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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/21136
Título

Changes in Cathepsin Gene Expression and Relative Enzymatic Activity During Gilthead Sea Bream Oogenesis

AutorCarnevali, Oliana; Cionna, C.; Tosti, L.; Cerdà, Joan ; Giocchini, G.
Palabras claveLysosomal enzymes
Yolk
Egg
Fecha de publicación30-may-2007
EditorJohn Wiley & Sons
CitaciónMolecular Reproduction & Development 75:97–104 (2008)
ResumenThe aim of this study was to provide evidence on the modulation of lysosomal enzymes in terms of both gene expression and enzymatic activity during follicle maturation. For this purpose three lysosomal enzymes, cathepsins B, D, and L, were studied in relation to yolk formation and degradation, during the main phases of ovarian follicle growth in the pelagophil species, the sea bream Sparus aurata. Specific attention was focused on the gene expression quantification method, on the assay of enzymatic activities, and on the relationship between the proteolytic cleavage of yolk proteins (YPs), cathepsin gene expression and cathepsin activities. For the gene expression study, the cathepsins B-like and L-like mRNAs were isolated and partially or fully characterized, respectively; the sequences were used as design specific primers for the quantification of cathepsin gene expression by real-time PCR, in follicles at different stages of maturation. The enzymatic assays for cathepsins B, D, and L were optimized in terms of specificity, sensitivity and reliability, using specific substrates and inhibitors. In ovulated eggs, the lipovitellin I (LV I) was degraded and the changes in electrophoretic pattern were preceded by an increase in the activity of a cysteine proteinase, cathepsin L, and its mRNA. Cathepsin B did not appear to be involved in YP changes during the final maturation stage.
Descripción8 pages, 4 figures, 3 tables
Versión del editorhttp://dx.doi.org/10.1002/mrd.20768
URIhttp://hdl.handle.net/10261/21136
DOI10.1002/mrd.20768
ISSN1040-452X
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