Production and characterization of recombinant vitellogenesis-inhibiting hormone from the American lobster Homarus americanus.
Recombinant peptides related to vitellogenesis-inhibiting hormone (VIH) of the American lobster Homarus americanus were expressed in bacterial cells, and then purified after being allowed to refold. Biological activities of the recombinant VIHs having an amidated C-terminus (rHoa-VIH-amide) and a free carboxyl-terminus (rHoa-VIH-OH) were examined using an ovarian fragment incubation system derived from the kuruma prawn, Marsupenaeus japonicus. The rHoa-VIH-amide significantly reduced vitellogenin mRNA levels in the ovary, while rHoa-VIH-OH had no effect. This is the first report that describes the production of a crustacean VIH having biological activity and the importance of the C-terminal amidation for its vitellogenesis-inhibiting activity.
Ohira
Tsuyoshi
T
Japan International Research Center for Agricultural Sciences, Tsukuba, Ibaraki 305-8686, Japan.
Okumura
Takuji
T
Suzuki
Michio
M
Yajima
Yosuke
Y
Tsutsui
Naoaki
N
Wilder
Marcy N
MN
Nagasawa
Hiromichi
H
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D005260:Female; D007447:Invertebrate Hormones / Q000737:chemistry* / Q000378:metabolism; D008297:Male; D008666:Metalloendopeptidases / Q000378:metabolism; D008969:Molecular Sequence Data; D008121:Nephropidae; D010053:Ovary / Q000378:metabolism; D010957:Plasmids / Q000378:metabolism; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry*
D002352:Carrier Proteins; D007447:Invertebrate Hormones; D011994:Recombinant Proteins; C073189:vitellogenesis inhibiting hormone; D008666:Metalloendopeptidases; C058921:endoproteinase Asp-N