scholarly journals Deaminated neuraminic acid-rich glycoprotein of rainbow trout egg vitelline envelope. Occurrence of a novel alpha-2,8-linked oligo(deaminated neuraminic acid) structure in O-linked glycan chains.

1990 ◽  
Vol 265 (35) ◽  
pp. 21811-21819 ◽  
Author(s):  
A Kanamori ◽  
S Inoue ◽  
M Iwasaki ◽  
K Kitajima ◽  
G Kawai ◽  
...  
1992 ◽  
Vol 135 (2) ◽  
pp. 303-NP ◽  
Author(s):  
S. J. Hyllner ◽  
C. Haux

ABSTRACT The major vitelline envelope proteins were detected in the plasma of female rainbow trout maturing under natural conditions by using the Western blot technique. Females were sampled every month from July until ovulation in January. The amount of vitelline envelope proteins in plasma increased markedly as the gonads increased in size from 0·4 to about 15% of the total body weight. The plasma level of oestradiol-17β largely followed the alterations in the amount of vitelline envelope proteins, indicating the endocrine control of vitelline envelope protein synthesis. In addition, plasma vitellogenin changed in a manner that resembled the changes in the amount of plasma vitelline envelope proteins. The appearance and growth of the vitelline envelope during oocyte development was demonstrated using immunohistochemical methods. The vitelline envelopes from oocytes at different stages of development were immunoreactive with the antibodies directed against the major vitelline envelope proteins. No immunoreactivity could be observed in the ooplasm or in the surrounding follicular cells, which indicated that the major vitelline envelope proteins were of extraovarian origin. The present study further supports the hypothesis that the major protein constituents of the vitelline envelope in teleosts are under the endocrine control of oestradiol17β and that the site of synthesis is outside the ovary. Journal of Endocrinology (1992) 135, 303–309


2015 ◽  
Vol 27 (3) ◽  
pp. 504 ◽  
Author(s):  
Joanna Nynca ◽  
Georg J. Arnold ◽  
Thomas Fröhlich ◽  
Andrzej Ciereszko

In the present study we used a shotgun proteomic approach to identify 54 proteins of rainbow trout ovarian fluid. The study has unravelled the identity of several proteins not previously reported in fish ovarian fluid. The proteome of trout ovarian fluid consists of diverse proteins participating in lipid binding and metabolism, carbohydrate and ion transport, innate immunity, maturation and ovulation processes. Most trout ovarian fluid proteins correspond to follicular fluid proteins of higher vertebrates, but 15% of the proteins were found to be different, such as those related to the immune system (precerebellin-like protein), proteolysis (myeloid cell lineage chitinase), carbohydrate and lipid binding and metabolism (vitellogenins), cell structure and shape (vitelline envelope protein gamma) and a protein with unknown functions (UPF0762 protein C6orf58 homologue). The present study could help in the decoding of the biological function of these proteins and in the discovery of potential biomarkers of oocyte quality.


Biochemistry ◽  
1993 ◽  
Vol 32 (35) ◽  
pp. 9221-9229 ◽  
Author(s):  
Yu Song ◽  
Ken Kitajima ◽  
Sadako Inoue ◽  
Yutaka Muto ◽  
Takeshi Kasama ◽  
...  

1991 ◽  
Vol 131 (2) ◽  
pp. 229-236 ◽  
Author(s):  
S. J. Hyllner ◽  
D. O. Oppen-Berntsen ◽  
J. V. Helvik ◽  
B. T. Walther ◽  
C. Haux

ABSTRACT During growth of the ovarian follicle, the teleost oocyte becomes surrounded by an acellular coat, the vitelline envelope. The nature, origin and number of the vitelline envelope proteins in fish appear to vary with species. In this work, polyclonal antibodies directed against vitelline envelope proteins from rainbow trout, brown trout and turbot were used to show that oestradiol-17β induces the major vitelline envelope proteins in juveniles, both males and females, from different species. The fact that males can synthesize vitelline envelope constituents shows that the origin of these proteins is not confined to the ovary. The vitelline envelope of rainbow trout eggs consists of three major proteins, designated α (60 kDa), β (55 kDa) and γ (50 kDa). The amino acid composition of each of the three proteins indicated that the three proteins are alike and the suggestion that these proteins represent a separate class of structural proteins is sustained. Journal of Endocrinology (1991) 131, 229–236


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