Ovary Of Scallop Research Articles

Pectenovarin, A New Ovarian Carotenoprotein from Japanese Scallop Mizuhopecten yessoensis.

The scallop Mizuhopecten yessoensis accumulates carotenoids in the ovary during the maturation stage. Its conspicuous pink color implies the presence of carotenoprotein. However, the carotenoprotein from the scallop ovary has never been isolated and characterized, probably due to its instability and complexity. Here, we developed an extraction and isolation procedure for the carotenoprotein by employing a basic buffer containing potassium bromide to facilitate its efficient extraction from the ovary, and we succeeded in obtaining the carotenoprotein, termed pectenovarin. The carotenoid composition of the pectenovarin was similar to that of the ovary. The N-terminal and internal amino acid sequences of pectenovarin showed a high similarity to those of vitellogenin, the precursor of egg yolk protein under analysis.

Oxidative Stability of Lipids Rich in EPA and DHA Extracted from Fermented Scallop Ovary

A novel seafood paste was developed by the fermentation of scallop ovary using rice malt (koji) and yeast culture. Chemical analysis of the product showed the formation of high level of free amino acids and organic acids during the fermentation. The product color and flavor resembled to Japanese traditional soybean miso. The contents of total lipids (TLs) extracted from the fermented products were ranged from 9.18% to 11.59% or 11.38% to 13.57%/dry sample weight. Although the TL was rich in oxidatively unstable polyunsaturated fatty acids (PUFAs) such as eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), little decrease was found in these PUFAs during the fermentation, showing the high oxidative stability of the TL from the fermented scallop ovary. Moreover, the oxidative stability of the TL extracted from the fermented products increased with increasing the fermentation time. This would be mainly due to the formation of lipid soluble antioxidants such as tocopherols, which might be derived from yeast used for fermentation.

A novel oocyte maturation arresting factor in the central nervous system of scallops inhibits serotonin-induced oocyte maturation and spawning of bivalve mollusks

Serotonin (5-hydroxytriptamine; 5-HT) is a major neurotransmitter that triggers oocyte maturation and sequential spawning in bivalve mollusks. A proteinous and heat-labile substance that proved to be a novel inhibitor of 5-HT-induced egg release from ovarian tissue was found in the cerebral and pedal ganglia (CPG) of the scallop Patinopecten yessoensis. The same inhibitory activity was also observed in the proteinous fraction from the supernatant of hemolymph. Histological observation demonstrated that the novel inhibitor prevented 5-HT from inducing oocyte maturation in the scallop ovary and that no prostaglandin F 2α (PGF 2α) inhibited 5-HT-induced oocyte maturation, although PGF 2α strongly prohibited 5-HT-induced egg release through the gonoduct from ovarian tissue. The novel inhibitor from the scallop CPG also prohibited 5-HT-induced oocyte maturation of other bivalve species as well as scallops. The novel inhibitor, mediated through a receptor mechanism on oocyte membranes, blocked extracellular Ca 2+ uptake into oocytes, which was observed in 5-HT-induced oocyte maturation. It is suggested that the novel inhibitor with a molecular mass of 60 kDa, named oocyte maturation arresting factor, which appears to be a universal substance for bivalve species, may be transported from the CPG to the ovary via hemolymph and may prohibit 5-HT-induced oocyte maturation due to the interference of extracellular Ca 2+ influx into oocytes, eventually resulting in the inhibition of spawning. On the other hand, it seems that PGF 2α inhibits 5-HT-induced transport of mature eggs through the gonoduct.

Molecular cloning and expression analysis of vitellogenin in scallop, Patinopecten yessoensis (Bivalvia, Mollusca).

The present study was undertaken to determine scallop vitellogenin (Vtg) cDNA sequence, to identify Vtg synthesizing cell, and to analyze the regulation of Vtg mRNA expression. Clones containing partial cDNA sequence of Vtg were isolated from cDNA library of the scallop ovary by immunoscreening with the anti-scallop vitellin (Vn) serum. The deduced amino acid sequence of the clone containing the longest cDNA insert (1,689 bp) was identified as a member of the lipid transport protein family and exhibited about 20-35% identity with Vtgs of other oviparous animals. Northern blot analysis identified a single transcript longer than 10 kb in the ovary. Dot blot analysis of the ovary showed a high amount of Vtg mRNA during the growing stage and the level was retained until spawning stage. In situ hybridization demonstrated the expression of Vtg mRNA in the auxiliary cells closely associated with growing oocytes, suggesting that the synthesis of a major yolk protein in the scallop occurs through hetero-synthetic pathway without mediation through the blood flow but occurs de novo in the ovary. The content of Vtg mRNA in the ovarian tissue cultured in vitro with vitellogenesis promoting factor (VPF), which strongly promotes Vtg protein synthesis, from the cerebral plus pedal ganglion (CPG) showed no change. The transcription of Vtg mRNA appeared to be promoted by estradiol-17beta (E2) not by VPF although VPF may enhance the translation of Vtg mRNA.

Identification and characterization of a novel calcineurin-binding protein in scallop testis.

Calcineurin has been inferred to function in meiosis and spermiogenesis in testis. Here, we identified a calcineurin-binding protein in scallop testis by Far-Western blot analysis using purified calcineurin as a probe. The molecular mass of the binding protein estimated on the blot was 75 kDa. The isolated cDNA clone encoded a novel 474-residue protein, named CaNBP75. The region between T6 and A210 of CaNBP75 was responsible for the interaction with calcineurin. CaNBP75 was predominantly expressed in testis and ovary of scallop. Thus, CaNBP75 may modulate the physiological function of calcineurin in the testis and ovary of scallop, such as in spermiogenesis or meiosis.

Gonadal Estrogen Profile and Immunohistochemical Localization of Steroidogenic Enzymes in the Oyster and Scallop during Sexual Maturation

Estrogen levels in the gonads of marine bivalves, the Pacific oyster Crassostrea gigas and scallop Patinopecten yessoensis were determined by high performance liquid chromatography (HPLC) using an electrochemical detector. Estrone (E1), estradiol-17β (E2), and a small amount of estriol (E3) were identified in the ovary, while only E2 was found in the testis. The level of E2 in the ovary was consistently higher than E1 and it increased with sexual maturation. These results indicate that E2 may play a role in the reproductive events of the oyster and scallop. In vitro experiments demonstrated the presence of 17β-hydroxysteroid dehydrogenase (17β-HSD) in the ovaries of both bivalves. The activity of 17β-HSD in the ovary was lower in the postspawning stage than in the early differentiating stage. The evidence for the presence of aromatase activity in the scallop ovary was obtained by 3H-water assay. The immunoreactivity against 3β-hydroxysteroid dehydrogenase (3β-HSD), P450 aromatase and E2 was detected in the cells along the outside of germinal acini of the scallop ovary. It is concluded that estrogens can be synthesized in the gonad, that their levels vary with the reproductive cycle, and that they have a role in the development of gametes.

Purification and Characterization of a Yolk Protein from the Scallop Ovary.

Purification and Characterization of a Yolk Protein from the Scallop Ovary.