Unique alternative translation from two open reading frames on Acpin1 mRNA yields an acrosomal protein and a salivary-gland-specific protein

Int J Urol. 2009 Jul;16(7):639-46. doi: 10.1111/j.1442-2042.2009.02325.x.

Abstract

Objective: To examine the expression profiles of the proteins translated from Acpin1 mRNA in germ cells.

Methods: Northern and western blotting of various tissues and immunohistochemical analysis of germ cells were carried out in a mouse model.

Results: ACPIN1 protein was transcribed from the longer, 3' open reading frame (ORF) of Acpin1. An alternative-splicing variant, Acpin1vs, contained only the smaller, 5' ORF of the full-length Acpin1 gene. Its gene product, SAGSIN1, was expressed specifically in salivary glands. Retrotransposed regions of Acpin1 homology were also detected in various chromosomes, and intronless paralogous genes on the X chromosome were expressed in the testis and other tissues. The genomic structure of Acpin1 is highly conserved in mammals.

Conclusion: The two ORFs on the Acpin1 mRNA are independently translated in differentiated cells. Analysis of gene Acpin1 might clarify the molecular mechanism of spermatogenesis.

MeSH terms

  • Acrosome / physiology*
  • Adaptor Proteins, Signal Transducing
  • Alternative Splicing / genetics
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Northern
  • Blotting, Western
  • DNA, Complementary / genetics
  • Male
  • Mice
  • Molecular Sequence Data
  • Nuclear Proteins
  • Open Reading Frames / genetics
  • Protein Biosynthesis / genetics*
  • Proteins / genetics*
  • Proteins / metabolism
  • RNA, Messenger / genetics
  • Salivary Glands / physiology*
  • Spermatogenesis / genetics

Substances

  • Adaptor Proteins, Signal Transducing
  • DNA, Complementary
  • Fam220a protein, mouse
  • Nuclear Proteins
  • Proteins
  • RNA, Messenger