The major excreted protein of transformed fibroblasts is an activable acid-protease.
Open Access
- 1 February 1986
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 261 (4) , 1760-1765
- https://doi.org/10.1016/s0021-9258(17)36004-0
Abstract
No abstract availableThis publication has 41 references indexed in Scilit:
- Amino acid sequence of human liver cathepsin BFEBS Letters, 1985
- Processing and lysosomal localization of a glycoprotein whose secretion is transformation stimulated.The Journal of cell biology, 1985
- Biosynthesis of lysosomal hydrolases: their synthesis in bound polysomes and the role of co- and post-translational processing in determining their subcellular distributionThe Journal of cell biology, 1982
- Cathepsinogen D: characterization and activation to cathepsin D and inhibitory peptidesFEBS Letters, 1981
- Stimulation of the release of two glycoproteins from mouse 3T3 cells by growth factors and by agents that increase intralysosomal pHBiochemical and Biophysical Research Communications, 1981
- Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling.The Journal of cell biology, 1980
- Fibronectins—adhesive glycoproteins of cell surface and bloodNature, 1978
- AN ENZYMATIC FUNCTION ASSOCIATED WITH TRANSFORMATION OF FIBROBLASTS BY ONCOGENIC VIRUSESThe Journal of Experimental Medicine, 1973
- Fluorescamine: A Reagent for Assay of Amino Acids, Peptides, Proteins, and Primary Amines in the Picomole RangeScience, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970