Expression of an active proteinase inhibitor, α1-antichymotrypsin, by human breast epithelial cells

Sandra J. Gendler, Zoltán A. Tökés

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


The synthesis of an active proteinase inhibitor, gp 66, by human breast epithelial cells is reported. This glycoprotein is identical to serum α1-antichymotrypsin, which inhibits proteinases that cleave at hydrophobic residues. Immunohistological studies show the in vivo expression on normal secretory and ductal epithelial cells and on primary and metastatic adenocarcinomas. Immunoaffinity-purified gp 66 from MCF-7 culture supernatants is an active inhibitor of chymotrypsin as determined in a fluorogenic enzyme assay and can form stable 88 kDa enzyme-inhibitor complexes. The synthesis of a functional inhibitor may represent the epithelial cell's attempt to stabilize its extracellular milieu.

Original languageEnglish (US)
Pages (from-to)242-253
Number of pages12
JournalBBA - General Subjects
Issue number2
StatePublished - Jun 19 1986


  • Breast
  • Breast adenocarcinoma
  • Epithelial cell
  • Mammary tissue
  • Proteinase inhibitor
  • α-Antichymotrypsin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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