Immunofluorescent localization of cathepsins B and D in human fibroblastsJS Mort, AR Poole and RS Decker
The proteinase cathepsin B has been localized in human fibroblasts using a monospecific antiserum that reacts in a precipitating manner with the denatured enzyme only. The distribution of staining as revealed by both direct and indirect immunofluorescence indicates a typical lysosomal localization similar to that observed for cathepsin D. Using dual localization methods employing fluorescein- and tetramethylrhodamine-labeled affinity purified antibodies both proteinases were usually observed in the same lysosome, indicating a combined role in intracellular digestion.
Volume 29,
Issue 5,
pp. 649-657,
05/01/1981
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F. Authier, M. Metioui, S. Fabrega, M. Kouach, and G. Briand Endosomal Proteolysis of Internalized Insulin at the C-terminal Region of the B Chain by Cathepsin D J. Biol. Chem., March 8, 2002; 277(11): 9437 - 9446. [Abstract] [Full Text] [PDF] |
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S. Gruenheid, E. Pinner, M. Desjardins, and P. Gros Natural Resistance to Infection with Intracellular Pathogens: The Nramp1 Protein Is Recruited to the Membrane of the Phagosome J. Exp. Med., February 17, 1997; 185(4): 717 - 730. [Abstract] [Full Text] [PDF] |
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C. Illy, O. Quraishi, J. Wang, E. Purisima, T. Vernet, and JohnS. Mort Role of the Occluding Loop in Cathepsin B Activity J. Biol. Chem., January 10, 1997; 272(2): 1197 - 1202. [Abstract] [Full Text] [PDF] |
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