Changes of lysosomal enzyme activities in sea bass (Dicentrarchus labrax) eggs and developing embryos

被引:67
作者
Carnevali, O
Mosconi, G
Cambi, A
Ridolfi, S
Zanuy, S
Polzonetti-Magni, AM
机构
[1] Univ Ancona, Ist Sci Mare, I-60131 Ancona, Italy
[2] Univ Camerino, Dipartimento Sci Morfol & Biochim Comparate, I-62032 Camerino, MC, Italy
[3] CSIC, Inst Acuicultura Torre Sal, Castellon de La Plana, Spain
关键词
fish embryo; fish cathepsins; pelagic egg spawner; sea bass; Dicentrarchus labrax;
D O I
10.1016/S0044-8486(01)00775-X
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
The sea bass Dicentrarchus labrax is a pelagic egg spawner; sinking eggs are unable to develop into embryos, and this is a limitation in the controlled reproduction of this species. The eggs were divided into good and poor quality, by virtue of their ability to float or sink in seawater. High levels of cathepsins B, D, and L were detected in the eggs, whereas no cathepsin A, C, and E activity was detected. Cathepsin D was found at significantly higher levels in sinking eggs, whereas cathepsin L was more abundant in floating eggs. Since degradation of yolk proteins is essential for the early development of the embryo, the levels of cathepsins A, B, C, D, E, and L were tested in different stages of embryo development. Cathepsin A activity was detectable from the morula stage at which time cathepsin B activity reached its maximal level. Cathepsins A and L reached maximal activity during segmentation, and this corresponded with major changes in the electrophoretic pattern of yolk proteins during embryogenesis suggesting their involvement in yolk protein mobilization at this time. Cathepsin D reached its maximal activity during hatching, (C) 2001 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:249 / 256
页数:8
相关论文
共 25 条
  • [1] BARRETT AJ, 1981, METHOD ENZYMOL, V80, P535
  • [2] Molecular cloning and expression of ovarian cathepsin D in seabream, Sparus aurata
    Carnevali, O
    Centonze, F
    Brooks, S
    Marota, I
    Sumpter, JP
    [J]. BIOLOGY OF REPRODUCTION, 1999, 61 (03) : 785 - 791
  • [3] Carnevali O, 1998, SCI MAR, V62, P311
  • [4] YOLK PROTEIN-CHANGES DURING OOCYTE GROWTH IN EUROPEAN SEA BASS DICENTRARCHUS-LABRAX L
    CARNEVALI, O
    MOSCONI, G
    RONCARATI, A
    BELVEDERE, P
    LIMATOLA, E
    POLZONETTIMAGNI, AM
    [J]. JOURNAL OF APPLIED ICHTHYOLOGY, 1993, 9 (3-4) : 175 - 184
  • [5] Yolk formation and degradation during oocyte maturation in seabream Sparus aurata:: Involvement of two lysosomal proteinases
    Carnevali, O
    Carletta, R
    Cambi, A
    Vita, A
    Bromage, N
    [J]. BIOLOGY OF REPRODUCTION, 1999, 60 (01) : 140 - 146
  • [6] FAGOTTO F, 1995, J CELL SCI, V108, P3645
  • [7] Proteolytic enzymes in yolk-sac membrane of quail egg. Purification and enzymatic characterisation
    Gerhartz, B
    Auerswald, EA
    Mentele, R
    Fritz, H
    Machleidt, W
    Kolb, HJ
    Wittmann, J
    [J]. COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 1997, 118 (01): : 159 - 166
  • [8] EFFECTS OF MICROBIAL PROTEINASE-INHIBITORS ON THE DEGRADATION OF ENDOGENOUS AND INTERNALIZED PROTEINS BY RAT YOLK SACS
    KNOWLES, SE
    BALLARD, FJ
    LIVESEY, G
    WILLIAMS, KE
    [J]. BIOCHEMICAL JOURNAL, 1981, 196 (01) : 41 - 48
  • [9] RELIABILITY OF MOLECULAR-WEIGHT DETERMINATION OF PROTEINS BY POLYACRYLAMIDE GRADIENT GEL-ELECTROPHORESIS IN PRESENCE OF SODIUM DODECYL-SULFATE
    LAMBIN, P
    [J]. ANALYTICAL BIOCHEMISTRY, 1978, 85 (01) : 114 - 125
  • [10] ROLE OF ACID-PHOSPHATASE IN BREAKDOWN OF YOLK PLATELETS IN DEVELOPING AMPHIBIAN EMBRYOS
    LEMANSKI, LF
    ALDOROTY, R
    [J]. JOURNAL OF MORPHOLOGY, 1977, 153 (03) : 419 - 425