain a factor or factors that directly inhibit the synthesis of Vn and other ovarian proteins. It is anticipated that the suppression of ovarian protein synthesis will be a useful bioassay for blue crab vitellogenesis‐inhibiting hormone. © 1995 Wiley‐Liss, Inc.
AB - The determine the site of vitellin (Vn) synthesis in the blue crab, Callinectes sapidus, tissues (ovary, hepatopancreas, and gill) from adult female crabs were incubated in vitro with [35S]methionine. Tissue extracts were separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and radiolabeled proteins were visualized by autoradiography: Four radiolabeled ovarian proteins (188, 168, 109, and 86 kDa) comigrated with the subunits of Vn. A Western blot analysis confirmed that these ovarian proteins were the Vn subunits. Proteins in the hepatopancreas and gill were also radiolabeled but were not Vn‐immunoreactive. In vitro incorporation of [35S] methionine into ovarian proteins was inhibited by an extract of eyestalks; the inhibition was dose‐dependent and specific. Autoradiography of the electrophoretically separated ovarian proteins revealed that the eyestalk extract inhibited incorporation of [35S] methionine into numerous proteins, including the Vn subunits. These results suggest that the ovary is a site of Vn synthesis and that the eyestalks contain a factor or factors that directly inhibit the synthesis of Vn and other ovarian proteins. It is anticipated that the suppression of ovarian protein synthesis will be a useful bioassay for blue crab vitellogenesis‐inhibiting hormone. © 1995 Wiley‐Liss, Inc.
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U2 - 10.1002/jez.1402710506
DO - 10.1002/jez.1402710506
M3 - Article
AN - SCOPUS:84985135313
VL - 271
SP - 364
EP - 372
JO - Journal of Experimental Zoology
JF - Journal of Experimental Zoology
SN - 1548-8969
IS - 5
ER -