An alpha-1-acid glycoprotein-like protein as a major component of the ovarian cavity fluid of viviparous fish, Neoditrema ransonnetii (Perciformes, Embiotocidae)

Comp Biochem Physiol A Mol Integr Physiol. 2009 Jun;153(2):222-9. doi: 10.1016/j.cbpa.2009.02.018. Epub 2009 Feb 24.

Abstract

Developing fetuses of surfperch (Neoditrema ransonnetii, Perciformes; Embiotocidae) are retained in the ovarian cavity until birth, where they are surrounded by ovarian cavity fluid (OCF). Expecting the OCF to have key roles in maintaining pregnancy, we purified and characterized a major glycoprotein of 51 kDa in the OCF of surfperch. On the basis of the N-terminal amino acid sequence, we cloned and sequenced a full-length cDNA. The deduced sequence comprises 214 amino acids (aa) including a signal peptide of 20 aa and a mature protein of 194 aa. This protein had an extremely low pI (below 2.8) and extraordinarily high glycosylation rate (more than 50%), characteristics being shared with alpha-1-acid glycoprotein (AGP), a member of the lipocalin superfamily. A homology search and phylogenetic analysis indicated that the 51 kDa protein and tributyltin-binding protein found in Japanese flounder are the closest known relatives of AGP. We therefore named the protein nrF-AGP. Messenger RNA of nrF-AGP was expressed intensively in the liver, but not at all in the ovarian tissue. Because nrF-AGP is the most salient component in OCF but not in plasma, we reasoned that it was selectively sequestered from blood to the ovarian cavity in pregnant females, and consequently, plays crucial roles in pregnancy.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Body Fluids / metabolism*
  • Electrophoresis, Gel, Two-Dimensional
  • Female
  • Molecular Sequence Data
  • Orosomucoid / isolation & purification*
  • Orosomucoid / metabolism
  • Ovary / metabolism*
  • Perciformes / physiology*
  • Phylogeny
  • RNA, Messenger / genetics
  • Sequence Alignment
  • Sequence Analysis, Protein
  • Species Specificity
  • Viviparity, Nonmammalian / physiology*

Substances

  • Orosomucoid
  • RNA, Messenger