| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Fondation Curie, Institut du Radium, Bâtiment 111, 91405-Orsay, France
It has been demonstrated that solid hepatoma lysosomes lack hyaluronidase activity, whereas normal rat liver lysosomes contain a high level of this enzyme. This result was also found with lysosomes from an ascites hepatoma, Walker carcinoma 256, and virally transformed BHK cells.
In contrast, ß-N-acetylglucosaminidase activity was shown to be present in lysosomes from tumor cells, although its level was decreased by about 75%, compared with that of controls. As it is known that hyaluronidase and ß-N-acetylglucosaminidase activities are increased in the extracellular space of tumors, we suggest that the lack of hyaluronidase and the important decrease of ß-N-acetylglucosaminidase in tumor lysosomes are due to a perturbation of the control of enzyme distribution from the Golgi apparatus to the lysosomes and the extracellular space.
1 Supported in part by a grant from the Lady Tate Memorial Trust (London, England).
Received 11/ 5/71. Accepted 2/15/73.
This article has been cited by other articles:
![]() |
V. B. Lokeshwar, M. J. Young, G. Goudarzi, N. Iida, A. I. Yudin, G. N. Cherr, and M. G. Selzer Identification of Bladder Tumor-derived Hyaluronidase: Its Similarity to HYAL1 Cancer Res., September 1, 1999; 59(17): 4464 - 4470. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Cancer Research | Clinical Cancer Research |
| Cancer Epidemiology Biomarkers & Prevention | Molecular Cancer Therapeutics |
| Molecular Cancer Research | Cancer Prevention Research |
| Cancer Prevention Journals Portal | Cancer Reviews Online |
| Annual Meeting Education Book | Meeting Abstracts Online |