Deduced primary structure of vitellogenin in the giant freshwater prawn, Macrobrachium rosenbergii, and yolk processing during ovarian maturation

Atsuro Okuno, Wei J. Yang, Vidya Jayasankar, Hisako Saido-Sakanaka, D. T T Huong, Safiah Jasmani, Muharijadi Atmomarsono, Thanumalayaperumal Subramoniam, Naoaki Tsutsui, Tsuyoshi Ohira, Ichiro Kawazoe, Katsumi Aida, Marcy N. Wilder

Research output: Contribution to journalArticle

74 Citations (Scopus)

Abstract

A cDNA encoding vitellogenin (Vg) in the giant freshwater prawn, Macrobrachium rosenbergii, was cloned based on the cDNA sequence of vitellin (Vn) fragments A-N and B-42 determined previously, and its amino acid sequence deduced. The open reading frame (ORF) encoded 2,537 amino acid residues and its deduced amino acid sequence possessed three consensus cleavage sites, R-X-R-R, similar to those reported in Vgs of insects. The deduced primary structure of Vg in M. rosenbergii was seen to be similar to that of Penaeus japonicus, especially in the N-terminal region. It is therefore likely that Vgs in crustacean species including prawns and other related decapods exhibit a similar structural pattern. Based on the deduced primary structure of Vg and analysis of the various Vg and Vn subunits found in the hemolymph and ovary during ovarian maturation, we demonstrated the post-translational processing of Vg in M. rosenbergii. This is the first time that Vg processing has been clearly demonstrated in a crustacean species. Vg, after being synthesized in the hepatopancreas, is considered to be cleaved by a subtilisin-like endoprotease to form two subunits, A and proB, which are then released into the hemolymph. In the hemolymph, proB is possibly cleaved by a processing enzyme of unknown identity to give rise to subunits B and C/D. The three processed subunits A, B, and C/D are sequestered by the ovary to give rise to three yolk proteins, Macr-VnA, VnB, and VnC/D.

Original languageEnglish
Pages (from-to)417-429
Number of pages13
JournalJournal of Experimental Zoology
Volume292
Issue number5
DOIs
Publication statusPublished - Apr 1 2002
Externally publishedYes

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Macrobrachium rosenbergii
vitellogenin
vitellin
hemolymph
amino acid sequences
Crustacea
Marsupenaeus japonicus
yolk proteins
subtilisin
hepatopancreas
Decapoda
open reading frames
shrimp
insects
amino acids
enzymes

ASJC Scopus subject areas

  • Animal Science and Zoology

Cite this

Deduced primary structure of vitellogenin in the giant freshwater prawn, Macrobrachium rosenbergii, and yolk processing during ovarian maturation. / Okuno, Atsuro; Yang, Wei J.; Jayasankar, Vidya; Saido-Sakanaka, Hisako; Huong, D. T T; Jasmani, Safiah; Atmomarsono, Muharijadi; Subramoniam, Thanumalayaperumal; Tsutsui, Naoaki; Ohira, Tsuyoshi; Kawazoe, Ichiro; Aida, Katsumi; Wilder, Marcy N.

In: Journal of Experimental Zoology, Vol. 292, No. 5, 01.04.2002, p. 417-429.

Research output: Contribution to journalArticle

Okuno, A, Yang, WJ, Jayasankar, V, Saido-Sakanaka, H, Huong, DTT, Jasmani, S, Atmomarsono, M, Subramoniam, T, Tsutsui, N, Ohira, T, Kawazoe, I, Aida, K & Wilder, MN 2002, 'Deduced primary structure of vitellogenin in the giant freshwater prawn, Macrobrachium rosenbergii, and yolk processing during ovarian maturation', Journal of Experimental Zoology, vol. 292, no. 5, pp. 417-429. https://doi.org/10.1002/jez.10083
Okuno, Atsuro ; Yang, Wei J. ; Jayasankar, Vidya ; Saido-Sakanaka, Hisako ; Huong, D. T T ; Jasmani, Safiah ; Atmomarsono, Muharijadi ; Subramoniam, Thanumalayaperumal ; Tsutsui, Naoaki ; Ohira, Tsuyoshi ; Kawazoe, Ichiro ; Aida, Katsumi ; Wilder, Marcy N. / Deduced primary structure of vitellogenin in the giant freshwater prawn, Macrobrachium rosenbergii, and yolk processing during ovarian maturation. In: Journal of Experimental Zoology. 2002 ; Vol. 292, No. 5. pp. 417-429.
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abstract = "A cDNA encoding vitellogenin (Vg) in the giant freshwater prawn, Macrobrachium rosenbergii, was cloned based on the cDNA sequence of vitellin (Vn) fragments A-N and B-42 determined previously, and its amino acid sequence deduced. The open reading frame (ORF) encoded 2,537 amino acid residues and its deduced amino acid sequence possessed three consensus cleavage sites, R-X-R-R, similar to those reported in Vgs of insects. The deduced primary structure of Vg in M. rosenbergii was seen to be similar to that of Penaeus japonicus, especially in the N-terminal region. It is therefore likely that Vgs in crustacean species including prawns and other related decapods exhibit a similar structural pattern. Based on the deduced primary structure of Vg and analysis of the various Vg and Vn subunits found in the hemolymph and ovary during ovarian maturation, we demonstrated the post-translational processing of Vg in M. rosenbergii. This is the first time that Vg processing has been clearly demonstrated in a crustacean species. Vg, after being synthesized in the hepatopancreas, is considered to be cleaved by a subtilisin-like endoprotease to form two subunits, A and proB, which are then released into the hemolymph. In the hemolymph, proB is possibly cleaved by a processing enzyme of unknown identity to give rise to subunits B and C/D. The three processed subunits A, B, and C/D are sequestered by the ovary to give rise to three yolk proteins, Macr-VnA, VnB, and VnC/D.",
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T1 - Deduced primary structure of vitellogenin in the giant freshwater prawn, Macrobrachium rosenbergii, and yolk processing during ovarian maturation

AU - Okuno, Atsuro

AU - Yang, Wei J.

AU - Jayasankar, Vidya

AU - Saido-Sakanaka, Hisako

AU - Huong, D. T T

AU - Jasmani, Safiah

AU - Atmomarsono, Muharijadi

AU - Subramoniam, Thanumalayaperumal

AU - Tsutsui, Naoaki

AU - Ohira, Tsuyoshi

AU - Kawazoe, Ichiro

AU - Aida, Katsumi

AU - Wilder, Marcy N.

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N2 - A cDNA encoding vitellogenin (Vg) in the giant freshwater prawn, Macrobrachium rosenbergii, was cloned based on the cDNA sequence of vitellin (Vn) fragments A-N and B-42 determined previously, and its amino acid sequence deduced. The open reading frame (ORF) encoded 2,537 amino acid residues and its deduced amino acid sequence possessed three consensus cleavage sites, R-X-R-R, similar to those reported in Vgs of insects. The deduced primary structure of Vg in M. rosenbergii was seen to be similar to that of Penaeus japonicus, especially in the N-terminal region. It is therefore likely that Vgs in crustacean species including prawns and other related decapods exhibit a similar structural pattern. Based on the deduced primary structure of Vg and analysis of the various Vg and Vn subunits found in the hemolymph and ovary during ovarian maturation, we demonstrated the post-translational processing of Vg in M. rosenbergii. This is the first time that Vg processing has been clearly demonstrated in a crustacean species. Vg, after being synthesized in the hepatopancreas, is considered to be cleaved by a subtilisin-like endoprotease to form two subunits, A and proB, which are then released into the hemolymph. In the hemolymph, proB is possibly cleaved by a processing enzyme of unknown identity to give rise to subunits B and C/D. The three processed subunits A, B, and C/D are sequestered by the ovary to give rise to three yolk proteins, Macr-VnA, VnB, and VnC/D.

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