Human breast milk contains procathepsin D - Detection by specific antibodies

V. Vetvicka, J. Vagner, M. Baudys, J. Tang, S. I. Foundling, M. Fusek

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


The presence of the zymogen of cathepsin D in human milk was detected using antibodies specific for the proenzyme and by the proteolytic activity at low pH. The antibodies were raised against a synthetic propetide of human cathepsin D and were tested using immunoprecipitations and western blots of samples from different breast cancer cell lines as well as cytosol fractions of human breast cancer tissues. In all experiments these antibodies recognized specifically procathepsin D. Procathepsin D from human milk was partially activated at low pH. The activity was monitored using hemoglobin 14C proteolytic assay, and it was abolished by pepstatin A - a specific inhibitor of aspartic proteinases. Western blots did not reveal presence of cathepsin B or cathepsin H. These data indicate specific secretion of cathepsin D in human breast milk.

Original languageEnglish (US)
Pages (from-to)921-928
Number of pages8
JournalBiochemistry and Molecular Biology International
Issue number5
StatePublished - 1993

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics


Dive into the research topics of 'Human breast milk contains procathepsin D - Detection by specific antibodies'. Together they form a unique fingerprint.

Cite this