Calreticulin is present in the acrosome of spermatids of rat testis

Biochem Biophys Res Commun. 1992 Jul 31;186(2):668-73. doi: 10.1016/0006-291x(92)90798-p.

Abstract

We have already succeeded in purifying a calcium-binding protein (CalBP) from rat spermatogenic cells [Nakamura et al., Biochem. Biophys. Res. Commun., 176 (1991) 1358]. In this study, the location of this protein within rat testis was examined, using a rabbit antisera for this protein. The antigen was localized on the developing acrosomes during spermiogenesis. The NH2-terminal amino acid sequence obtained for rat CalBP was identical to that of calreticulin obtained for the skeletal muscle of mice and closely resembled that for rabbit calreticulin. On the immunoblot analysis, the purified rat CalBP reacted with an antibody raised against rabbit skeletal muscle calreticulin. The results indicate that calreticulin is present in the acrosome of spermatids of rat testes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acrosome / chemistry
  • Acrosome / ultrastructure*
  • Amino Acid Sequence
  • Animals
  • Calcium-Binding Proteins / analysis*
  • Calcium-Binding Proteins / chemistry
  • Calreticulin
  • Electrophoresis, Polyacrylamide Gel
  • Fluorescent Antibody Technique
  • Immunoblotting
  • Male
  • Mice
  • Molecular Sequence Data
  • Molecular Weight
  • Rabbits
  • Rats
  • Rats, Inbred Strains
  • Sequence Homology, Nucleic Acid
  • Spermatids / chemistry
  • Spermatids / cytology*
  • Testis / chemistry
  • Testis / cytology*

Substances

  • Calcium-Binding Proteins
  • Calreticulin