Purification and Initial Functions of Sex-Specific Storage Protein 2 in Bombyx mori

Protein J. 2015 Aug;34(4):256-66. doi: 10.1007/s10930-015-9619-9.

Abstract

In this study, we identified a heat-resistant protein from the chrysalis stage of the silkworm which we named sex-specific storage protein 2 (SSP2). This protein was stable even at 80 °C, and has an amino acid sequence that is 90.65 % homologous to SP2. We utilized the heat-resistant characteristics of SSP2 to purify the protein and maintain its biological activity. In addition, using flow cytometry and the MTT assay, we found that SSP2 had anti-apoptotic effects on BmN cells, and that SSP2 could also inhibit cell apoptosis induced by chemical factors. These results suggest that SSP2 has a cell-protective function, and provides a basis for future work on the function of storage proteins in silkworm.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis / drug effects
  • Bombyx / chemistry*
  • Cell Line
  • Cell Survival / drug effects
  • Hot Temperature
  • Insect Proteins / chemistry*
  • Insect Proteins / isolation & purification*
  • Insect Proteins / pharmacology
  • Molecular Sequence Data
  • Protein Stability
  • Pupa / chemistry*
  • Sequence Alignment

Substances

  • Insect Proteins