Purification and characterization of perchloric acid soluble protein from rat lung

Comp Biochem Physiol B Biochem Mol Biol. 2003 Jun;135(2):255-62. doi: 10.1016/s1096-4959(03)00073-3.

Abstract

We isolated a perchloric acid soluble protein from the post-mitochondria supernatant fraction of the rat lung and designated it as RLu-PSP1. The protein is soluble in 5% perchloric acid and was purified by ammonium sulfate fractionation and CM-Sephadex chromatography. The amino acid sequence of RLu-PSP was identical with that of rat liver PSP (RL-PSP). RLu-PSP inhibited protein synthesis in a rabbit reticulocyte lysate system. It was expressed mainly in cytoplasm of bronchioles and alveolar epithelial cells of the lung from 60-day-old rats. In 15-day-old rat embryos, the epithelial-lining of the terminal buds of the respiratory tree was immunopositive. The expression of RLu-PSP increased from the embryonic 15th day to the postnatal 40th day. This is the first report on the presence of a PSP in rat lung and on its involvement in the regulation of cellular growth and differentiation.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Embryo, Mammalian / chemistry
  • Heat-Shock Proteins / analysis
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism*
  • Liver / cytology
  • Liver / growth & development
  • Liver / metabolism
  • Lung / embryology
  • Lung / growth & development
  • Lung / metabolism*
  • Male
  • Molecular Sequence Data
  • Rabbits
  • Rats
  • Rats, Inbred BB
  • Ribonucleases / analysis
  • Ribonucleases / chemistry
  • Ribonucleases / genetics
  • Ribonucleases / metabolism*
  • Serine Endopeptidases / metabolism

Substances

  • Heat-Shock Proteins
  • Rida protein, rat
  • Ribonucleases
  • Serine Endopeptidases
  • lysyl endopeptidase