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Related Experiment Videos

[Primary structure of human protein pS2].

M C Rio1, P Lepage, P Diemunsch

  • 1Laboratoire de Génétique moléculaire des Eucaryotes du C.N.R.S., Strasbourg.

Comptes Rendus De L'Academie Des Sciences. Serie III, Sciences De La Vie
|January 1, 1988
PubMed
Summary

Researchers purified and sequenced the pS2 protein from both breast cancer cells (MCF-7) and normal stomach mucosa. The pS2 protein sequences were identical, confirming gene expression in distinct human tissues.

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Area of Science:

  • Molecular Biology
  • Protein Chemistry
  • Gastroenterology

Background:

  • pS2 mRNA is expressed in hormone-dependent breast carcinoma cells (MCF-7) and normal human stomach mucosa.
  • The mRNA encodes a putative 84 amino-acid protein secreted after signal peptide removal.

Purpose of the Study:

  • To purify and characterize the pS2 protein secreted by MCF-7 cells and normal gastric mucosa.
  • To confirm the identity and sequence of the pS2 protein in both cell types.

Main Methods:

  • Purification of the pS2 protein from cell secretions.
  • Trypsin digestion of the purified pS2 protein.
  • Amino-acid sequencing of the resulting peptides.

Main Results:

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  • The secreted pS2 protein from MCF-7 cells is 60 amino acids long, matching the mRNA sequence.
  • The N-terminal glutamic acid indicates a 24 amino-acid signal peptide.
  • Gastric pS2 protein shares identical signal peptide and initial 48 amino acids with MCF-7 pS2 protein, with potential N-terminal pyroglutamic acid cyclization.

    • Conclusions:

    • The pS2 protein sequence is conserved between breast cancer cells and normal gastric mucosa.
    • Confirms the expression and secretion of a structurally identical pS2 protein in distinct human tissues.