PUBLICATION

Sex- and tissue-specific expression of aspartic proteinases in Danio rerio (zebrafish)

Authors
Riggio, M., Scudiero, R., Filosa, S., and Parisi, E.
ID
ZDB-PUB-010130-4
Date
2000
Source
Gene   260(1-2): 67-75 (Journal)
Registered Authors
Parisi, Elio
Keywords
cathepsin D; evolution; gene expression; nothepsin
MeSH Terms
  • Amino Acid Sequence
  • Animals
  • Aspartic Acid Endopeptidases/genetics*
  • Base Sequence
  • Blotting, Northern
  • Cathepsin D/genetics
  • DNA, Complementary/chemistry
  • DNA, Complementary/genetics
  • Female
  • Gene Expression Regulation, Enzymologic
  • Male
  • Molecular Sequence Data
  • Phylogeny
  • RNA/genetics
  • RNA/metabolism
  • Sequence Analysis, DNA
  • Sex Factors
  • Tissue Distribution
  • Zebrafish/genetics*
PubMed
11137292 Full text @ Gene
Abstract
Full-length zebrafish cDNAs encoding two aspartic proteinases were cloned and sequenced. One of the two cDNAs was a 1708bp product with an open reading frame of 398 amino acid residues corresponding to a cathepsin D. The other was a 1383bp 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.
Genes / Markers
Figures
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Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping