Sex- and tissue-specific expression of aspartic proteinases in Danio rerio (zebrafish).
Full-length zebrafish cDNAs encoding two aspartic proteinases were cloned and sequenced. One of the two cDNAs was a 1708 bp product with an open reading frame of 398 amino acid residues corresponding to a cathepsin D. The other was a 1383 bp product encoding a polypeptide chain of 416 amino acids homologous to nothepsin, an aspartic proteinase first identified by us in the liver of Antarctic Notothenioidei. Gene expression assessed by RT-PCR and northern blot hybridization of RNA from different tissues showed that the expression was tissue- and sex-specific. Whereas the cathepsin D gene was expressed in all the tissues examined independently of the sex, the nothepsin gene was expressed exclusively in female livers.
Riggio
M
M
Dipartimento di Biologia Evolutiva e Comparata, Università Federico II, Naples, Italy.
Scudiero
R
R
Filosa
S
S
Parisi
E
E
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000235:genetics*; D001483:Base Sequence; D015152:Blotting, Northern; D002402:Cathepsin D / Q000235:genetics; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D005260:Female; D015971:Gene Expression Regulation, Enzymologic; D008297:Male; D008969:Molecular Sequence Data; D010802:Phylogeny; D012313:RNA / Q000235:genetics / Q000378:metabolism; D017422:Sequence Analysis, DNA; D012737:Sex Factors; D014018:Tissue Distribution; D015027:Zebrafish / Q000235:genetics*
D018076:DNA, Complementary; D012313:RNA; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D