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Gewählte Publikation:

Mach, L; Mort, JS; Glössl, J.
(1994): Noncovalent complexes between the lysosomal proteinase cathepsin B and its propeptide account for stable, extracellular, high molecular mass forms of the enzyme.
J Biol Chem. 1994; 269(17):13036-13040

Although the lysosomal cysteine proteinase cathepsin B is alkaline pH-labile, active, stable high molecular mass forms have been reported previously from the culture medium of human and murine mammary tumor explants and the sputum of patients with purulent bronchiectasis. A similar, catalytically active, high molecular mass form of recombinant human cathepsin B produced in yeast has now been found to represent a noncovalent complex between the 30-kDa single chain enzyme and its 6-kDa propeptide formed during autocatalytic maturation of the proenzyme (see accompanying article; Mach, L., Mort, J. S., and Glossl, J. (1994) J. Biol. Chem. 269, 13030-13035). Incubation of the complex under acidic conditions resulted in dissociation and degradation of the inhibitory propeptide leading to increased enzymatic activity, as also observed for partially purified cathepsin B isoenzymes from purulent sputum and mammary tumor explant media. The stabilization of the processed proteinase as a noncovalent complex with its proregion provides an important mechanism whereby extracellular cathepsin B can lie dormant until regional acidification mediates its activity.
Autor*innen der BOKU Wien:
Glößl Josef
Mach Lukas
Find related publications in this database (using NML MeSH Indexing)
Amino Acid Sequence -
Breast Neoplasms - enzymology
Cathepsin B - genetics
Culture Media - genetics
Enzyme Precursors - metabolism
Enzyme Stability - metabolism
Humans - metabolism
Hydrogen-Ion Concentration - metabolism
Isoenzymes - genetics
Lysosomes - enzymology
Molecular Sequence Data - enzymology
Molecular Weight - enzymology
Protein Processing, Post-Translational - enzymology
Saccharomyces cerevisiae - genetics
Sputum - enzymology
Tumor Cells, Cultured - enzymology

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