| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
* Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan; and
Tsukuba Research Institute, Novartis Pharma, Tsukuba, Japan
Extravasation of peripheral blood monocytes through vascular basement membranes requires degradation of extracellular matrix components including heparan sulfate proteoglycans (HSPGs). Heparanase, the heparan sulfate-specific endo-
-glucuronidase, has previously been shown to be a key enzyme in melanoma invasion, yet its involvement in monocyte extravasation has not been elucidated. We examined a potential regulatory mechanism of heparanase in HSPG degradation and transmigration through basement membranes in leukocyte trafficking using human promonocytic leukemia U937 and THP-1 cells. PMA-treated cells were shown to degrade 35S-sulfated HSPG in endothelial extracellular matrix into fragments of an approximate molecular mass of 5 kDa. This was not found with untreated cells. The gene expression levels of heparanase or the enzyme activity of the amount of cell lysates were no different between untreated and treated cells. Immunocytochemical staining with anti-heparanase mAb revealed pericellular distribution of heparanase in PMA-treated cells but not in untreated cells. Cell surface heparanase capped into a restricted area on PMA-treated cells when they were allowed to adhere. Addition of a chemoattractant fMLP induced polarization of the PMA-treated cells and heparanase redistribution at the leading edge of migration. Therefore a major regulatory process of heparanase activity in the cells seems to be surface expression and capping of the enzyme. Addition of the anti-heparanase Ab significantly inhibited enzymatic activity and transmigration of the PMA-treated cells, suggesting that the cell surface redistribution of heparanase is involved in monocyte extravasation through basement membranes.
This article has been cited by other articles:
|
|
 |
|
  A. Eudes, G. Mouille, J. Thevenin, A. Goyallon, Z. Minic, and L. Jouanin Purification, Cloning and Functional Characterization of an Endogenous beta-Glucuronidase in Arabidopsis thaliana Plant Cell Physiol., September 1, 2008; 49(9): 1331 - 1341. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. J. Wood and M. D. Hulett Cell Surface-expressed Cation-independent Mannose 6-Phosphate Receptor (CD222) Binds Enzymatically Active Heparanase Independently of Mannose 6-Phosphate to Promote Extracellular Matrix Degradation J. Biol. Chem., February 15, 2008; 283(7): 4165 - 4176. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. M. de Mestre, M. A. Staykova, J. R. Hornby, D. O. Willenborg, and M. D. Hulett Expression of the heparan sulfate-degrading enzyme heparanase is induced in infiltrating CD4+ T cells in experimental autoimmune encephalomyelitis and regulated at the level of transcription by early growth response gene1 J. Leukoc. Biol., November 1, 2007; 82(5): 1289 - 1300. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Benhamron, H. Nechushtan, I. Verbovetski, A. Krispin, G. Abboud-Jarrous, E. Zcharia, E. Edovitsky, E. Nahari, T. Peretz, I. Vlodavsky, et al. Translocation of Active Heparanase to Cell Surface Regulates Degradation of Extracellular Matrix Heparan Sulfate upon Transmigration of Mature Monocyte-Derived Dendritic Cells. J. Immunol., June 1, 2006; 176(11): 6417 - 6424. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
